| Year |
Citation |
Score |
| 2022 |
Riegert AS, Narindoshvili T, Platzer NE, Raushel FM. Functional Characterization of a HAD Phosphatase Involved in Capsular Polysaccharide Biosynthesis in . Biochemistry. PMID 36214481 DOI: 10.1021/acs.biochem.2c00484 |
0.354 |
|
| 2022 |
Riegert AS, Narindoshvili T, Coricello A, Richards NGJ, Raushel FM. Correction to "Functional Characterization of Two PLP-Dependent Enzymes Involved in Capsular Polysaccharide Biosynthesis from ". Biochemistry. 61: 46. PMID 34928582 DOI: 10.1021/acs.biochem.1c00789 |
0.309 |
|
| 2021 |
Truong DP, Rousseau S, Machala BW, Huddleston JP, Zhu M, Hull KG, Romo D, Raushel FM, Sacchettini JC, Glasner ME. Second-Shell Amino Acid R266 Helps Determine -Succinylamino Acid Racemase Reaction Specificity in Promiscuous -Succinylamino Acid Racemase/-Succinylbenzoate Synthase Enzymes. Biochemistry. PMID 34845903 DOI: 10.1021/acs.biochem.1c00627 |
0.373 |
|
| 2020 |
Xiang DF, Narindoshvili T, Raushel FM. Atropselective Hydrolysis of Chiral Binol-Phosphate Esters Catalyzed by the Phosphotriesterase from sp. TCM1. Biochemistry. PMID 33167613 DOI: 10.1021/acs.biochem.0c00831 |
0.35 |
|
| 2020 |
Bigley AN, Narindoshvili T, Raushel FM. A Chemoenzymatic Synthesis of the ()-Isomer of the Antiviral Prodrug Remdesivir. Biochemistry. PMID 32786401 DOI: 10.1021/Acs.Biochem.0C00591 |
0.318 |
|
| 2020 |
Mabanglo MF, Huddleston JP, Mukherjee K, Taylor ZW, Raushel FM. Structure and Reaction Mechanism of YcjR, an Epimerase that Facilitates the Interconversion of D-Gulosides to D-Glucosides in Escherichia coli. Biochemistry. PMID 32437133 DOI: 10.1021/Acs.Biochem.0C00334 |
0.413 |
|
| 2020 |
Huddleston JP, Anderson TK, Spencer KD, Thoden JB, Raushel FM, Holden HM. Structural Analysis of Cj1427, an Essential NAD-dependent Dehydrogenase for the Biosynthesis of the Heptose Residues in the Capsular Polysaccharides of Campylobacter jejuni. Biochemistry. PMID 32168450 DOI: 10.1021/Acs.Biochem.0C00096 |
0.408 |
|
| 2020 |
Huddleston JP, Raushel FM. Functional Characterization of Cj1427, a Unique Ping-Pong Dehydrogenase Responsible for the Oxidation of GDP-d-α-d--heptose in . Biochemistry. PMID 32168448 DOI: 10.1021/Acs.Biochem.0C00097 |
0.337 |
|
| 2020 |
Bigley AN, Narindoshvili T, Xiang DF, Raushel FM. Stereoselective Formation of Multiple Reaction Products by the Phosphotriesterase from Sphingobium sp. TCM1. Biochemistry. PMID 32167750 DOI: 10.1021/Acs.Biochem.0C00089 |
0.444 |
|
| 2019 |
Huddleston JP, Raushel FM. Biosynthesis of GDP-d--α-d--heptose for the Capsular Polysaccharide of . Biochemistry. PMID 31449400 DOI: 10.1021/Acs.Biochem.9B00548 |
0.34 |
|
| 2019 |
Hogancamp TN, Cory SA, Barondeau DP, Raushel FM. Structure and Chemical Reaction Mechanism of LigU, an Enzyme that Catalyzes an Allylic Isomerization in the Bacterial Degradation of Lignin. Biochemistry. PMID 31339729 DOI: 10.1021/Acs.Biochem.9B00549 |
0.479 |
|
| 2019 |
Huddleston JP, Thoden JB, Dopkins BJ, Narindoshvili T, Fose BJ, Holden HM, Raushel FM. Structural and Functional Characterization of YdjI, an Aldolase of Unknown Specificity in Escherichia coli K12. Biochemistry. PMID 31322866 DOI: 10.1021/Acs.Biochem.9B00326 |
0.403 |
|
| 2019 |
Huddleston JP, Raushel FM. Functional Characterization of YdjH, a Sugar Kinase of Unknown Specificity in K12. Biochemistry. PMID 31314509 DOI: 10.1021/Acs.Biochem.9B00327 |
0.343 |
|
| 2019 |
Xiang DF, Bigely AN, Desormeaux E, Narindoshvili T, Raushel FM. Enzyme-Catalyzed Kinetic Resolution of Chiral Precursors to Antiviral Prodrugs. Biochemistry. PMID 31268686 DOI: 10.1021/Acs.Biochem.9B00530 |
0.45 |
|
| 2019 |
Bigley AN, Raushel FM. The evolution of phosphotriesterase for decontamination and detoxification of organophosphorus chemical warfare agents. Chemico-Biological Interactions. 308: 80-88. PMID 31100274 DOI: 10.1016/J.Cbi.2019.05.023 |
0.374 |
|
| 2019 |
Raushel FM, Taylor ZW. Manganese-Induced Substrate Promiscuity in the Reaction Catalyzed by Phosphoglutamine Cytidylyltransferase from Campylobacter jejuni. Biochemistry. PMID 30929435 DOI: 10.1021/Acs.Biochem.9B00189 |
0.442 |
|
| 2019 |
Bigely AN, Desormeaux E, Xiang DF, Bae SY, Harvey SP, Raushel FM. Overcoming the Challenges of Enzyme Evolution to Adapt Phosphotriesterase for V-agent Decontamination. Biochemistry. PMID 30893549 DOI: 10.1021/Acs.Biochem.9B00097 |
0.404 |
|
| 2019 |
Mukherjee KW, Huddleston J, Narindoshvili T, Nemmara V, Raushel FM. Functional Characterization of the ycjQRS Gene Cluster from Escherichia coli: A Novel Pathway for the Transformation of D-Gulosides to D-Glucosides. Biochemistry. PMID 30742415 DOI: 10.1021/Acs.Biochem.8B01278 |
0.328 |
|
| 2019 |
Bigley AN, Xiang DF, Narindoshvili T, Burgert CW, Hengge AC, Raushel FM. Transition State Analysis of the Reaction Catalyzed by the Phosphotriesterase from Sphingobium sp. TCM1. Biochemistry. PMID 30730705 DOI: 10.1021/Acs.Biochem.9B00041 |
0.696 |
|
| 2019 |
Zhi Y, Narindoshvili T, Bogomolnaya L, Talamantes M, El Saadi A, Andrews-Polymenis H, Raushel FM. Deciphering the Enzymatic Function of the Bovine Enteric Infection Related Protein YfeJ from Salmonella enterica Serotype Typhimurium. Biochemistry. PMID 30715856 DOI: 10.1021/Acs.Biochem.8B01283 |
0.426 |
|
| 2018 |
Nemmara V, Xiang DF, Fedorov A, Fedorov EV, Bonanno JB, Almo SC, Raushel FM. Substrate Profile of the Phosphotriesterase Homology Protein from Escherichia coli. Biochemistry. PMID 30277746 DOI: 10.1021/Acs.Biochem.8B00935 |
0.518 |
|
| 2018 |
Hogancamp TN, Mabanglo MF, Raushel FM. Structure and Reaction Mechanism of the LigJ Hydratase: An Enzyme Critical for the Bacterial Degradation of Lignin in the Protocatechuate 4,5-Cleavage Pathway. Biochemistry. PMID 30207699 DOI: 10.1021/Acs.Biochem.8B00713 |
0.498 |
|
| 2018 |
Halling P, Fitzpatrick PF, Raushel FM, Rohwer J, Schnell S, Wittig U, Wohlgemuth R, Kettner C. An empirical analysis of enzyme function reporting for experimental reproducibility: Missing/incomplete information in published papers. Biophysical Chemistry. 242: 22-27. PMID 30195215 DOI: 10.1016/J.Bpc.2018.08.004 |
0.604 |
|
| 2018 |
Ghodge SV, Raushel FM. Structure, Mechanism, and Substrate Profiles of the Trinuclear Metallophosphatases from the Amidohydrolase Superfamily. Methods in Enzymology. 607: 187-216. PMID 30149858 DOI: 10.1016/Bs.Mie.2018.04.019 |
0.815 |
|
| 2018 |
Taylor ZW, Chamberlain AR, Raushel FM. Substrate Specificity and Chemical Mechanism for the Reaction Catalyzed by Glutamine Kinase. Biochemistry. PMID 30142271 DOI: 10.1021/Acs.Biochem.8B00811 |
0.437 |
|
| 2018 |
Mukherjee KW, Narindoshvili T, Raushel FM. Discovery of a Kojibiose Phosphorylase in Escherichia coli K-12. Biochemistry. PMID 29684280 DOI: 10.1021/Acs.Biochem.8B00392 |
0.34 |
|
| 2018 |
Hogancamp TN, Raushel FM. Functional Annotation of LigU as a 1,3-Allylic Isomerase During the Degradation of Lignin in the Protocatechuate 4,5-Cleavage Pathway from the Soil Bacterium Sphingobium sp. SYK-6. Biochemistry. PMID 29658701 DOI: 10.1021/Acs.Biochem.8B00295 |
0.389 |
|
| 2018 |
Taylor ZW, Raushel FM. Cytidine Diphosphoramidate Kinase: An Enzyme Required for the Biosynthesis of the O-Methyl Phosphoramidate Modification in the Capsular Polysaccharides of Campylobacter jejuni. Biochemistry. PMID 29578334 DOI: 10.1021/Acs.Biochem.8B00279 |
0.378 |
|
| 2018 |
Bigley AN, Narindoshvili T, Xiang DF, Raushel FM. Multiple Reaction Products from the Hydrolysis of Chiral and Prochiral Organophosphate Substrates by the Phosphotriesterase from Sphingobium sp. TCM1. Biochemistry. PMID 29513982 DOI: 10.1021/Acs.Biochem.8B00145 |
0.492 |
|
| 2018 |
Bae SY, Myslinski JM, McMahon LR, Height JJ, Bigley AN, Raushel FM, Harvey SP. An OPAA enzyme mutant with increased catalytic efficiency on the nerve agents sarin, soman, and GP. Enzyme and Microbial Technology. 112: 65-71. PMID 29499783 DOI: 10.1016/J.Enzmictec.2017.11.001 |
0.443 |
|
| 2018 |
Swainston N, Baici A, Bakker BM, Cornish-Bowden A, Fitzpatrick PF, Halling P, Leyh TS, O'Donovan C, Raushel FM, Reschel U, Rohwer JM, Schnell S, Schomburg D, Tipton KF, Tsai MD, et al. STRENDA DB: enabling the validation and sharing of enzyme kinetics data. The Febs Journal. PMID 29498804 DOI: 10.1111/Febs.14427 |
0.554 |
|
| 2017 |
Sheng X, Patskovsky Y, Vladimirova A, Bonanno JB, Almo SC, Himo F, Raushel FM. Mechanism and Structure of γ-Resorcylate Decarboxylase. Biochemistry. PMID 29283551 DOI: 10.1021/Acs.Biochem.7B01213 |
0.489 |
|
| 2017 |
Taylor Z, Brown HA, Holden HM, Raushel FM. Biosynthesis of Nucleoside Diphosphoramidates in Campylobacter jejuni. Biochemistry. PMID 29023101 DOI: 10.1021/Acs.Biochem.7B00905 |
0.415 |
|
| 2017 |
