| Year |
Citation |
Score |
| 2020 |
North JA, Wildenthal JA, Erb TJ, Evans BS, Byerly KM, Gerlt JA, Tabita FR. A bifunctional salvage pathway for two distinct S-adenosylmethionine byproducts that is widespread in bacteria, including pathogenic Escherichia coli. Molecular Microbiology. PMID 31950558 DOI: 10.1111/Mmi.14459 |
0.653 |
|
| 2020 |
Stack T, Morrison KN, Dettmer TM, Wille B, Kim C, Joyce R, Jermain M, Naing YT, Bhatti K, San Francisco B, Carter MS, Gerlt JA. Characterization of an L-Ascorbate Catabolic Pathway with Unprecedented Enzymatic Transformations. Journal of the American Chemical Society. PMID 31917558 DOI: 10.1021/Jacs.9B09863 |
0.371 |
|
| 2019 |
Zallot R, Oberg N, Gerlt JA. The EFI Web Resource for Genomic Enzymology Tools: Leveraging Protein, Genome, and Metagenome Databases to Discover Novel Enzymes and Metabolic Pathways. Biochemistry. PMID 31553576 DOI: 10.1021/Acs.Biochem.9B00735 |
0.302 |
|
| 2018 |
Gerlt JA, Erb TJ. Editorial overview: Novel enzymes, coenzymes, and metabolic pathways. Current Opinion in Chemical Biology. 47: A4-A6. PMID 30497880 DOI: 10.1016/J.Cbpa.2018.11.008 |
0.623 |
|
| 2018 |
Reyes AC, Plache DC, Koudelka AP, Amyes TL, Gerlt JA, Richard JP. Enzyme Architecture: Breaking Down the Catalytic Cage that Activates Orotidine 5'-Monophosphate Decarboxylase for Catalysis. Journal of the American Chemical Society. PMID 30475611 DOI: 10.1021/Jacs.8B09609 |
0.358 |
|
| 2018 |
Zallot R, Oberg NO, Gerlt JA. 'Democratized' genomic enzymology web tools for functional assignment. Current Opinion in Chemical Biology. 47: 77-85. PMID 30268904 DOI: 10.1016/J.Cbpa.2018.09.009 |
0.3 |
|
| 2018 |
Bouvier JT, Sernova NV, Ghasempur S, Rodionova IA, Vetting MW, Al-Obaidi NF, Almo SC, Gerlt JA, Rodionov DA. Novel Metabolic Pathways and Regulons for Hexuronate Utilization in Proteobacteria. Journal of Bacteriology. PMID 30249705 DOI: 10.1128/Jb.00431-18 |
0.346 |
|
| 2018 |
Carter MS, Zhang X, Huang H, Bouvier JT, Francisco BS, Vetting MW, Al-Obaidi N, Bonanno JB, Ghosh A, Zallot RG, Andersen HM, Almo SC, Gerlt JA. Functional assignment of multiple catabolic pathways for D-apiose. Nature Chemical Biology. PMID 29867142 DOI: 10.1038/S41589-018-0067-7 |
0.392 |
|
| 2018 |
Calhoun S, Korczynska M, Wichelecki DJ, San Francisco B, Zhao S, Rodionov DA, Vetting MW, Al-Obaidi NF, Lin H, O'Meara MJ, Scott DA, Morris JH, Russel D, Almo SC, Osterman AL, ... Gerlt JA, et al. Prediction of enzymatic pathways by integrative pathway mapping. Elife. 7. PMID 29377793 DOI: 10.7554/Elife.31097 |
0.356 |
|
| 2017 |
Gerlt JA. Genomic Enzymology: Web Tools for Leveraging Protein Family Sequence-Function Space and Genome Context to Discover Novel Functions. Biochemistry. 56: 4293-4308. PMID 28826221 DOI: 10.1021/Acs.Biochem.7B00614 |
0.356 |
|
| 2016 |
Zhang X, Carter MS, Vetting MW, San Francisco B, Zhao S, Al-Obaidi NF, Solbiati JO, Thiaville JJ, de Crécy-Lagard V, Jacobson MP, Almo SC, Gerlt JA. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proceedings of the National Academy of Sciences of the United States of America. PMID 27402745 DOI: 10.1073/Pnas.1605546113 |
0.382 |
|
| 2016 |
Yadava U, Vetting MW, Al Obaidi N, Carter MS, Gerlt JA, Almo SC. Structure of an ABC transporter solute-binding protein specific for the amino sugars glucosamine and galactosamine. Acta Crystallographica. Section F, Structural Biology Communications. 72: 467-472. PMID 27303900 DOI: 10.1107/S2053230X16007500 |
0.325 |
|
| 2016 |
Thiaville JJ, Flood J, Yurgel S, Prunetti L, Elbadawi-Sidhu M, Hutinet G, Forouhar F, Zhang X, Ganesan V, Reddy P, Fiehn O, Gerlt JA, Hunt JF, Copley SD, De Crecy-Lagard V. Members of a novel kinase family (DUF1537) can recycle toxic intermediates into an essential metabolite. Acs Chemical Biology. PMID 27294475 DOI: 10.1021/Acschembio.6B00279 |
0.354 |
|
| 2016 |
Huang H, Carter MS, Vetting MW, Al-Obaidi N, Patskovsky Y, Almo SC, Gerlt JA. Correction to "A General Strategy for the Discovery of Metabolic Pathways: d-Threitol, l-Threitol, and Erythritol Utilization in Mycobacterium smegmatis". Journal of the American Chemical Society. PMID 26978037 DOI: 10.1021/Jacs.6B01906 |
0.322 |
|
| 2016 |
Vetting MW, Bouvier JT, Gerlt JA, Almo SC. Purification, crystallization and structural elucidation of D-galactaro-1,4-lactone cycloisomerase from Agrobacterium tumefaciens involved in pectin degradation. Acta Crystallographica. Section F, Structural Biology Communications. 72: 36-41. PMID 26750482 DOI: 10.1107/S2053230X15023286 |
0.416 |
|
| 2016 |
Gerlt JA. Tools and strategies for discovering novel enzymes and metabolic pathways Perspectives On Science. 9: 24-32. DOI: 10.1016/J.Pisc.2016.07.001 |
0.359 |
|
| 2015 |
Huang H, Carter MS, Vetting MW, Al-Obaidi N, Patskovsky Y, Almo SC, Gerlt JA. A General Strategy for the Discovery of Metabolic Pathways: D-Threitol, L-Threitol, and Erythritol Utilization in Mycobacterium smegmatis. Journal of the American Chemical Society. PMID 26560079 DOI: 10.1021/Jacs.5B08968 |
0.381 |
|
| 2015 |
Wichelecki DJ, Vetting MW, Chou L, Al-Obaidi N, Bouvier JT, Almo SC, Gerlt JA. ABC Transport System Solute Binding Protein-Guided Identification of Novel D-Altritol and Galactitol Catabolic Pathways in Agrobacterium tumefaciencs C58. The Journal of Biological Chemistry. PMID 26472925 DOI: 10.1074/Jbc.M115.686857 |
0.433 |
|
| 2015 |
Goryanova B, Goldman LM, Ming S, Amyes TL, Gerlt JA, Richard JP. Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5'-Monophosphate Decarboxylase. Biochemistry. 54: 4555-64. PMID 26135041 DOI: 10.1021/Acs.Biochem.5B00591 |
0.398 |
|
| 2015 |
Gerlt JA, Bouvier JT, Davidson DB, Imker HJ, Sadkhin B, Slater DR, Whalen KL. Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks. Biochimica Et Biophysica Acta. 1854: 1019-1037. PMID 25900361 DOI: 10.1016/J.Bbapap.2015.04.015 |
0.747 |
|
| 2015 |
Zhang X, Kumar R, Vetting MW, Zhao S, Jacobson MP, Almo SC, Gerlt JA. A unique cis-3-hydroxy-l-proline dehydratase in the enolase superfamily. Journal of the American Chemical Society. 137: 1388-91. PMID 25608448 DOI: 10.1021/Ja5103986 |
0.387 |
|
| 2015 |
Vetting MW, Al-Obaidi N, Zhao S, San Francisco B, Kim J, Wichelecki DJ, Bouvier JT, Solbiati JO, Vu H, Zhang X, Rodionov DA, Love JD, Hillerich BS, Seidel RD, Quinn RJ, ... ... Gerlt JA, et al. Experimental strategies for functional annotation and metabolism discovery: targeted screening of solute binding proteins and unbiased panning of metabolomes. Biochemistry. 54: 909-31. PMID 25540822 DOI: 10.1021/Bi501388Y |
0.323 |
|
| 2015 |
Whalen K, Sadkhin B, Davidson D, Gerlt J. Sequence Similarity Networks for the Protein Universe The Faseb Journal. 29. DOI: 10.1096/Fasebj.29.1_Supplement.573.17 |
0.326 |
|
| 2014 |
Cho K, Evans BS, Wood BM, Kumar R, Erb TJ, Warlick BP, Gerlt JA, Sweedler JV. Integration of untargeted metabolomics with transcriptomics reveals active metabolic pathways. Metabolomics : Official Journal of the Metabolomic Society. 2014. PMID 25705145 DOI: 10.1007/S11306-014-0713-3 |
0.773 |
|
| 2014 |