Taylor ZW, Brown HA, Narindoshvili T, Wenzel CQ, Szymanski C, Holden HM, Raushel FM. Discovery of a Glutamine Kinase Required for the Biosynthesis of the O-Methyl Phosphoramidate Modifications Found in the Capsular Polysaccharides of Campylobacter jejuni. Journal of the American Chemical Society. PMID 28650156 DOI: 10.1021/Jacs.7B04824 |
0.412 |
|
| 2017 |
Sheng X, Zhu W, Huddleston J, Xiang DF, Raushel FM, Richards NGJ, Himo F. A Combined Experimental-Theoretical Study of the LigW-Catalyzed Decarboxylation of 5-Carboxyvanillate in the Metabolic Pathway for Lignin Degradation Acs Catalysis. 7: 4968-4974. DOI: 10.1021/Acscatal.7B01166 |
0.345 |
|
| 2016 |
Mabanglo MF, Xiang DF, Bigley AN, Raushel FM. Structure of a Novel Phosphotriesterase from Sphingobium sp. TCM1; A Familiar Binuclear Metal Center Embedded in a 7-Bladed β-Propeller Protein Fold. Biochemistry. PMID 27353520 DOI: 10.1021/Acs.Biochem.6B00364 |
0.438 |
|
| 2016 |
Bigley AN, Xiang DF, Ren Z, Xue H, Hull KG, Romo D, Raushel FM. Chemical Mechanism of the Phosphotriesterase from Sphingobium sp. Strain TCM1, an Enzyme Capable of Hydrolyzing Organophosphate Flame Retardants. Journal of the American Chemical Society. PMID 26907457 DOI: 10.1021/Jacs.5B12739 |
0.442 |
|
| 2016 |
Vladimirova A, Patskovsky Y, Fedorov AA, Bonanno JB, Fedorov EV, Toro R, Hillerich B, Seidel RD, Richards NG, Almo SC, Raushel FM. Substrate Distortion and the Catalytic Reaction Mechanism of 5-Carboxyvanillate Decarboxylase. Journal of the American Chemical Society. 138: 826-36. PMID 26714575 DOI: 10.1021/Jacs.5B08251 |
0.526 |
|
| 2016 |
Raushel FM. Finding homes for orphan enzymes Perspectives in Science. 9: 3-7. DOI: 10.1016/J.Pisc.2016.02.002 |
0.339 |
|
| 2015 |
Yang K, Ren Z, Raushel FM, Zhang J. Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structure (London, England : 1993). PMID 26724995 DOI: 10.1016/J.Str.2015.11.009 |
0.344 |
|
| 2015 |
Xiang DF, Bigley AN, Ren Z, Xue H, Hull KG, Romo D, Raushel FM. Interrogation of the Substrate Profile and Catalytic Properties of the Phosphotriesterase from Sphingobium sp. Strain TCM1: An Enzyme Capable of Hydrolyzing Organophosphate Flame Retardants and Plasticizers. Biochemistry. PMID 26629649 DOI: 10.1021/Acs.Biochem.5B01144 |
0.441 |
|
| 2015 |
Bigley AN, Mabanglo MF, Harvey SP, Raushel FM. Variants of Phosphotriesterase for the Enhanced Detoxification of the Chemical Warfare Agent VR. Biochemistry. 54: 5502-12. PMID 26274608 DOI: 10.1021/Acs.Biochem.5B00629 |
0.428 |
|
| 2015 |
Ren Z, Ranganathan S, Zinnel NF, Russell WK, Russell DH, Raushel FM. Subunit Interactions within the Carbon-Phosphorus Lyase Complex from Escherichia coli. Biochemistry. 54: 3400-11. PMID 25954983 DOI: 10.1021/Acs.Biochem.5B00194 |
0.347 |
|
| 2015 |
Xiang DF, Patskovsky Y, Nemmara VV, Toro R, Almo SC, Raushel FM. Function discovery and structural characterization of a methylphosphonate esterase. Biochemistry. 54: 2919-30. PMID 25873441 DOI: 10.1021/Acs.Biochem.5B00199 |
0.499 |
|
| 2015 |
Ghodge SV, Raushel FM. Discovery of a Previously Unrecognized Ribonuclease from Escherichia coli That Hydrolyzes 5'-Phosphorylated Fragments of RNA. Biochemistry. 54: 2911-8. PMID 25871919 DOI: 10.1021/Acs.Biochem.5B00192 |
0.815 |
|
| 2015 |
Fedorov AA, Martí-Arbona R, Nemmara VV, Hitchcock D, Fedorov EV, Almo SC, Raushel FM. Structure of N-formimino-L-glutamate iminohydrolase from Pseudomonas aeruginosa. Biochemistry. 54: 890-7. PMID 25559274 DOI: 10.1021/Bi501299Y |
0.353 |
|
| 2015 |
Kamat SS, Raushel FM. PhnJ – A novel radical SAM enzyme from the C–P lyase complex Perspectives in Science. 4: 32-37. DOI: 10.1016/J.Pisc.2014.12.006 |
0.618 |
|
| 2014 |
Hitchcock DS, Fedorov AA, Fedorov EV, Almo SC, Raushel FM. Discovery of a bacterial 5-methylcytosine deaminase. Biochemistry. 53: 7426-35. PMID 25384249 DOI: 10.1021/Bi5012767 |
0.462 |
|
| 2014 |
Hobbs ME, Williams HJ, Hillerich B, Almo SC, Raushel FM. l-Galactose metabolism in Bacteroides vulgatus from the human gut microbiota. Biochemistry. 53: 4661-70. PMID 24963813 DOI: 10.1021/Bi500656M |
0.315 |
|
| 2014 |
Korczynska M, Xiang DF, Zhang Z, Xu C, Narindoshvili T, Kamat SS, Williams HJ, Chang SS, Kolb P, Hillerich B, Sauder JM, Burley SK, Almo SC, Swaminathan S, Shoichet BK, ... Raushel FM, et al. Functional annotation and structural characterization of a novel lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. Biochemistry. 53: 4727-38. PMID 24955762 DOI: 10.1021/Bi500595C |
0.654 |
|
| 2014 |
Manta B, Raushel FM, Himo F. Reaction mechanism of zinc-dependent cytosine deaminase from Escherichia coli: a quantum-chemical study. The Journal of Physical Chemistry. B. 118: 5644-52. PMID 24833316 DOI: 10.1021/Jp501228S |
0.444 |
|
| 2014 |
Xiang DF, Kumaran D, Swaminathan S, Raushel FM. Structural characterization and function determination of a nonspecific carboxylate esterase from the amidohydrolase superfamily with a promiscuous ability to hydrolyze methylphosphonate esters. Biochemistry. 53: 3476-85. PMID 24832101 DOI: 10.1021/Bi5004266 |
0.402 |
|
| 2014 |
Barelier S, Cummings JA, Rauwerdink AM, Hitchcock DS, Farelli JD, Almo SC, Raushel FM, Allen KN, Shoichet BK. Substrate deconstruction and the nonadditivity of enzyme recognition. Journal of the American Chemical Society. 136: 7374-82. PMID 24791931 DOI: 10.1021/Ja501354Q |
0.474 |
|
| 2014 |
Cummings JA, Vetting M, Ghodge SV, Xu C, Hillerich B, Seidel RD, Almo SC, Raushel FM. Prospecting for unannotated enzymes: discovery of a 3',5'-nucleotide bisphosphate phosphatase within the amidohydrolase superfamily. Biochemistry. 53: 591-600. PMID 24401123 DOI: 10.1021/Bi401640R |
0.835 |
|
| 2014 |
Tipton KF, Armstrong RN, Bakker BM, Bairoch A, Cornish-Bowden A, Halling PJ, Hofmeyr J, Leyh TS, Kettner C, Raushel FM, Rohwer J, Schomburg D, Steinbeck C. Standards for Reporting Enzyme Data: The STRENDA Consortium: What it aims to do and why it should be helpful Perspectives in Science. 1: 131-137. DOI: 10.1016/J.Pisc.2014.02.012 |
0.392 |
|
| 2013 |
Dunaway-Mariano D, Holden HM, Raushel FM. W. W. "Mo" Cleland: a catalytic life. Biochemistry. 52: 9092-6. PMID 24308306 DOI: 10.1021/Bi4015709 |
0.434 |
|
| 2013 |
Raushel FM. Biochemistry. Not an oxidase, but a peroxidase. Science (New York, N.Y.). 342: 943-4. PMID 24264984 DOI: 10.1126/Science.1247233 |
0.371 |
|
| 2013 |
Ghodge SV, Cummings JA, Williams HJ, Raushel FM. Discovery of a cyclic phosphodiesterase that catalyzes the sequential hydrolysis of both ester bonds to phosphorus. Journal of the American Chemical Society. 135: 16360-3. PMID 24147537 DOI: 10.1021/Ja409376K |
0.832 |
|
| 2013 |
Kamat SS, Burgos ES, Raushel FM. Potent inhibition of the C-P lyase nucleosidase PhnI by Immucillin-A triphosphate. Biochemistry. 52: 7366-8. PMID 24111876 DOI: 10.1021/Bi4013287 |
0.636 |
|
| 2013 |
Goble AM, Feng Y, Raushel FM, Cronan JE. Discovery of a cAMP deaminase that quenches cyclic AMP-dependent regulation. Acs Chemical Biology. 8: 2622-9. PMID 24074367 DOI: 10.1021/Cb4004628 |
0.376 |
|
| 2013 |
Goble AM, Toro R, Li X, Ornelas A, Fan H, Eswaramoorthy S, Patskovsky Y, Hillerich B, Seidel R, Sali A, Shoichet BK, Almo SC, Swaminathan S, Tanner ME, Raushel FM. Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes. Biochemistry. 52: 6525-36. PMID 23972005 DOI: 10.1021/Bi400750A |
0.758 |
|
| 2013 |
Hitchcock DS, Fan H, Kim J, Vetting M, Hillerich B, Seidel RD, Almo SC, Shoichet BK, Sali A, Raushel FM. Structure-guided discovery of new deaminase enzymes. Journal of the American Chemical Society. 135: 13927-33. PMID 23968233 DOI: 10.1021/Ja4066078 |
0.643 |
|
| 2013 |
Meier MM, Rajendran C, Malisi C, Fox NG, Xu C, Schlee S, Barondeau DP, Höcker B, Sterner R, Raushel FM. Molecular engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template. Journal of the American Chemical Society. 135: 11670-7. PMID 23837603 DOI: 10.1021/Ja405911H |
0.444 |
|
| 2013 |
Kamat SS, Raushel FM. The enzymatic conversion of phosphonates to phosphate by bacteria. Current Opinion in Chemical Biology. 17: 589-96. PMID 23830682 DOI: 10.1016/J.Cbpa.2013.06.006 |
0.643 |
|
| 2013 |
Bigley AN, Xu C, Henderson TJ, Harvey SP, Raushel FM. Enzymatic neutralization of the chemical warfare agent VX: evolution of phosphotriesterase for phosphorothiolate hydrolysis. Journal of the American Chemical Society. 135: 10426-32. PMID 23789980 DOI: 10.1021/Ja402832Z |
0.446 |
|
| 2013 |
Kamat SS, Williams HJ, Dangott LJ, Chakrabarti M, Raushel FM. The catalytic mechanism for aerobic formation of methane by bacteria. Nature. 497: 132-6. PMID 23615610 DOI: 10.1038/Nature12061 |
0.642 |
|
| 2013 |
Ghodge SV, Fedorov AA, Fedorov EV, Hillerich B, Seidel R, Almo SC, Raushel FM. Structural and mechanistic characterization of L-histidinol phosphate phosphatase from the polymerase and histidinol phosphatase family of proteins. Biochemistry. 52: 1101-12. PMID 23327428 DOI: 10.1021/Bi301496P |