Desai BJ, Goto Y, Cembran A, Fedorov AA, Almo SC, Gao J, Suga H, Gerlt JA. Investigating the role of a backbone to substrate hydrogen bond in OMP decarboxylase using a site-specific amide to ester substitution. Proceedings of the National Academy of Sciences of the United States of America. 111: 15066-71. PMID 25275007 DOI: 10.1073/Pnas.1411772111 |
0.815 |
|
| 2014 |
Wichelecki DJ, Vendiola JA, Jones AM, Al-Obaidi N, Almo SC, Gerlt JA. Investigating the physiological roles of low-efficiency D-mannonate and D-gluconate dehydratases in the enolase superfamily: pathways for the catabolism of L-gulonate and L-idonate. Biochemistry. 53: 5692-9. PMID 25145794 DOI: 10.1021/Bi500837W |
0.381 |
|
| 2014 |
Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, San Francisco B, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, ... Gerlt JA, et al. Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. Elife. 3. PMID 24980702 DOI: 10.7554/Elife.03275 |
0.55 |
|
| 2014 |
Goldman LM, Amyes TL, Goryanova B, Gerlt JA, Richard JP. Enzyme architecture: Deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5′-monophosphate decarboxylase Journal of the American Chemical Society. 136: 10156-10165. PMID 24958125 DOI: 10.1021/Ja505037V |
0.393 |
|
| 2014 |
Wichelecki DJ, Graff DC, Al-Obaidi N, Almo SC, Gerlt JA. Identification of the in vivo function of the high-efficiency D-mannonate dehydratase in Caulobacter crescentus NA1000 from the enolase superfamily. Biochemistry. 53: 4087-9. PMID 24947666 DOI: 10.1021/Bi500683X |
0.339 |
|
| 2014 |
Groninger-Poe FP, Bouvier JT, Vetting MW, Kalyanaraman C, Kumar R, Almo SC, Jacobson MP, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: galactarate dehydratase III from Agrobacterium tumefaciens C58. Biochemistry. 53: 4192-203. PMID 24926996 DOI: 10.1021/Bi5005377 |
0.412 |
|
| 2014 |
Majumdar S, Lukk T, Solbiati JO, Bauer S, Nair SK, Cronan JE, Gerlt JA. Roles of small laccases from Streptomyces in lignin degradation. Biochemistry. 53: 4047-58. PMID 24870309 DOI: 10.1021/Bi500285T |
0.779 |
|
| 2014 |
Ghasempur S, Eswaramoorthy S, Hillerich BS, Seidel RD, Swaminathan S, Almo SC, Gerlt JA. Discovery of a novel L-lyxonate degradation pathway in Pseudomonas aeruginosa PAO1. Biochemistry. 53: 3357-66. PMID 24831290 DOI: 10.1021/Bi5004298 |
0.388 |
|
| 2014 |
Wichelecki DJ, Balthazor BM, Chau AC, Vetting MW, Fedorov AA, Fedorov EV, Lukk T, Patskovsky YV, Stead MB, Hillerich BS, Seidel RD, Almo SC, Gerlt JA. Discovery of function in the enolase superfamily: D-mannonate and d-gluconate dehydratases in the d-mannonate dehydratase subgroup Biochemistry. 53: 2722-2731. PMID 24697546 DOI: 10.1021/Bi500264P |
0.731 |
|
| 2014 |
Wichelecki DJ, Froese DS, Kopec J, Muniz JR, Yue WW, Gerlt JA. Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ. Biochemistry. 53: 2732-8. PMID 24697329 DOI: 10.1021/Bi500349E |
0.319 |
|
| 2014 |
Kumar R, Zhao S, Vetting MW, Wood BM, Sakai A, Cho K, Solbiati J, Almo SC, Sweedler JV, Jacobson MP, Gerlt JA, Cronan JE. Prediction and biochemical demonstration of a catabolic pathway for the osmoprotectant proline betaine. Mbio. 5: e00933-13. PMID 24520058 DOI: 10.1128/Mbio.00933-13 |
0.734 |
|
| 2014 |
Bouvier JT, Groninger-Poe FP, Vetting M, Almo SC, Gerlt JA. Galactaro δ-lactone isomerase: Lactone isomerization by a member of the amidohydrolase superfamily Biochemistry. 53: 614-616. PMID 24450804 DOI: 10.1021/Bi5000492 |
0.385 |
|
| 2014 |
Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, Francisco BS, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, ... Gerlt JA, et al. Author response: Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks Elife. DOI: 10.7554/Elife.03275.025 |
0.545 |
|
| 2013 |