0.826 |
|
| 2013 |
Fan H, Hitchcock DS, Seidel RD, Hillerich B, Lin H, Almo SC, Sali A, Shoichet BK, Raushel FM. Assignment of pterin deaminase activity to an enzyme of unknown function guided by homology modeling and docking. Journal of the American Chemical Society. 135: 795-803. PMID 23256477 DOI: 10.1021/Ja309680B |
0.41 |
|
| 2013 |
Hobbs ME, Vetting M, Williams HJ, Narindoshvili T, Kebodeaux DM, Hillerich B, Seidel RD, Almo SC, Raushel FM. Discovery of an L-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily. Biochemistry. 52: 239-53. PMID 23214453 DOI: 10.1021/Bi3015554 |
0.337 |
|
| 2013 |
Ornelas A, Korczynska M, Ragumani S, Kumaran D, Narindoshvili T, Shoichet BK, Swaminathan S, Raushel FM. Functional annotation and three-dimensional structure of an incorrectly annotated dihydroorotase from cog3964 in the amidohydrolase superfamily. Biochemistry. 52: 228-38. PMID 23214420 DOI: 10.1021/Bi301483Z |
0.696 |
|
| 2013 |
Bigley AN, Raushel FM. Catalytic mechanisms for phosphotriesterases. Biochimica Et Biophysica Acta. 1834: 443-53. PMID 22561533 DOI: 10.1016/J.Bbapap.2012.04.004 |
0.522 |
|
| 2012 |
Tsai PC, Fox N, Bigley AN, Harvey SP, Barondeau DP, Raushel FM. Enzymes for the homeland defense: optimizing phosphotriesterase for the hydrolysis of organophosphate nerve agents. Biochemistry. 51: 6463-75. PMID 22809162 DOI: 10.1021/Bi300811T |
0.675 |
|
| 2012 |
Fan F, Williams HJ, Boyer JG, Graham TL, Zhao H, Lehr R, Qi H, Schwartz B, Raushel FM, Meek TD. On the catalytic mechanism of human ATP citrate lyase. Biochemistry. 51: 5198-211. PMID 22657152 DOI: 10.1021/Bi300611S |
0.449 |
|
| 2012 |
Hobbs ME, Malashkevich V, Williams HJ, Xu C, Sauder JM, Burley SK, Almo SC, Raushel FM. Structure and catalytic mechanism of LigI: insight into the amidohydrolase enzymes of cog3618 and lignin degradation. Biochemistry. 51: 3497-507. PMID 22475079 DOI: 10.1021/Bi300307B |
0.515 |
|
| 2012 |
Xiang DF, Kolb P, Fedorov AA, Xu C, Fedorov EV, Narindoshivili T, Williams HJ, Shoichet BK, Almo SC, Raushel FM. Structure-based function discovery of an enzyme for the hydrolysis of phosphorylated sugar lactones. Biochemistry. 51: 1762-73. PMID 22313111 DOI: 10.1021/Bi201838B |
0.524 |
|
| 2011 |
Kamat SS, Williams HJ, Raushel FM. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature. 480: 570-3. PMID 22089136 DOI: 10.1038/Nature10622 |
0.648 |
|
| 2011 |
Gerlt JA, Allen KN, Almo SC, Armstrong RN, Babbitt PC, Cronan JE, Dunaway-Mariano D, Imker HJ, Jacobson MP, Minor W, Poulter CD, Raushel FM, Sali A, Shoichet BK, Sweedler JV. The Enzyme Function Initiative. Biochemistry. 50: 9950-62. PMID 21999478 DOI: 10.1021/Bi201312U |
0.379 |
|
| 2011 |
Kamat SS, Holmes-Hampton GP, Bagaria A, Kumaran D, Tichy SE, Gheyi T, Zheng X, Bain K, Groshong C, Emtage S, Sauder JM, Burley SK, Swaminathan S, Lindahl PA, Raushel FM. The catalase activity of diiron adenine deaminase. Protein Science : a Publication of the Protein Society. 20: 2080-94. PMID 21998098 DOI: 10.1002/Pro.748 |
0.635 |
|
| 2011 |
Goble AM, Fan H, Sali A, Raushel FM. Discovery of a cytokinin deaminase. Acs Chemical Biology. 6: 1036-40. PMID 21823622 DOI: 10.1021/Cb200198C |
0.367 |
|
| 2011 |
Goble AM, Zhang Z, Sauder JM, Burley SK, Swaminathan S, Raushel FM. Pa0148 from Pseudomonas aeruginosa catalyzes the deamination of adenine. Biochemistry. 50: 6589-97. PMID 21710971 DOI: 10.1021/Bi200868U |
0.462 |
|
| 2011 |
Hitchcock DS, Fedorov AA, Fedorov EV, Dangott LJ, Almo SC, Raushel FM. Rescue of the orphan enzyme isoguanine deaminase. Biochemistry. 50: 5555-7. PMID 21604715 DOI: 10.1021/Bi200680Y |
0.348 |
|
| 2011 |
Hall RS, Fedorov AA, Xu C, Fedorov EV, Almo SC, Raushel FM. Three-dimensional structure and catalytic mechanism of cytosine deaminase. Biochemistry. 50: 5077-85. PMID 21545144 DOI: 10.1021/Bi200483K |
0.481 |
|
| 2011 |
Kamat SS, Fan H, Sauder JM, Burley SK, Shoichet BK, Sali A, Raushel FM. Enzymatic deamination of the epigenetic base N-6-methyladenine. Journal of the American Chemical Society. 133: 2080-3. PMID 21275375 DOI: 10.1021/Ja110157U |
0.609 |
|
| 2011 |
Raushel FM. Chemical biology: Catalytic detoxification. Nature. 469: 310-1. PMID 21248836 DOI: 10.1038/469310A |
0.37 |
|
| 2011 |
Kamat SS, Bagaria A, Kumaran D, Holmes-Hampton GP, Fan H, Sali A, Sauder JM, Burley SK, Lindahl PA, Swaminathan S, Raushel FM. Catalytic mechanism and three-dimensional structure of adenine deaminase. Biochemistry. 50: 1917-27. PMID 21247091 DOI: 10.1021/Bi101788N |
0.64 |
|
| 2010 |
Meyer ME, Gutierrez JA, Raushel FM, Richards NG. A conserved glutamate controls the commitment to acyl-adenylate formation in asparagine synthetase. Biochemistry. 49: 9391-401. PMID 20853825 DOI: 10.1021/Bi1010688 |
0.467 |
|
| 2010 |
Tsai PC, Bigley A, Li Y, Ghanem E, Cadieux CL, Kasten SA, Reeves TE, Cerasoli DM, Raushel FM. Stereoselective hydrolysis of organophosphate nerve agents by the bacterial phosphotriesterase. Biochemistry. 49: 7978-87. PMID 20701311 DOI: 10.1021/Bi101056M |
0.814 |
|
| 2010 |
Tsai PC, Fan Y, Kim J, Yang L, Almo SC, Gao YQ, Raushel FM. Structural determinants for the stereoselective hydrolysis of chiral substrates by phosphotriesterase. Biochemistry. 49: 7988-97. PMID 20695627 DOI: 10.1021/Bi101058Z |
0.745 |
|
| 2010 |
Xiang DF, Patskovsky Y, Xu C, Fedorov AA, Fedorov EV, Sisco AA, Sauder JM, Burley SK, Almo SC, Raushel FM. Functional identification and structure determination of two novel prolidases from cog1228 in the amidohydrolase superfamily . Biochemistry. 49: 6791-803. PMID 20604542 DOI: 10.1021/Bi100897U |
0.377 |
|
| 2010 |
Hall RS, Agarwal R, Hitchcock D, Sauder JM, Burley SK, Swaminathan S, Raushel FM. Discovery and structure determination of the orphan enzyme isoxanthopterin deaminase . Biochemistry. 49: 4374-82. PMID 20415463 DOI: 10.1021/Bi100252S |
0.489 |
|
| 2010 |
Lund L, Fan Y, Shao Q, Gao YQ, Raushel FM. Carbamate transport in carbamoyl phosphate synthetase: a theoretical and experimental investigation. Journal of the American Chemical Society. 132: 3870-8. PMID 20187643 DOI: 10.1021/Ja910441V |
0.64 |
|
| 2010 |
Hall RS, Fedorov AA, Marti-Arbona R, Fedorov EV, Kolb P, Sauder JM, Burley SK, Shoichet BK, Almo SC, Raushel FM. The hunt for 8-oxoguanine deaminase. Journal of the American Chemical Society. 132: 1762-3. PMID 20088583 DOI: 10.1021/Ja909817D |
0.466 |
|
| 2010 |
Cummings JA, Nguyen TT, Fedorov AA, Kolb P, Xu C, Fedorov EV, Shoichet BK, Barondeau DP, Almo SC, Raushel FM. Structure, mechanism, and substrate profile for Sco3058: the closest bacterial homologue to human renal dipeptidase . Biochemistry. 49: 611-22. PMID 20000809 DOI: 10.1021/Bi901935Y |
0.748 |
|
| 2009 |
Nguyen TT, Fedorov AA, Williams L, Fedorov EV, Li Y, Xu C, Almo SC, Raushel FM. The mechanism of the reaction catalyzed by uronate isomerase illustrates how an isomerase may have evolved from a hydrolase within the amidohydrolase superfamily. Biochemistry. 48: 8879-90. PMID 19678710 DOI: 10.1021/Bi901046X |
0.808 |
|
| 2009 |
Fan Y, Lund L, Shao Q, Gao YQ, Raushel FM. A combined theoretical and experimental study of the ammonia tunnel in carbamoyl phosphate synthetase. Journal of the American Chemical Society. 131: 10211-9. PMID 19569682 DOI: 10.1021/Ja902557R |
0.634 |
|
| 2009 |
Cummings JA, Fedorov AA, Xu C, Brown S, Fedorov E, Babbitt PC, Almo SC, Raushel FM. Annotating enzymes of uncertain function: the deacylation of D-amino acids by members of the amidohydrolase superfamily. Biochemistry. 48: 6469-81. PMID 19518059 DOI: 10.1021/Bi900661B |
0.38 |
|
| 2009 |
Xiang DF, Xu C, Kumaran D, Brown AC, Sauder JM, Burley SK, Swaminathan S, Raushel FM. Functional annotation of two new carboxypeptidases from the amidohydrolase superfamily of enzymes. Biochemistry. 48: 4567-76. PMID 19358546 DOI: 10.1021/Bi900453U |
0.44 |
|
| 2009 |
Xiang DF, Patskovsky Y, Xu C, Meyer AJ, Sauder JM, Burley SK, Almo SC, Raushel FM. Functional identification of incorrectly annotated prolidases from the amidohydrolase superfamily of enzymes. Biochemistry. 48: 3730-42. PMID 19281183 DOI: 10.1021/Bi900111Q |
0.427 |
|
| 2009 |
Pieper U, Chiang R, Seffernick JJ, Brown SD, Glasner ME, Kelly L, Eswar N, Sauder JM, Bonanno JB, Swaminathan S, Burley SK, Zheng X, Chance MR, Almo SC, Gerlt JA, ... Raushel FM, et al. Target selection and annotation for the structural genomics of the amidohydrolase and enolase superfamilies. Journal of Structural and Functional Genomics. 10: 107-25. PMID 19219566 DOI: 10.1007/S10969-008-9056-5 |
0.345 |
|
| 2009 |
Xiang DF, Kolb P, Fedorov AA, Meier MM, Fedorov LV, Nguyen TT, Sterner R, Almo SC, Shoichet BK, Raushel FM. Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily. Biochemistry. 48: 2237-47. PMID 19159332 DOI: 10.1021/Bi802274F |
0.772 |
|
| 2008 |
Kim J, Tsai PC, Chen SL, Himo F, Almo SC, Raushel FM. Structure of diethyl phosphate bound to the binuclear metal center of phosphotriesterase. Biochemistry. 47: 9497-504. PMID 18702530 DOI: 10.1021/Bi800971V |
0.714 |
|
| 2008 |
Tyagi R, Eswaramoorthy S, Burley SK, Raushel FM, Swaminathan S. A common catalytic mechanism for proteins of the HutI family. Biochemistry. 47: 5608-15. PMID 18442260 DOI: 10.1021/Bi800180G |
0.386 |
|
| 2008 |
Williams L, Fan F, Blanchard JS, Raushel FM. Positional isotope exchange analysis of the Mycobacterium smegmatis cysteine ligase (MshC). Biochemistry. 47: 4843-50. PMID 18373355 DOI: 10.1021/Bi800327U |
0.737 |
|
| 2008 |
Liao RZ, Yu JG, Raushel FM, Himo F. Theoretical investigation of the reaction mechanism of the dinuclear zinc enzyme dihydroorotase. Chemistry (Weinheim An Der Bergstrasse, Germany). 14: 4287-92. PMID 18366031 DOI: 10.1002/Chem.200701948 |
0.468 |
|
| 2008 |
Fan Y, Lund L, Yang L, Raushel FM, Gao YQ. Mechanism for the transport of ammonia within carbamoyl phosphate synthetase determined by molecular dynamics simulations. Biochemistry. 47: 2935-44. PMID 18220365 DOI: 10.1021/Bi701572H |
0.617 |
|
| 2008 |
Nguyen TT, Brown S, Fedorov AA, Fedorov EV, Babbitt PC, Almo SC, Raushel FM. At the periphery of the amidohydrolase superfamily: Bh0493 from Bacillus halodurans catalyzes the isomerization of D-galacturonate to D-tagaturonate. Biochemistry. 47: 1194-206. PMID 18171028 DOI: 10.1021/Bi7017738 |
0.705 |
|
| 2007 |
Li Y, Raushel FM. Differentiation of chiral phosphorus enantiomers by P and H NMR spectroscopy using amino acid derivatives as chemical solvating agents. Tetrahedron, Asymmetry. 18: 1391-1397. PMID 18037983 DOI: 10.1016/J.Tetasy.2007.06.012 |
0.316 |
|
| 2007 |
Fresquet V, Williams L, Raushel FM. Partial randomization of the four sequential amidation reactions catalyzed by cobyric acid synthetase with a single point mutation. Biochemistry. 46: 13983-93. PMID 18001139 DOI: 10.1021/Bi7016238 |
0.674 |
|
| 2007 |
Ghanem E, Li Y, Xu C, Raushel FM. Characterization of a phosphodiesterase capable of hydrolyzing EA 2192, the most toxic degradation product of the nerve agent VX. Biochemistry. 46: 9032-40. PMID 17630782 DOI: 10.1021/Bi700561K |
0.799 |
|
| 2007 |
Hermann JC, Marti-Arbona R, Fedorov AA, Fedorov E, Almo SC, Shoichet BK, Raushel FM. Structure-based activity prediction for an enzyme of unknown function. Nature. 448: 775-9. PMID 17603473 DOI: 10.1038/Nature05981 |
0.421 |
|
| 2007 |
Hall RS, Brown S, Fedorov AA, Fedorov EV, Xu C, Babbitt PC, Almo SC, Raushel FM. Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase. Biochemistry. 46: 7953-62. PMID 17567048 DOI: 10.1021/Bi700544C |
0.474 |
|
| 2007 |
Hall RS, Xiang DF, Xu C, Raushel FM. N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion. Biochemistry. 46: 7942-52. PMID 17567047 DOI: 10.1021/Bi700543X |
0.484 |
|
| 2007 |
Samples CR, Raushel FM, DeRose VJ. Activation of the binuclear metal center through formation of phosphotriesterase-inhibitor complexes. Biochemistry. 46: 3435-42. PMID 17315951 DOI: 10.1021/Bi061951D |
0.395 |
|
| 2007 |
Williams L, Fresquet V, Santander PJ, Raushel FM. The multiple amidation reactions catalyzed by Cobyric acid synthetase from Salmonella typhimurium are sequential and dissociative. Journal of the American Chemical Society. 129: 294-5. PMID 17212407 DOI: 10.1021/Ja067962B |
0.663 |
|
| 2007 |
Proteasa G, Tahboub YR, Galijasevic S, Raushel FM, Abu-Soud HM. Kinetic evidence supports the existence of two halide binding sites that have a distinct impact on the heme iron microenvironment in myeloperoxidase. Biochemistry. 46: 398-405. PMID 17209550 DOI: 10.1021/Bi0609725 |
0.319 |
|
| 2006 |
Nowlan C, Li Y, Hermann JC, Evans T, Carpenter J, Ghanem E, Shoichet BK, Raushel FM. Resolution of chiral phosphate, phosphonate, and phosphinate esters by an enantioselective enzyme library. Journal of the American Chemical Society. 128: 15892-902. PMID 17147402 DOI: 10.1021/Ja0658618 |
0.835 |
|
| 2006 |
Hermann JC, Ghanem E, Li Y, Raushel FM, Irwin JJ, Shoichet BK. Predicting substrates by docking high-energy intermediates to enzyme structures. Journal of the American Chemical Society. 128: 15882-91. PMID 17147401 DOI: 10.1021/Ja065860F |
0.82 |
|
| 2006 |
Martí-Arbona R, Raushel FM. Mechanistic characterization of N-formimino-L-glutamate iminohydrolase from Pseudomonas aeruginosa. Biochemistry. 45: 14256-62. PMID 17128965 DOI: 10.1021/Bi061673I |
0.44 |
|
| 2006 |
Weeks A, Lund L, Raushel FM. Tunneling of intermediates in enzyme-catalyzed reactions. Current Opinion in Chemical Biology. 10: 465-72. PMID 16931112 DOI: 10.1016/J.Cbpa.2006.08.008 |
0.664 |
|
| 2006 |
Williams L, Nguyen T, Li Y, Porter TN, Raushel FM. Uronate isomerase: a nonhydrolytic member of the amidohydrolase superfamily with an ambivalent requirement for a divalent metal ion. Biochemistry. 45: 7453-62. PMID 16768441 DOI: 10.1021/Bi060531L |
0.804 |
|
| 2006 |
Sakai A, Xiang DF, Xu C, Song L, Yew WS, Raushel FM, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: N-succinylamino acid racemase and a new pathway for the irreversible conversion of D- to L-amino acids. Biochemistry. 45: 4455-62. PMID 16584181 DOI: 10.1021/Bi060230B |
0.419 |
|
| 2006 |
Xu C, Hall R, Cummings J, Raushel FM. Tight binding inhibitors of N-acyl amino sugar and N-acyl amino acid deacetylases. Journal of the American Chemical Society. 128: 4244-5. PMID 16568996 DOI: 10.1021/Ja0600680 |
0.4 |
|
| 2006 |
Martí-Arbona R, Xu C, Steele S, Weeks A, Kuty GF, Seibert CM, Raushel FM. Annotating enzymes of unknown function: N-formimino-L-glutamate deiminase is a member of the amidohydrolase superfamily. Biochemistry. 45: 1997-2005. PMID 16475788 DOI: 10.1021/Bi0525425 |
0.309 |
|
| 2006 |
Korpan YI, Raushel FM, Nazarenko EA, Soldatkin AP, Jaffrezic-Renault N, Martelet C. Sensitivity and specificity improvement of an ion sensitive field effect transistors-based biosensor for potato glycoalkaloids detection. Journal of Agricultural and Food Chemistry. 54: 707-12. PMID 16448172 DOI: 10.1021/Jf0529316 |
0.301 |
|
| 2006 |
Proteasa G, Tahboub Y, Galijasevic S, Raushel F, Abu-Soud H. P180. Kinetic evidence supports the existence of two halide binding sites that displays distinct impact on the heme iron microenvironment in myeloperoxidase Nitric Oxide. 14: 76. DOI: 10.1016/J.Niox.2006.04.250 |
0.305 |
|
| 2005 |
Martí-Arbona R, Thoden JB, Holden HM, Raushel FM. Functional significance of Glu-77 and Tyr-137 within the active site of isoaspartyl dipeptidase. Bioorganic Chemistry. 33: 448-58. PMID 16289685 DOI: 10.1016/J.Bioorg.2005.10.002 |
0.47 |
|
| 2005 |
Li Y, Raushel FM. Inhibitors designed for the active site of dihydroorotase. Bioorganic Chemistry. 33: 470-83. PMID 16213543 DOI: 10.1016/J.Bioorg.2005.08.001 |
0.339 |
|
| 2005 |
Irwin JJ, Raushel FM, Shoichet BK. Virtual screening against metalloenzymes for inhibitors and substrates. Biochemistry. 44: 12316-28. PMID 16156645 DOI: 10.1021/Bi050801K |
0.375 |
|
| 2005 |
Samples CR, Howard T, Raushel FM, DeRose VJ. Protonation of the binuclear metal center within the active site of phosphotriesterase. Biochemistry. 44: 11005-13. PMID 16101284 DOI: 10.1021/Bi0506270 |
0.428 |
|
| 2005 |
Ghanem E, Raushel FM. Detoxification of organophosphate nerve agents by bacterial phosphotriesterase. Toxicology and Applied Pharmacology. 207: 459-70. PMID 15982683 DOI: 10.1016/J.Taap.2005.02.025 |
0.801 |
|
| 2005 |
Martí-Arbona R, Fresquet V, Thoden JB, Davis ML, Holden HM, Raushel FM. Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 44: 7115-24. PMID 15882050 DOI: 10.1021/Bi050008R |
0.46 |
|
| 2005 |
Seibert CM, Raushel FM. Structural and catalytic diversity within the amidohydrolase superfamily. Biochemistry. 44: 6383-91. PMID 15850372 DOI: 10.1021/Bi047326V |
0.424 |
|
| 2005 |
Harvey SP, Kolakowski JE, Cheng TC, Rastogi VK, Reiff LP, DeFrank JJ, Raushel FM, Hill C. Stereospecificity in the enzymatic hydrolysis of cyclosarin (GF) Enzyme and Microbial Technology. 37: 547-555. DOI: 10.1016/J.Enzmictec.2005.04.004 |
0.461 |
|
| 2005 |
Lawson GE, Lee Y, Raushel FM, Singh A. Phospholipid-Based Catalytic Nanocapsules Advanced Functional Materials. 15: 267-272. DOI: 10.1002/Adfm.200400153 |
0.436 |
|
| 2004 |
Porter TN, Li Y, Raushel FM. Mechanism of the dihydroorotase reaction. Biochemistry. 43: 16285-92. PMID 15610022 DOI: 10.1021/Bi048308G |
0.835 |
|
| 2004 |
Abu-Soud HM, Raushel FM, Hazen SL. A novel multistep mechanism for oxygen binding to ferrous hemoproteins: rapid kinetic analysis of ferrous-dioxy myeloperoxidase (compound III) formation. Biochemistry. 43: 11589-95. PMID 15350145 DOI: 10.1021/Bi049541H |
0.331 |
|
| 2004 |