Zhao S, Kumar R, Sakai A, Vetting MW, Wood BM, Brown S, Bonanno JB, Hillerich BS, Seidel RD, Babbitt PC, Almo SC, Sweedler JV, Gerlt JA, Cronan JE, Jacobson MP. Discovery of new enzymes and metabolic pathways by using structure and genome context. Nature. 502: 698-702. PMID 24056934 DOI: 10.1038/Nature12576 |
0.757 |
|
| 2013 |
Goryanova B, Goldman LM, Amyes TL, Gerlt JA, Richard JP. Role of a guanidinium cation-phosphodianion pair in stabilizing the vinyl carbanion intermediate of orotidine 5′-phosphate decarboxylase-catalyzed reactions Biochemistry. 52: 7500-7511. PMID 24053466 DOI: 10.1021/Bi401117Y |
0.397 |
|
| 2013 |
Kellett WF, Brunk E, Desai BJ, Fedorov AA, Almo SC, Gerlt JA, Rothlisberger U, Richards NG. Computational, structural, and kinetic evidence that Vibrio vulnificus FrsA is not a cofactor-independent pyruvate decarboxylase. Biochemistry. 52: 1842-4. PMID 23452154 DOI: 10.1021/Bi400093Y |
0.801 |
|
| 2012 |
Warlick BPE, Imker HJ, Sriram J, Tabita FR, Gerlt JA. Mechanistic diversity in the RuBisCO superfamily: RuBisCO from rhodospirillum rubrum is not promiscuous for reactions catalyzed by RuBisCO-like proteins Biochemistry. 51: 9470-9479. PMID 23110715 DOI: 10.1021/Bi301311T |
0.777 |
|
| 2012 |
Erb TJ, Evans BS, Cho K, Warlick BP, Sriram J, Wood BM, Imker HJ, Sweedler JV, Tabita FR, Gerlt JA. A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis. Nature Chemical Biology. 8: 926-32. PMID 23042035 DOI: 10.1038/Nchembio.1087 |
0.772 |
|
| 2012 |
Warlick BP, Evans BS, Erb TJ, Ramagopal UA, Sriram J, Imker HJ, Sauder JM, Bonanno JB, Burley SK, Tabita FR, Almo SC, Sweedler JS, Gerlt JA. 1-methylthio-d-xylulose 5-phosphate methylsulfurylase: A novel route to 1-deoxy-d-xylulose 5-phosphate in Rhodospirillum rubrum Biochemistry. 51: 8324-8326. PMID 23035785 DOI: 10.1021/Bi301215G |
0.779 |
|
| 2012 |
Desai BJ, Wood BM, Fedorov AA, Fedorov EV, Goryanova B, Amyes TL, Richard JP, Almo SC, Gerlt JA. Conformational changes in orotidine 5′-monophosphate decarboxylase: A structure-based explanation for how the 5′-phosphate group activates the enzyme Biochemistry. 51: 8665-8678. PMID 23030629 DOI: 10.1021/Bi301188K |
0.811 |
|
| 2012 |
Tsang WY, Wood BM, Wong FM, Wu W, Gerlt JA, Amyes TL, Richard JP. Proton transfer from C-6 of uridine 5′-monophosphate catalyzed by orotidine 5′-monophosphate decarboxylase: Formation and stability of a vinyl carbanion intermediate and the effect of a 5-fluoro substituent Journal of the American Chemical Society. 134: 14580-14594. PMID 22812629 DOI: 10.1021/Ja3058474 |
0.665 |
|
| 2012 |
Amyes TL, Ming SA, Goldman LM, Wood BM, Desai BJ, Gerlt JA, Richard JP. Orotidine 5′-monophosphate decarboxylase: Transition state stabilization from remote protein-phosphodianion interactions Biochemistry. 51: 4630-4632. PMID 22620855 DOI: 10.1021/Bi300585E |
0.804 |
|
| 2012 |
Lukk T, Sakai A, Kalyanaraman C, Brown SD, Imker HJ, Song L, Fedorov AA, Fedorov EV, Toro R, Hillerich B, Seidel R, Patskovsky Y, Vetting MW, Nair SK, Babbitt PC, ... ... Gerlt JA, et al. Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily. Proceedings of the National Academy of Sciences of the United States of America. 109: 4122-7. PMID 22392983 DOI: 10.1073/Pnas.1112081109 |
0.812 |
|
| 2012 |
Gerlt JA, Babbitt PC, Jacobson MP, Almo SC. Divergent evolution in enolase superfamily: strategies for assigning functions. The Journal of Biological Chemistry. 287: 29-34. PMID 22069326 DOI: 10.1074/Jbc.R111.240945 |
0.33 |
|
| 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 |
0.757 |
|
| 2011 |