Thoden JB, Huang X, Kim J, Raushel FM, Holden HM. Long-range allosteric transitions in carbamoyl phosphate synthetase. Protein Science : a Publication of the Protein Society. 13: 2398-405. PMID 15322282 DOI: 10.1110/Ps.04822704 |
0.656 |
|
| 2004 |
Park MS, Hill CM, Li Y, Hardy RK, Khanna H, Khang YH, Raushel FM. Catalytic properties of the PepQ prolidase from Escherichia coli. Archives of Biochemistry and Biophysics. 429: 224-30. PMID 15313226 DOI: 10.1016/J.Abb.2004.06.022 |
0.394 |
|
| 2004 |
Fresquet V, Williams L, Raushel FM. Mechanism of cobyrinic acid a,c-diamide synthetase from Salmonella typhimurium LT2. Biochemistry. 43: 10619-27. PMID 15311923 DOI: 10.1021/Bi048972X |
0.654 |
|
| 2004 |
Hong SB, Raushel FM. Control of stereoselectivity in phosphotriesterase. Methods in Enzymology. 388: 256-66. PMID 15289077 DOI: 10.1016/S0076-6879(04)88022-4 |
0.445 |
|
| 2004 |
Li Y, Aubert SD, Maes EG, Raushel FM. Enzymatic resolution of chiral phosphinate esters. Journal of the American Chemical Society. 126: 8888-9. PMID 15264807 DOI: 10.1021/Ja048457M |
0.816 |
|
| 2004 |
Aubert SD, Li Y, Raushel FM. Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase. Biochemistry. 43: 5707-15. PMID 15134445 DOI: 10.1021/Bi0497805 |
0.808 |
|
| 2004 |
Kim J, Raushel FM. Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between sequential active sites. Biochemistry. 43: 5334-40. PMID 15122899 DOI: 10.1021/Bi049945+ |
0.662 |
|
| 2004 |
Kim J, Raushel FM. Access to the carbamate tunnel of carbamoyl phosphate synthetase. Archives of Biochemistry and Biophysics. 425: 33-41. PMID 15081891 DOI: 10.1016/J.Abb.2004.02.031 |
0.631 |
|
| 2004 |
Fresquet V, Thoden JB, Holden HM, Raushel FM. Kinetic mechanism of asparagine synthetase from Vibrio cholerae. Bioorganic Chemistry. 32: 63-75. PMID 14990305 DOI: 10.1016/J.Bioorg.2003.10.002 |
0.463 |
|
| 2003 |
Hill CM, Li WS, Thoden JB, Holden HM, Raushel FM. Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site. Journal of the American Chemical Society. 125: 8990-1. PMID 15369336 DOI: 10.1021/Ja0358798 |
0.695 |
|
| 2003 |
Garrett JB, Mullins LS, Raushel FM. Effect of linker sequence on the stability of circularly permuted variants of ribonuclease T1. Bioorganic Chemistry. 31: 412-24. PMID 12941293 DOI: 10.1016/S0045-2068(03)00079-8 |
0.314 |
|
| 2003 |
Lum KT, Huebner HJ, Li Y, Phillips TD, Raushel FM. Organophosphate nerve agent toxicity in Hydra attenuata. Chemical Research in Toxicology. 16: 953-7. PMID 12924922 DOI: 10.1021/Tx034047K |
0.773 |
|
| 2003 |
Raushel FM, Thoden JB, Holden HM. Enzymes with molecular tunnels. Accounts of Chemical Research. 36: 539-48. PMID 12859215 DOI: 10.1021/Ar020047K |
0.45 |
|
| 2003 |
Li Y, Aubert SD, Raushel FM. Operational control of stereoselectivity during the enzymatic hydrolysis of racemic organophosphorus compounds. Journal of the American Chemical Society. 125: 7526-7. PMID 12812487 DOI: 10.1021/Ja035625M |
0.808 |
|
| 2003 |
Williams L, Zheng R, Blanchard JS, Raushel FM. Positional isotope exchange analysis of the pantothenate synthetase reaction. Biochemistry. 42: 5108-13. PMID 12718554 DOI: 10.1021/Bi0340853 |
0.731 |
|
| 2003 |
Thoden JB, Marti-Arbona R, Raushel FM, Holden HM. High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 42: 4874-82. PMID 12718528 DOI: 10.1021/Bi034233P |
0.463 |
|
| 2003 |
Thoden JB, Kim J, Raushel FM, Holden HM. The catalytic mechanism of galactose mutarotase. Protein Science : a Publication of the Protein Society. 12: 1051-9. PMID 12717027 DOI: 10.1110/Ps.0243203 |
0.659 |
|
| 2003 |
Gerlt JA, Raushel FM. Evolution of function in (beta/alpha)8-barrel enzymes. Current Opinion in Chemical Biology. 7: 252-64. PMID 12714059 DOI: 10.1016/S1367-5931(03)00019-X |
0.359 |
|
| 2002 |
Kim J, Howell S, Huang X, Raushel FM. Structural defects within the carbamate tunnel of carbamoyl phosphate synthetase. Biochemistry. 41: 12575-81. PMID 12379099 DOI: 10.1021/Bi020421O |
0.653 |
|
| 2002 |
Thoden JB, Kim J, Raushel FM, Holden HM. Structural and kinetic studies of sugar binding to galactose mutarotase from Lactococcus lactis. The Journal of Biological Chemistry. 277: 45458-65. PMID 12218067 DOI: 10.1074/Jbc.M208395200 |
0.61 |
|
| 2002 |
Thoden JB, Huang X, Raushel FM, Holden HM. Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia. The Journal of Biological Chemistry. 277: 39722-7. PMID 12130656 DOI: 10.1074/Jbc.M206915200 |
0.46 |
|
| 2002 |
Raushel FM. Bacterial detoxification of organophosphate nerve agents. Current Opinion in Microbiology. 5: 288-95. PMID 12057683 DOI: 10.1016/S1369-5274(02)00314-4 |
0.44 |
|
| 2002 |
Li WS, Li Y, Hill CM, Lum KT, Raushel FM. Enzymatic synthesis of chiral organophosphothioates from prochiral precursors. Journal of the American Chemical Society. 124: 3498-9. PMID 11929226 DOI: 10.1021/Ja017840D |
0.798 |
|
| 2002 |
Pierrat OA, Raushel FM. A functional analysis of the allosteric nucleotide monophosphate binding site of carbamoyl phosphate synthetase. Archives of Biochemistry and Biophysics. 400: 34-42. PMID 11913968 DOI: 10.1006/Abbi.2002.2767 |
0.367 |
|
| 2002 |
Pierrat OA, Javid-Majd F, Raushel FM. Dissection of the conduit for allosteric control of carbamoyl phosphate synthetase by ornithine. Archives of Biochemistry and Biophysics. 400: 26-33. PMID 11913967 DOI: 10.1006/Abbi.2002.2768 |
0.357 |
|
| 2002 |
Miles BW, Thoden JB, Holden HM, Raushel FM. Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin. The Journal of Biological Chemistry. 277: 4368-73. PMID 11729189 DOI: 10.1074/Jbc.M108582200 |
0.481 |
|
| 2001 |
Anderson MA, Shim H, Raushel FM, Cleland WW. Hydrolysis of phosphotriesters: determination of transition states in parallel reactions by heavy-atom isotope effects. Journal of the American Chemical Society. 123: 9246-53. PMID 11562204 DOI: 10.1021/Ja011025G |
0.637 |
|
| 2001 |
Kim J, Raushel FM. Allosteric control of the oligomerization of carbamoyl phosphate synthetase from Escherichia coli. Biochemistry. 40: 11030-6. PMID 11551199 DOI: 10.1021/Bi011121U |
0.551 |
|
| 2001 |
Li WS, Lum KT, Chen-Goodspeed M, Sogorb MA, Raushel FM. Stereoselective detoxification of chiral sarin and soman analogues by phosphotriesterase. Bioorganic & Medicinal Chemistry. 9: 2083-91. PMID 11504644 DOI: 10.1016/S0968-0896(01)00113-4 |
0.768 |
|
| 2001 |
Thoden JB, Phillips GN, Neal TM, Raushel FM, Holden HM. Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry. 40: 6989-97. PMID 11401542 DOI: 10.1021/Bi010682I |
0.39 |
|
| 2001 |
Huang X, Holden HM, Raushel FM. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annual Review of Biochemistry. 70: 149-80. PMID 11395405 DOI: 10.1146/Annurev.Biochem.70.1.149 |
0.468 |
|
| 2001 |
Hill CM, Li WS, Cheng TC, DeFrank JJ, Raushel FM. Stereochemical specificity of organophosphorus acid anhydrolase toward p-nitrophenyl analogs of soman and sarin. Bioorganic Chemistry. 29: 27-35. PMID 11300693 DOI: 10.1006/Bioo.2000.1189 |
0.605 |
|
| 2001 |
Benning MM, Shim H, Raushel FM, Holden HM. High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta. Biochemistry. 40: 2712-22. PMID 11258882 DOI: 10.1021/Bi002661E |
0.554 |
|
| 2001 |
Chen-Goodspeed M, Sogorb MA, Wu F, Raushel FM. Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues. Biochemistry. 40: 1332-9. PMID 11170460 DOI: 10.1021/Bi001549D |
0.817 |
|
| 2001 |
Chen-Goodspeed M, Sogorb MA, Wu F, Hong SB, Raushel FM. Structural determinants of the substrate and stereochemical specificity of phosphotriesterase. Biochemistry. 40: 1325-31. PMID 11170459 DOI: 10.1021/Bi001548L |
0.817 |
|
| 2000 |
Zhu W, Li WS, Raushel FM, Vigh G. Experimental verification of a predicted, previously unseen separation selectivity pattern in the capillary electrophoretic separation of noncharged enantiomers by octakis(2,3-diacetyl-6-sulfato)-gamma-cyclodextrin. Electrophoresis. 21: 3249-56. PMID 11001223 DOI: 10.1002/1522-2683(20000901)21:15<3249::Aid-Elps3249>3.0.Co;2-C |
0.551 |
|
| 2000 |
Huang X, Raushel FM. Restricted passage of reaction intermediates through the ammonia tunnel of carbamoyl phosphate synthetase. The Journal of Biological Chemistry. 275: 26233-40. PMID 10950966 DOI: 10.1074/Jbc.275.34.26233 |
0.464 |
|
| 2000 |
Healy VL, Mullins LS, Li X, Hall SE, Raushel FM, Walsh CT. D-Ala-D-X ligases: evaluation of D-alanyl phosphate intermediate by MIX, PIX and rapid quench studies. Chemistry & Biology. 7: 505-14. PMID 10903933 DOI: 10.1016/S1074-5521(00)00135-6 |
0.324 |
|
| 2000 |
Huang X, Raushel FM. Role of the hinge loop linking the N- and C-terminal domains of the amidotransferase subunit of carbamoyl phosphate synthetase. Archives of Biochemistry and Biophysics. 380: 174-80. PMID 10900147 DOI: 10.1006/Abbi.2000.1913 |
0.44 |
|
| 2000 |