Iiams V, Desai BJ, Fedorov AA, Fedorov EV, Almo SC, Gerlt JA. Mechanism of the orotidine 5′-monophosphate decarboxylase-catalyzed reaction: Importance of residues in the orotate binding site Biochemistry. 50: 8497-8507. PMID 21870810 DOI: 10.1021/Bi2012355 |
0.808 |
|
| 2011 |
Goryanova B, Amyes TL, Gerlt JA, Richard JP. OMP decarboxylase: Phosphodianion binding energy is used to stabilize a vinyl carbanion intermediate Journal of the American Chemical Society. 133: 6545-6548. PMID 21486036 DOI: 10.1021/Ja201734Z |
0.383 |
|
| 2011 |
Wichelecki DJ, Froese DS, Kopec J, Muniz JR, Yue WW, Gerlt JA. Enzymatic and structural characterization of rTS gamma provides insights into the function of rTS beta. Biochemistry. 53: 2732-2738. DOI: 10.2210/Pdb4A35/Pdb |
0.303 |
|
| 2010 |
Toth K, Amyes TL, Wood BM, Chan K, Gerlt JA, Richard JP. Product deuterium isotope effects for orotidine 5'-monophosphate decarboxylase: effect of changing substrate and enzyme structure on the partitioning of the vinyl carbanion reaction intermediate. Journal of the American Chemical Society. 132: 7018-24. PMID 20441167 DOI: 10.1021/Ja102408K |
0.775 |
|
| 2010 |
Wood BM, Amyes TL, Fedorov AA, Fedorov EV, Shabila A, Almo SC, Richard JP, Gerlt JA. Conformational changes in orotidine 5′-monophosphate decarboxylase: "remote" residues that stabilize the active conformation Biochemistry. 49: 3514-3516. PMID 20369850 DOI: 10.1021/Bi100443A |
0.68 |
|
| 2010 |
Barnett SA, Amyes TL, Wood BM, Gerlt JA, Richard JP. Activation of R235A mutant orotidine 5′-monophosphate decarboxylase by the guanidinium cation: Effective molarity of the cationic side chain of Arg-235 Biochemistry. 49: 824-826. PMID 20050635 DOI: 10.1021/Bi902174Q |
0.651 |
|
| 2009 |
Rakus JF, Kalyanaraman C, Fedorov AA, Fedorov EV, Mills-Groninger FP, Toro R, Bonanno J, Bain K, Sauder JM, Burley SK, Almo SC, Jacobson MP, Gerlt JA. Computation-facilitated assignment of the function in the enolase superfamily: a regiochemically distinct galactarate dehydratase from Oceanobacillus iheyensis . Biochemistry. 48: 11546-58. PMID 19883118 DOI: 10.1021/Bi901731C |
0.831 |
|
| 2009 |
Toth K, Amyes TL, Wood BM, Chan KK, Gerlt JA, Richard JP. An examination of the relationship between active site loop size and thermodynamic activation parameters for orotidine 5'-monophosphate decarboxylase from mesophilic and thermophilic organisms. Biochemistry. 48: 8006-13. PMID 19618917 DOI: 10.1021/Bi901064K |
0.779 |
|
| 2009 |
Gerlt JA. Acetoacetate decarboxylase: Hydrophobics, not electrostatics Nature Chemical Biology. 5: 454-455. PMID 19536104 DOI: 10.1038/Nchembio0709-454 |
0.308 |
|
| 2009 |
Chan KK, Wood BM, Fedorov AA, Fedorov EV, Imker HJ, Amyes TL, Richard JP, Almo SC, Gerlt JA. Mechanism of the orotidine 5′-monophosphate decarboxylase-catalyzed reaction: Evidence for substrate destabilization Biochemistry. 48: 5518-5531. PMID 19435314 DOI: 10.1021/Bi900623R |
0.812 |
|
| 2009 |
Wood BM, Chan KK, Amyes TL, Richard JP, Gerlt JA. Mechanism of the orotidine 5′-monophosphate decarboxylase-catalyzed reaction: Effect of solvent viscosity on kinetic constants Biochemistry. 48: 5510-5517. PMID 19435313 DOI: 10.1021/Bi9006226 |
0.724 |
|
| 2009 |
Gerlt JA, Babbitt PC. Enzyme (re)design: lessons from natural evolution and computation Current Opinion in Chemical Biology. 13: 10-18. PMID 19237310 DOI: 10.1016/J.Cbpa.2009.01.014 |
0.326 |
|
| 2009 |
Sakai A, Fedorov AA, Fedorov EV, Schnoes AM, Glasner ME, Brown S, Rutter ME, Bain K, Chang S, Gheyi T, Sauder JM, Burley SK, Babbitt PC, Almo SC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes. Biochemistry. 48: 1445-53. PMID 19220063 DOI: 10.1021/Bi802277H |