Benning MM, Hong SB, Raushel FM, Holden HM. The binding of substrate analogs to phosphotriesterase. The Journal of Biological Chemistry. 275: 30556-60. PMID 10871616 DOI: 10.1074/Jbc.M003852200 |
0.458 |
|
| 2000 |
Hill CM, Wu F, Cheng TC, DeFrank JJ, Raushel FM. Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters. Bioorganic & Medicinal Chemistry Letters. 10: 1285-8. PMID 10866401 DOI: 10.1016/S0960-894X(00)00213-4 |
0.458 |
|
| 2000 |
Shim H, Raushel FM. Self-assembly of the binuclear metal center of phosphotriesterase. Biochemistry. 39: 7357-64. PMID 10858282 DOI: 10.1021/Bi000291O |
0.571 |
|
| 2000 |
Miles BW, Raushel FM. Synchronization of the three reaction centers within carbamoyl phosphate synthetase. Biochemistry. 39: 5051-6. PMID 10819970 DOI: 10.1021/Bi992772H |
0.396 |
|
| 2000 |
Raushel FM, Holden HM. Phosphotriesterase: an enzyme in search of its natural substrate. Advances in Enzymology and Related Areas of Molecular Biology. 74: 51-93. PMID 10800593 DOI: 10.1002/9780470123201.Ch2 |
0.488 |
|
| 2000 |
Huang X, Raushel FM. An engineered blockage within the ammonia tunnel of carbamoyl phosphate synthetase prevents the use of glutamine as a substrate but not ammonia. Biochemistry. 39: 3240-7. PMID 10727215 DOI: 10.1021/Bi9926173 |
0.484 |
|
| 2000 |
Javid-Majd F, Mullins LS, Raushel FM, Stapleton MA. The differentially conserved residues of carbamoyl-phosphate synthetase. The Journal of Biological Chemistry. 275: 5073-80. PMID 10671550 DOI: 10.1074/Jbc.275.7.5073 |
0.375 |
|
| 2000 |
Wu F, Li WS, Chen-Goodspeed M, Sogorb MA, Raushel FM. Rationally engineered mutants of phosphotriesterase for preparative scale isolation of chiral organophosphates [1] Journal of the American Chemical Society. 122: 10206-10207. DOI: 10.1021/Ja002546R |
0.829 |
|
| 1999 |
Holden HM, Thoden JB, Raushel FM. Carbamoyl phosphate synthetase: an amazing biochemical odyssey from substrate to product. Cellular and Molecular Life Sciences : Cmls. 56: 507-22. PMID 11212301 DOI: 10.1007/S000180050448 |
0.427 |
|
| 1999 |
Huang X, Raushel FM. Deconstruction of the catalytic array within the amidotransferase subunit of carbamoyl phosphate synthetase. Biochemistry. 38: 15909-14. PMID 10625457 DOI: 10.1021/Bi991805Q |
0.48 |
|
| 1999 |
Thoden JB, Huang X, Raushel FM, Holden HM. The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway. Biochemistry. 38: 16158-66. PMID 10587438 DOI: 10.1021/Bi991741J |
0.457 |
|
| 1999 |
Thoden JB, Raushel FM, Wesenberg G, Holden HM. The binding of inosine monophosphate to Escherichia coli carbamoyl phosphate synthetase. The Journal of Biological Chemistry. 274: 22502-7. PMID 10428826 DOI: 10.1074/Jbc.274.32.22502 |
0.473 |
|
| 1999 |
Hong SB, Raushel FM. Stereochemical preferences for chiral substrates by the bacterial phosphotriesterase. Chemico-Biological Interactions. 119: 225-34. PMID 10421456 DOI: 10.1016/S0009-2797(99)00031-9 |
0.507 |
|
| 1999 |
Raushel FM, Thoden JB, Holden HM. The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia. Biochemistry. 38: 7891-9. PMID 10387030 DOI: 10.1021/Bi990871P |
0.503 |
|
| 1999 |
Thoden JB, Raushel FM, Benning MM, Rayment I, Holden HM. The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution. Acta Crystallographica. Section D, Biological Crystallography. 55: 8-24. PMID 10089390 DOI: 10.1107/S0907444998006234 |
0.439 |
|
| 1999 |
Thoden JB, Wesenberg G, Raushel FM, Holden HM. Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding. Biochemistry. 38: 2347-57. PMID 10029528 DOI: 10.1021/Bi982517H |
0.441 |
|
| 1999 |
Braxton BL, Mullins LS, Raushel FM, Reinhart GD. Allosteric dominance in carbamoyl phosphate synthetase. Biochemistry. 38: 1394-401. PMID 9931004 DOI: 10.1021/Bi982097W |
0.398 |
|
| 1999 |
Hong SB, Raushel FM. Stereochemical constraints on the substrate specificity of phosphotriesterase. Biochemistry. 38: 1159-65. PMID 9930975 DOI: 10.1021/Bi982204M |
0.484 |
|
| 1999 |
Hong SB, Raushel FM. Stereochemical constraints on the catalytic hydrolysis of organophosphate nerve agents by phosphotriesterase Phosphorus, Sulfur and Silicon and Related Elements. 144: 521-524. DOI: 10.1080/10426509908546296 |
0.506 |
|
| 1999 |
Mullins LS, Raushel FM. Channeling of ammonia through the intermolecular tunnel contained within carbamoyl phosphate synthetase [13] Journal of the American Chemical Society. 121: 3803-3804. DOI: 10.1021/Ja990063L |
0.382 |
|
| 1999 |
Chen-Goodspeed M, Vanhooke JL, Holden HM, Raushel FM. Kinetic mechanism of kanamycin nucleotidyltransferase from Staphylococcus aureus Bioorganic Chemistry. 27: 395-408. DOI: 10.1006/Bioo.1999.1144 |
0.8 |
|
| 1998 |
Holden HM, Thoden JB, Raushel FM. Carbamoyl phosphate synthetase: a tunnel runs through it. Current Opinion in Structural Biology. 8: 679-85. PMID 9914247 DOI: 10.1016/S0959-440X(98)80086-9 |
0.425 |
|
| 1998 |
Miles BW, Banzon JA, Raushel FM. Regulatory control of the amidotransferase domain of carbamoyl phosphate synthetase. Biochemistry. 37: 16773-9. PMID 9843448 DOI: 10.1021/Bi982018G |
0.433 |
|
| 1998 |
Raushel FM, Thodent JB, Reinhart GD, Holden HM. Carbamoyl phosphate synthetase: A crooked path from substrates to products Current Opinion in Chemical Biology. 2: 624-632. PMID 9818189 DOI: 10.1016/S1367-5931(98)80094-X |
0.485 |
|
| 1998 |
Raushel FM, Mullins LS, Gibson GE. A stringent test for the nucleotide switch mechanism of carbamoyl phosphate synthetase. Biochemistry. 37: 10272-8. PMID 9665735 DOI: 10.1021/Bi980753M |
0.413 |
|
| 1998 |
Shim H, Hong SB, Raushel FM. Hydrolysis of phosphodiesters through transformation of the bacterial phosphotriesterase. The Journal of Biological Chemistry. 273: 17445-50. PMID 9651332 DOI: 10.1074/Jbc.273.28.17445 |
0.685 |
|
| 1998 |
Thoden JB, Miran SG, Phillips JC, Howard AJ, Raushel FM, Holden HM. Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis. Biochemistry. 37: 8825-31. PMID 9636022 DOI: 10.1021/Bi9807761 |
0.482 |
|
| 1998 |
Francisco WA, Abu-Soud HM, DelMonte AJ, Singleton DA, Baldwin TO, Raushel FM. Deuterium kinetic isotope effects and the mechanism of the bacterial luciferase reaction Biochemistry. 37: 2596-2606. PMID 9485410 DOI: 10.1021/Bi972266X |
0.361 |
|
| 1998 |
Gibson GE, Mullins LS, Raushel FM. Carbamoyl phosphate synthetase from Escherichia coil does not catalyze the dehydration of bicarbonate to carbon dioxide Bioorganic Chemistry. 26: 255-268. DOI: 10.1006/Bioo.1998.1103 |
0.411 |
|
| 1997 |
Watkins LM, Kuo JM, Chen-Goodspeed M, Raushel FM. A combinatorial library for the binuclear metal center of bacterial phosphotriesterase Proteins: Structure, Function and Genetics. 29: 553-561. PMID 9408951 DOI: 10.1002/(Sici)1097-0134(199712)29:4<553::Aid-Prot14>3.0.Co;2-L |
0.814 |
|
| 1997 |
Watkins LM, Mahoney HJ, McCulloch JK, Raushel FM. Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase Journal of Biological Chemistry. 272: 25596-25601. PMID 9325279 DOI: 10.1074/Jbc.272.41.25596 |
0.421 |
|
| 1997 |
Hong SB, Raushel FM. Inhibitors directed towards the binuclear metal center of phosphotriesterase Journal of Enzyme Inhibition. 12: 191-203. PMID 9314115 DOI: 10.3109/14756369709029314 |
0.438 |
|
| 1997 |
Mullins LS, Pace CN, Raushel FM. Conformational stability of ribonuclease T1 determined by hydrogen- deuterium exchange Protein Science. 6: 1387-1395. PMID 9232639 DOI: 10.1002/Pro.5560060702 |
0.314 |
|
| 1997 |
Hong SB, Mullins LS, Shim H, Raushel FM. Mechanism-based inhibitors for the inactivation of the bacterial phosphotriesterase. Biochemistry. 36: 9022-8. PMID 9220990 DOI: 10.1021/Bi970680R |
0.647 |
|
| 1997 |
Abu-Soud HM, Gachhui R, Raushel FM, Stuehr DJ. The ferrous-dioxy complex of neuronal nitric oxide synthase: Divergent effects of L-arginine and tetrahydrobiopterin on its stability Journal of Biological Chemistry. 272: 17349-17353. PMID 9211873 DOI: 10.1074/Jbc.272.28.17349 |
0.3 |
|
| 1997 |
Thoden JB, Holden HM, Wesenberg G, Raushel FM, Rayment I. Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product. Biochemistry. 36: 6305-16. PMID 9174345 DOI: 10.1021/Bi970503Q |
0.462 |
|
| 1997 |
Kuo JM, Chae MY, Raushel FM. Perturbations to the active site of phosphotriesterase Biochemistry. 36: 1982-1988. PMID 9047295 DOI: 10.1021/Bi962099L |
0.478 |
|
| 1997 |
Mullins LS, Hong SB, Gibson GE, Walker H, Stadtman TC, Raushel FM. Identification of a phosphorylated enzyme intermediate in the catalytic mechanism for selenophosphate synthetase Journal of the American Chemical Society. 119: 6684-6685. DOI: 10.1021/Ja971074M |
0.452 |
|
| 1996 |
Javid-Majd F, Stapleton MA, Harmon MF, Hanks BA, Mullins LS, Raushel FM. Comparison of the functional differences for the homologous residues within the carboxy phosphate and carbamate domains of carbamoyl phosphate synthetase Biochemistry. 35: 14362-14369. PMID 8916923 DOI: 10.1021/Bi961184Q |
0.407 |
|
| 1996 |