0.656 |
|
| 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, 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 |
0.374 |
|
| 2009 |
Froese DS, Dobson CM, White AP, Wu X, Padovani D, Banerjee R, Haller T, Gerlt JA, Surette MG, Gravel RA. Sleeping beauty mutase (sbm) is expressed and interacts with ygfd in Escherichia coli Microbiological Research. 164: 1-8. PMID 18950999 DOI: 10.1016/J.Micres.2008.08.006 |
0.608 |
|
| 2008 |
Kalyanaraman C, Imker HJ, Fedorov AA, Fedorov EV, Glasner ME, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP. Discovery of a dipeptide epimerase enzymatic function guided by homology modeling and virtual screening. Structure (London, England : 1993). 16: 1668-77. PMID 19000819 DOI: 10.1016/J.Str.2008.08.015 |
0.763 |
|
| 2008 |
Imker HJ, Singh J, Warlick BP, Tabita FR, Gerlt JA. Mechanistic diversity in the RuBisCO superfamily: A novel isomerization reaction catalyzed by the RuBisCO-like protein from Rhodospirillum rubrum Biochemistry. 47: 11171-11173. PMID 18826254 DOI: 10.1021/Bi801685F |
0.803 |
|
| 2008 |
Rakus JF, Fedorov AA, Fedorov EV, Glasner ME, Hubbard BK, Delli JD, Babbitt PC, Almo SC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase Biochemistry. 47: 9944-9954. PMID 18754693 DOI: 10.1021/Bi800914R |
0.823 |
|
| 2008 |
Rea D, Hovington R, Rakus JF, Gerlt JA, Fülöp V, Bugg TDH, Roper DI. Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12 Biochemistry. 47: 9955-9965. PMID 18754683 DOI: 10.1021/Bi800943G |
0.831 |
|
| 2008 |
Chan KK, Fedorov AA, Fedorov EV, Almo SC, Gerlt JA. Structural basis for substrate specificity in phosphate binding (β/α)8-barrels: D-allulose 6-phosphate 3-epimerase from Escherichia coli K-12 Biochemistry. 47: 9608-9617. PMID 18700786 DOI: 10.1021/Bi800821V |
0.694 |
|
| 2008 |
Barnett SA, Amyes TL, Wood BM, Gerlt JA, Richard JP. Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5′-monophosphate decarboxylase: A two-part substrate approach Biochemistry. 47: 7785-7787. PMID 18598058 DOI: 10.1021/Bi800939K |
0.633 |
|
| 2008 |
Amyes TL, Wood BM, Chan K, Gerlt JA, Richard JP. Formation and stability of a vinyl carbanion at the active site of orotidine 5′-monophosphate decarboxylase: pKa of the C-6 proton of enzyme-bound UMP Journal of the American Chemical Society. 130: 1574-1575. PMID 18186641 DOI: 10.1021/Ja710384T |
0.755 |
|
| 2007 |
Vick JE, Gerlt JA. Evolutionary potential of (beta/alpha)8-barrels: stepwise evolution of a "new" reaction in the enolase superfamily. Biochemistry. 46: 14589-97. PMID 18020459 DOI: 10.1021/Bi7019063 |
0.825 |
|
| 2007 |
Gerlt JA. A Protein Structure (or Function ?) Initiative Structure. 15: 1353-1356. PMID 17997960 DOI: 10.1016/J.Str.2007.10.003 |
0.422 |
|
| 2007 |
Rakus JF, Fedorov AA, Fedorov EV, Glasner ME, Vick JE, Babbitt PC, Almo SC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans. Biochemistry. 46: 12896-908. PMID 17944491 DOI: 10.1021/Bi701703W |
0.798 |
|
| 2007 |
Toth K, Amyes TL, Wood BM, Chan K, Gerlt JA, Richard JP. Product deuterium isotope effect for orotidine 5'-monophosphate decarboxylase: evidence for the existence of a short-lived carbanion intermediate. Journal of the American Chemical Society. 129: 12946-7. PMID 17918849 DOI: 10.1021/Ja076222F |
0.751 |
|
| 2007 |
Wen SY, Fedorov AA, Fedorov EV, Almo SC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2 Biochemistry. 46: 9564-9577. PMID 17649980 DOI: 10.1021/Bi7008882 |
0.414 |
|
| 2007 |