Stapleton MA, Javid-Majd F, Harmon MF, Hanks BA, Grahmann JL, Mullins LS, Raushel FM. Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase Biochemistry. 35: 14352-14361. PMID 8916922 DOI: 10.1021/Bi961183Y |
0.411 |
|
| 1996 |
Braxton BL, Mullins LS, Raushel FM, Reinhart GD. Allosteric effects of carbamoyl phosphate synthetase from Escherichia coli are entropy-driven Biochemistry. 35: 11918-11924. PMID 8794775 DOI: 10.1021/Bi961305M |
0.33 |
|
| 1996 |
Johnson JL, Raushel FM. Influence of primary sequence transpositions on the folding pathways of ribonuclease T1 Biochemistry. 35: 10223-10233. PMID 8756488 DOI: 10.1021/Bi953026P |
0.32 |
|
| 1996 |
Garrett JB, Mullins LS, Raushel FM. Are turns required for the folding of ribonuclease T1? Protein Science. 5: 204-211. PMID 8745397 DOI: 10.1002/Pro.5560050203 |
0.334 |
|
| 1996 |
Hong SB, Raushel FM. Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase Biochemistry. 35: 10904-10912. PMID 8718883 DOI: 10.1021/Bi960663M |
0.491 |
|
| 1996 |
Vanhooke JL, Benning MM, Raushel FM, Holden HM. Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate Biochemistry. 35: 6020-6025. PMID 8634243 DOI: 10.1021/Bi960325L |
0.495 |
|
| 1995 |
Thoden JB, Raushel FM, Mareya S, Tomchick D, Rayment I. Crystallization and preliminary X-ray crystallographic analysis of carbamoyl phosphate synthetase from Escherichia coli. Acta Crystallographica. Section D, Biological Crystallography. 51: 827-9. PMID 15299816 DOI: 10.1107/S0907444994012801 |
0.336 |
|
| 1995 |
Baldwin TO, Christopher JA, Raushel FM, Sinclair JF, Ziegler MM, Fisher AJ, Rayment I. Structure of bacterial luciferase. Current Opinion in Structural Biology. 5: 798-809. PMID 8749369 DOI: 10.1016/0959-440X(95)80014-X |
0.384 |
|
| 1995 |
Chae MY, Omburo GA, Lindahl PA, Raushel FM. Utilization of copper as a paramagnetic probe for the binuclear metal center of phosphotriesterase Archives of Biochemistry and Biophysics. 316: 765-772. PMID 7864632 DOI: 10.1006/Abbi.1995.1102 |
0.329 |
|
| 1995 |
Banzon JA, Kuo JM, Fischer DR, Stang PJ, Raushel FM. Histidine-254 is essential for the inactivation of phosphotriesterase with the alkynyl phosphate esters and diethyl pyrocarbonate. Biochemistry. 34: 750-4. PMID 7827033 DOI: 10.1021/Bi00003A007 |
0.413 |
|
| 1995 |
Banzon JA, Kuo JM, Miles BW, Fischer DR, Stang PJ, Raushel FM. Mechanism-based inactivation of phosphotriesterase by reaction of a critical histidine with a ketene intermediate. Biochemistry. 34: 743-9. PMID 7827032 DOI: 10.1021/Bi00003A006 |
0.505 |
|
| 1995 |
Benning MM, Kuo JM, Raushel FM, Holden HM. Three-dimensional structure of the binuclear metal center of phosphotriesterase Biochemistry. 34: 7973-7978. PMID 7794910 DOI: 10.1021/Bi00025A002 |
0.36 |
|
| 1995 |
Mullins LS, Raushel FM. Positional isotope exchange as probe of enzyme action Methods in Enzymology. 249: 398-425. PMID 7791621 DOI: 10.1016/0076-6879(95)49043-4 |
0.319 |
|
| 1995 |
Fisher AJ, Raushel FM, Baldwin TO, Rayment I. Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 A resolution. Biochemistry. 34: 6581-6. PMID 7756289 DOI: 10.1021/Bi00020A002 |
0.375 |
|
| 1995 |
Mareya SM, Raushel FM. Mapping the structural domains of E. coli carbamoyl phosphate synthetase using limited proteolysis. Bioorganic & Medicinal Chemistry. 3: 525-32. PMID 7648201 DOI: 10.1016/0968-0896(95)00042-F |
0.406 |
|
| 1995 |
Czerwinski RM, Mareya SM, Raushel FM. Regulatory changes in the control of carbamoyl phosphate synthetase induced by truncation and mutagenesis of the allosteric binding domain Biochemistry. 34: 13920-13927. PMID 7577987 DOI: 10.1021/Bi00042A025 |
0.419 |
|
| 1995 |
Kuo JM, Mullins LS, Garrett JB, Raushel FM. Circular permutation of RNase T1 through PCR based site-directed mutagenesis Techniques in Protein Chemistry. 6: 333-340. DOI: 10.1016/S1080-8914(06)80041-4 |
0.347 |
|
| 1995 |
Mullins LS, Chae MY, Raushel FM. Phosphorus-31 NMR relaxation studies of diethyl P-methoxyphenyl phosphate bound to phosphotriesterase Bioorganic and Medicinal Chemistry Letters. 5: 3067-3072. DOI: 10.1016/0960-894X(95)00539-7 |
0.306 |
|
| 1994 |
Kuo JM, Raushel FM. Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis. Biochemistry. 33: 4265-72. PMID 8155644 DOI: 10.1021/Bi00180A022 |
0.478 |
|
| 1994 |
Mareya SM, Raushel FM. A molecular wedge for triggering the amidotransferase activity of carbamoyl phosphate synthetase. Biochemistry. 33: 2945-50. PMID 8130208 DOI: 10.1021/Bi00176A026 |
0.463 |
|
| 1994 |
Pei L, Omburo G, McGuinn WD, Petrikovics I, Dave K, Raushel FM, Wild JR, DeLoach JR, Way JL. Encapsulation of phosphotriesterase within murine erythrocytes. Toxicology and Applied Pharmacology. 124: 296-301. PMID 8122276 DOI: 10.1006/Taap.1994.1035 |
0.445 |
|
| 1994 |
Benning MM, Kuo JM, Raushel FM, Holden HM. Three-dimensional structure of phosphotriesterase: An enzyme capable of detoxifying organophosphate nerve agents Biochemistry. 33: 15001-15007. PMID 7999757 DOI: 10.1021/Bi00254A008 |
0.419 |
|
| 1994 |
Hong S, Raushel FM. Synthesis and enzymatic hydrolysis of a light-emitting substrate for phosphotriesterase Bioorganic & Medicinal Chemistry Letters. 4: 2705-2708. DOI: 10.1016/S0960-894X(01)80701-0 |
0.391 |
|
| 1994 |
Chae MY, Postula JF, Raushel FM. Stereospcific enzymatic hydrolysis of phosphorus-sulfur bonds in chiral organophosphate triesters Bioorganic and Medicinal Chemistry Letters. 4: 1473-1478. DOI: 10.1016/S0960-894X(01)80516-3 |
0.355 |
|
| 1993 |
RodrÃguez EJ, Debouck C, Deckman IC, Abu-Soud H, Raushel FM, Meek TD. Inhibitor binding to the Phe53Trp mutant of HIV-1 protease promotes conformational changes detectable by spectrofluorometry. Biochemistry. 32: 3557-63. PMID 8466899 DOI: 10.1021/Bi00065A006 |
0.365 |
|
| 1993 |
Rajapaksa R, Abu-Soud H, Raushel FM, Harris BG, Cook PF. Pre-steady-state kinetics reveal a slow isomerization of the enzyme-NAD complex in the NAD-malic enzyme reaction. Biochemistry. 32: 1928-34. PMID 8448150 DOI: 10.1021/Bi00059A007 |
0.452 |
|
| 1993 |
Miles BW, Mareya SM, Post LE, Post DJ, Sun Hee Chang, Raushel FM. Differential roles for three conserved histidine residues within the large subunit of carbamoyl phosphate synthetase Biochemistry. 32: 232-240. PMID 8418843 DOI: 10.1021/Bi00052A030 |
0.484 |
|
| 1993 |
Omburo GA, Mullins LS, Raushel FM. Structural characterization of the divalent cation sites of bacterial phosphotriesterase by 113Cd NMR spectroscopy. Biochemistry. 32: 9148-55. PMID 8396425 DOI: 10.1021/Bi00086A021 |
0.438 |
|
| 1993 |
Chae MY, Omburo GA, Lindahl PA, Raushel FM. Antiferromagnetic coupling in the binuclear metal cluster of manganese-substituted phosphotriesterase Journal of the American Chemical Society. 115: 12173-12174. DOI: 10.1021/Ja00078A069 |
0.39 |
|
| 1992 |
Abu-Soud H, Mullins LS, Baldwin TO, Raushel FM. Stopped-flow kinetic analysis of the bacterial luciferase reaction Biochemistry. 31: 3807-3813. PMID 1567836 DOI: 10.1021/Bi00130A011 |
0.354 |
|
| 1992 |
Braxton BL, Mullins LS, Raushel FM, Reinhart GD. Quantifying the allosteric properties of Escherichia coli carbamyl phosphate synthetase: Determination of thermodynamic linked-function parameters in an ordered kinetic mechanism Biochemistry. 31: 2309-2316. PMID 1531767 DOI: 10.1021/Bi00123A015 |
0.395 |
|
| 1992 |
Raushel FM, Miles BW, Post LE, David J. P. Mutational analysis of two putative domains within the large subunit of carbamoyl phosphate synthetase from escherichia coli Bioorganic and Medicinal Chemistry Letters. 2: 319-322. DOI: 10.1016/S0960-894X(01)80209-2 |
0.344 |
|
| 1991 |
Caldwell SR, Raushel FM. Detoxification of organophosphate pesticides using an immobilized phosphotriesterase from Pseudomonas diminuta. Biotechnology and Bioengineering. 37: 103-9. PMID 18597346 DOI: 10.1002/Bit.260370203 |
0.469 |
|
| 1991 |
Miran SG, Chang SH, Raushel FM. Role of the four conserved histidine residues in the amidotransferase domain of carbamoyl phosphate synthetase. Biochemistry. 30: 7901-7. PMID 1868065 DOI: 10.1021/Bi00246A005 |
0.487 |
|
| 1991 |
Caldwell SR, Raushel FM. Detoxification of organophosphate pesticides using a nylon based immobilized phosphotriesterase from Pseudomonas diminuta. Applied Biochemistry and Biotechnology. 31: 59-73. PMID 1665681 DOI: 10.1007/Bf02922126 |
0.454 |
|
| 1991 |
Caldwell SR, Raushel FM, Weiss PM, Cleland WW. Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis. Biochemistry. 30: 7444-50. PMID 1649629 DOI: 10.1021/Bi00244A011 |
0.527 |
|
| 1991 |
Caldwell SR, Newcomb JR, Schlecht KA, Raushel FM. Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Biochemistry. 30: 7438-44. PMID 1649628 DOI: 10.1021/Bi00244A010 |
0.392 |
|
| 1991 |