Song L, Kalyanaraman C, Fedorov AA, Fedorov EV, Glasner ME, Brown S, Imker HJ, Babbitt PC, Almo SC, Jacobson MP, Gerlt JA. Prediction and assignment of function for a divergent N-succinyl amino acid racemase. Nature Chemical Biology. 3: 486-91. PMID 17603539 DOI: 10.1038/Nchembio.2007.11 |
0.75 |
|
| 2007 |
Imker HJ, Fedorov AA, Fedorov EV, Almo SC, Gerlt JA. Mechanistic diversity in the RuBisCO superfamily: The "enolase" in the methionine salvage pathway in Geobacillus kaustophilus Biochemistry. 46: 4077-4089. PMID 17352497 DOI: 10.1021/Bi7000483 |
0.808 |
|
| 2007 |
Fedorov A, Imker H, Fedorov E, Gerlt J, Almo S. The enolase in the methionine salvage pathway: crystal structure and function Acta Crystallographica Section a Foundations of Crystallography. 63: s120-s121. DOI: 10.1107/S0108767307097395 |
0.7 |
|
| 2006 |
Yew WS, Fedorov AA, Fedorov EV, Wood BM, Almo SC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: D-tartrate dehydratase from Bradyrhizobium japonicum Biochemistry. 45: 14598-14608. PMID 17144653 DOI: 10.1021/Bi061688G |
0.813 |
|
| 2006 |
Yew WS, Fedorov AA, Fedorov EV, Rakus JF, Pierce RW, Almo SC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris Biochemistry. 45: 14582-14597. PMID 17144652 DOI: 10.1021/Bi061687O |
0.811 |
|
| 2006 |
Glasner ME, Gerlt JA, Babbitt PC. Evolution of enzyme superfamilies Current Opinion in Chemical Biology. 10: 492-497. PMID 16935022 DOI: 10.1016/J.Cbpa.2006.08.012 |
0.451 |
|
| 2006 |
Glasner ME, Fayazmanesh N, Chiang RA, Sakai A, Jacobson MP, Gerlt JA, Babbitt PC. Evolution of Structure and Function in the o-Succinylbenzoate Synthase/N-Acylamino Acid Racemase Family of the Enolase Superfamily Journal of Molecular Biology. 360: 228-250. PMID 16740275 DOI: 10.1016/J.Jmb.2006.04.055 |
0.6 |
|
| 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 |
0.793 |
|
| 2006 |
Brown SD, Gerlt JA, Seffernick JL, Babbitt P. A gold standard set of mechanistically diverse enzyme superfamilies Genome Biology. 7. PMID 16507141 DOI: 10.1186/Gb-2006-7-1-R8 |
0.304 |
|
| 2006 |
Akana J, Fedorov AA, Fedorov E, Novak WRP, Babbitt PC, Almo SC, Gerlt JA. D-ribulose 5-phosphate 3-epimerase: Functional and structural relationships to members of the ribulose-phosphate binding (β/α) 8-barrel superfamily Biochemistry. 45: 2493-2503. PMID 16489742 DOI: 10.1021/Bi052474M |
0.823 |
|
| 2005 |
Vick JE, Schmidt DM, Gerlt JA. Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase superfamily. Biochemistry. 44: 11722-9. PMID 16128573 DOI: 10.1021/Bi050963G |
0.815 |
|
| 2005 |
Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 44: 1816-23. PMID 15697207 DOI: 10.1021/Bi0478143 |
0.825 |
|
| 2005 |
Yew WS, Akana J, Wise EL, Rayment I, Gerlt JA. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 44: 1807-15. PMID 15697206 DOI: 10.1021/Bi047815V |
0.821 |
|
| 2005 |
Gerlt JA, Babbitt PC, Rayment I. Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity. Archives of Biochemistry and Biophysics. 433: 59-70. PMID 15581566 DOI: 10.1016/J.Abb.2004.07.034 |
0.434 |
|
| 2004 |
Wise EL, Akana J, Gerlt JA, Rayment I. Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution. Acta Crystallographica. Section D, Biological Crystallography. 60: 1687-90. PMID 15333955 DOI: 10.1107/S0907444904015896 |
0.812 |
|
| 2004 |
Klenchin VA, Schmidt DM, Gerlt JA, Rayment I. Evolution of enzymatic activities in the enolase superfamily: structure of a substrate-liganded complex of the L-Ala-D/L-Glu epimerase from Bacillus subtilis. Biochemistry. 43: 10370-8. PMID 15301535 DOI: 10.1021/Bi049197O |
0.715 |
|
| 2004 |
Eberhard ED, Gerlt JA. Evolution of function in the crotonase superfamily: The stereochemical course of the reaction catalyzed by 2-ketocyclohexanecarboxyl-CoA hydrolase Journal of the American Chemical Society. 126: 7188-7189. PMID 15186151 DOI: 10.1021/Ja0482381 |
0.813 |
|
| 2004 |
Wise EL, Yew WS, Gerlt JA, Rayment I. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: crystallographic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 43: 6438-46. PMID 15157078 DOI: 10.1021/bi0497392 |
0.7 |
|
| 2004 |
Yew WS, Wise EL, Rayment I, Gerlt JA. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 43: 6427-37. PMID 15157077 DOI: 10.1021/Bi049741T |
0.742 |
|
| 2004 |
Thoden JB, Taylor Ringia EA, Garrett JB, Gerlt JA, Holden HM, Rayment I. Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis. Biochemistry. 43: 5716-27. PMID 15134446 DOI: 10.1021/bi0497897 |
0.365 |
|
| 2004 |
Wong BJ, Gerlt JA. Evolution of Function in the Crotonase Superfamily: (3S)-Methylglutaconyl-CoA Hydratase from Pseudomonas putida Biochemistry. 43: 4646-4654. PMID 15096032 DOI: 10.1021/Bi0360307 |
0.496 |
|
| 2004 |
Taylor Ringia EA, Garrett JB, Thoden JB, Holden HM, Rayment I, Gerlt JA. Evolution of enzymatic activity in the enolase superfamily: functional studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis. Biochemistry. 43: 224-9. PMID 14705949 DOI: 10.1021/Bi035815+ |
0.452 |
|
| 2004 |
Wong BL, Gerlt JA. Divergent Function in the Crotonase Superfamily: An Anhydride Intermediate in the Reactions Catalyzed by 3-Hydroisobutyryl-CoA Hydrolase [J. Am. Chem. Soc.2003,125, 12076−12077]. Journal of the American Chemical Society. 126: 1921-1921. DOI: 10.1021/Ja033467T |
0.395 |
|
| 2003 |
Klenchin VA, Taylor Ringia EA, Gerlt JA, Rayment I. Evolution of enzymatic activity in the enolase superfamily: structural and mutagenic studies of the mechanism of the reaction catalyzed by o-succinylbenzoate synthase from Escherichia coli. Biochemistry. 42: 14427-33. PMID 14661953 DOI: 10.1021/Bi035545V |
0.464 |
|
| 2003 |
Zhou H, Schmidt DMZ, Gerlt JA, Van Der Donk WA. Chemical and Enzymatic Synthesis of Fluorinated-Dehydroalanine-Containing Peptides Chembiochem. 4: 1206-1215. PMID 14613113 DOI: 10.1002/Cbic.200300654 |
0.345 |
|
| 2003 |
Wise EL, Yew WS, Gerlt JA, Rayment I. Structural evidence for a 1,2-enediolate intermediate in the reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, a member of the orotidine 5'-monophosphate decarboxylase suprafamily. Biochemistry. 42: 12133-42. PMID 14567674 DOI: 10.1021/Bi0348819 |
0.728 |
|
| 2003 |
Wong BJ, Gerlt JA. Divergent function in the crotonase superfamily: An anhydride intermediate in the reaction catalyzed by 3-hydroxyisobutyryl-CoA hydrolase Journal of the American Chemical Society. 125: 12076-12077. PMID 14518977 DOI: 10.1021/Ja037652I |
0.469 |
|
| 2003 |
Schmidt DM, Mundorff EC, Dojka M, Bermudez E, Ness JE, Govindarajan S, Babbitt PC, Minshull J, Gerlt JA. Evolutionary potential of (beta/alpha)8-barrels: functional promiscuity produced by single substitutions in the enolase superfamily. Biochemistry. 42: 8387-93. PMID 12859183 DOI: 10.1021/Bi034769A |
0.735 |
|
| 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 |
0.377 |
|
| 2003 |
McLeish MJ, Kneen MM, Gopalakrishna KN, Koo CW, Babbitt PC, Gerlt JA, Kenyon GL. Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633. Journal of Bacteriology. 185: 2451-6. PMID 12670968 DOI: 10.1128/Jb.185.8.2451-2456.2003 |
0.564 |
|
| 2002 |
Wise E, Yew WS, Babbitt PC, Gerlt JA, Rayment I. Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 41: 3861-9. PMID 11900527 DOI: 10.1021/Bi012174E |
0.742 |
|
| 2002 |
Wen Shan Yew, Gerlt JA. Utilization of L-ascorbate by