Blankenship JN, Abu-Soud H, Francisco WA, Raushel FM, Fischer DR, Stang PJ. Mechanism-based inactivation of a bacterial phosphotriesterase by an alkynyl phosphate ester Journal of the American Chemical Society. 113: 8560-8561. DOI: 10.1021/Ja00022A074 |
0.333 |
|
| 1991 |
Caldwell SR, Raushel FM, Weiss PM, Cleland WW. Primary and secondary oxygen-18 isotope effects in the alkaline and enzyme-catalyzed hydrolysis of phosphotriesters Journal of the American Chemical Society. 113: 730-732. DOI: 10.1021/Ja00002A083 |
0.602 |
|
| 1990 |
Dumas DP, Durst HD, Landis WG, Raushel FM, Wild JR. Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta Archives of Biochemistry and Biophysics. 277: 155-159. PMID 2154956 DOI: 10.1016/0003-9861(90)90564-F |
0.502 |
|
| 1989 |
Kim SC, Raushel FM. The interaction of monofluorofumarate with adenylosuccinate lyase. Journal of Enzyme Inhibition. 2: 153-61. PMID 3241180 DOI: 10.3109/14756368809040721 |
0.4 |
|
| 1989 |
Kim SC, Raushel FM. Mechanism-based inactivation of rabbit muscle phosphoglucomutase by nojirimycin 6-phosphate. Biochemistry. 27: 7328-32. PMID 2974722 DOI: 10.1021/Bi00419A022 |
0.343 |
|
| 1989 |
Donarski WJ, Dumas DP, Heitmeyer DP, Lewis VE, Raushel FM. Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Biochemistry. 28: 4650-5. PMID 2548585 DOI: 10.1021/Bi00437A021 |
0.477 |
|
| 1988 |
Raushel FM, Villafranca JJ. Positional isotope exchange. Crc Critical Reviews in Biochemistry. 23: 1-26. PMID 3284712 |
0.557 |
|
| 1988 |
Kim SC, Singh AN, Raushel FM. Analysis of the galactosyltransferase reaction by positional isotope exchange and secondary deuterium isotope effects. Archives of Biochemistry and Biophysics. 267: 54-9. PMID 3143309 DOI: 10.1016/0003-9861(88)90007-0 |
0.346 |
|
| 1988 |
Lewis VE, Donarski WJ, Wild JR, Raushel FM. Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase. Biochemistry. 27: 1591-7. PMID 2835095 DOI: 10.1021/Bi00405A030 |
0.394 |
|
| 1988 |
Scholten JD, Hogg JL, Raushel FM. Methyl chymotrypsin catalyzed hydrolyses of specific substrate esters indicate multiple proton catalysis is possible with a modified charge relay triad Journal of the American Chemical Society. 110: 8246-8247. DOI: 10.1021/Ja00232A053 |
0.36 |
|
| 1988 |
Singh AN, Newborn J, Raushel FM. Enzymatic synthesis of uridine-5′-O-(2-thiodiphosphoglucose) and related sugar phosphorothioates Bioorganic Chemistry. 16: 206-214. DOI: 10.1016/0045-2068(88)90009-0 |
0.327 |
|
| 1987 |
Mallis LM, Raushel FM, Russell DH. Differentiation of isotopically labeled nucleotides using fast atom bombardment tandem mass spectrometry. Analytical Chemistry. 59: 980-4. PMID 3592217 DOI: 10.1021/Ac00134A012 |
0.321 |
|
| 1987 |
Hester LS, Raushel FM. Determination of the energetics of the UDP-glucose pyrophosphorylase reaction by positional isotope exchange inhibition Biochemistry. 26: 6465-6471. PMID 2827728 DOI: 10.1021/Bi00394A026 |
0.382 |
|
| 1987 |
Matos J, Raushel F, Wong C. S-adenosylmethionine: studies on chemical and enzymatic synthesis. Biotechnology and Applied Biochemistry. 9: 39-52. DOI: 10.1111/J.1470-8744.1987.Tb00461.X |
0.391 |
|
| 1986 |
Kim SC, Raushel FM. Isotopic probes of the argininosuccinate lyase reaction. Biochemistry. 25: 4744-9. PMID 3768310 DOI: 10.1021/Bi00365A004 |
0.402 |
|
| 1986 |
Chapman TL, Shull TB, Raushel FM. Stereochemical probes of the argininosuccinate synthetase reaction. Biochemistry. 25: 4739-44. PMID 3768309 DOI: 10.1021/Bi00365A003 |
0.391 |
|
| 1986 |
Hilscher LW, Hanson CD, Russell DH, Raushel FM. Measurement of positional isotope exchange rates in enzyme-catalyzed reactions by fast atom bombardment mass spectrometry: application to argininosuccinate synthetase. Biochemistry. 24: 5888-93. PMID 2867775 DOI: 10.1021/Bi00342A030 |
0.406 |
|
| 1985 |
Ghose C, Raushel FM. Determination of the mechanism of the argininosuccinate synthetase reaction by static and dynamic quench experiments Biochemistry. 24: 5894-5898. PMID 3878725 DOI: 10.1021/Bi00342A031 |
0.415 |
|
| 1984 |
Raushel FM, Garrard LJ. A positional isotope exchange study of the argininosuccinate lyase reaction. Biochemistry. 23: 1791-5. PMID 6722123 DOI: 10.1021/Bi00303A032 |
0.395 |
|
| 1984 |
Raushel FM. Nitro analogs of substrates for argininosuccinate synthetase and argininosuccinate lyase. Archives of Biochemistry and Biophysics. 232: 520-5. PMID 6547814 DOI: 10.1016/0003-9861(84)90569-1 |
0.451 |
|
| 1983 |
Raushel FM, Nygaard R. Kinetic mechanism of bovine liver argininosuccinate lyase. Archives of Biochemistry and Biophysics. 221: 143-7. PMID 6830252 DOI: 10.1016/0003-9861(83)90130-3 |
0.313 |
|
| 1983 |
Garrard LJ, Mathis JM, Raushel FM. Substrate-induced inactivation of argininosuccinate lyase by monofluorofumarate and difluorofumarate Biochemistry. 22: 3729-3735. PMID 6615795 DOI: 10.1021/bi00285a002 |
0.365 |
|
| 1983 |
Raushel FM, Seiglie JL. Kinetic mechanism of argininosuccinate synthetase. Archives of Biochemistry and Biophysics. 225: 979-85. PMID 6605113 DOI: 10.1016/0003-9861(83)90114-5 |
0.354 |
|
| 1983 |
Raushel FM, Anderson PM, Villafranca JJ. A nuclear magnetic resonance study of the topography of binding sites of Escherichia coli carbamoyl-phosphate synthetase. Biochemistry. 22: 1872-6. PMID 6342670 DOI: 10.1021/Bi00277A020 |
0.626 |
|
| 1982 |
Villafranca JJ, Raushel FM. The monovalent cation site of pyruvate kinase and other enzymes: NMR investigations. Federation Proceedings. 41: 2961-5. PMID 7140996 |
0.61 |
|
| 1982 |
Viola RE, Raushel FM, Rendina AR, Cleland WW. Substrate synergism and the kinetic mechanism of yeast hexokinase. Biochemistry. 21: 1295-302. PMID 7041974 DOI: 10.1021/Bi00535A029 |
0.725 |
|
| 1981 |
Cunningham BA, Raushel FM, Villafranca JJ, Benkovic SJ. Distances between structural metal ion, substrates, and allosteric modifier of fructose bisphosphatase. Biochemistry. 20: 359-62. PMID 6258638 DOI: 10.1021/Bi00505A020 |
0.635 |
|
| 1980 |
Raushel FM, Villafranca JJ. A multinuclear nuclear magnetic resonance study of the monovalent-divalent cation sites of pyruvate kinase. Biochemistry. 19: 5481-5. PMID 7193048 DOI: 10.1021/Bi00565A003 |
0.656 |
|
| 1980 |
Raushel FM, Villafranca JJ. Phosphorus-31 nuclear magnetic resonance application to positional isotope exchange reactions catalyzed by Escherichia coli carbamoyl-phosphate synthetase: analysis of forward and reverse enzymatic reactions. Biochemistry. 19: 3170-4. PMID 6996701 DOI: 10.1021/Bi00555A009 |
0.586 |
|
| 1980 |
Villafranca JJ, Raushel FM. Biophysical applications of NMR to phosphoryl transfer enzymes and metal nuclei of metalloproteins. Annual Review of Biophysics and Bioengineering. 9: 363-92. PMID 6104944 DOI: 10.1146/annurev.bb.09.060180.002051 |
0.573 |
|
| 1980 |
Pillai RP, Raushel FM, Villafranca JJ. Stereochemistry of binding of thiophosphate analogs of ATP and ADP to carbamate kinase, glutamine synthetase, and carbamoyl-phosphate synthetase. Archives of Biochemistry and Biophysics. 199: 7-15. PMID 6101943 DOI: 10.1016/0003-9861(80)90249-0 |
0.642 |
|
| 1980 |
Raushel FM, Villafranca JJ. A direct NMR method for the determination of correlation times in enzyme complexes involving monovalent cations and paramagnetic centers Journal of the American Chemical Society. 102: 6618-6619. DOI: 10.1021/Ja00541A067 |
0.617 |
|
| 1979 |
Raushel FM, Rawding CJ, Anderson PM, Villafranca JJ. Paramagnetic probes for carbamoyl-phosphate synthetase: metal ion binding studies and preparation of nitroxide spin-labeled derivatives. Biochemistry. 18: 5562-6. PMID 229896 DOI: 10.1021/Bi00592A006 |
0.556 |
|
| 1979 |
Raushel FM, Villafranca JJ. Determination of rate-limiting steps of Escherichia coli carbamoyl-phosphate synthase. Rapid quench and isotope partitioning experiments. Biochemistry. 18: 3424-9. PMID 223631 DOI: 10.1021/Bi00582A033 |
0.598 |
|
| 1978 |
Raushel FM, Anderson PM, Villafranca JJ. Kinetic mechanism of Escherichia coli carbamoyl-phosphate synthetase. Biochemistry. 17: 5587-91. PMID 215204 DOI: 10.1021/Bi00619A001 |
0.642 |
|
| 1978 |
Raushel FM, Anderson PM, Villafranca JJ. Carbamyl phosphate synthetase of Escherichia coli uses the same diastereomer of adenosine-5'-[2-thiotriphosphate] at both ATP sites. The Journal of Biological Chemistry. 253: 6627-9. PMID 211124 |
0.605 |
|
| 1977 |
Raushel FM, Cleland WW. Bovine liver fructokinase: purification and kinetic properties. Biochemistry. 16: 2169-75. PMID 193556 DOI: 10.1021/Bi00629A020 |
0.564 |
|
| 1977 |
Raushel FM, Cleland WW. Determination of the rate-limiting steps and chemical mechanism of fructokinase by isotope exchange, isotope partitioning, and pH studies. Biochemistry. 16: 2176-81. PMID 16640 DOI: 10.1021/Bi00629A021 |
0.609 |
|
| 1973 |
Raushel FM, Cleland WW. The substrate and anomeric specificity of fructokinase. The Journal of Biological Chemistry. 248: 8174-7. PMID 4356621 |
0.535 |
|
| Show low-probability matches. |
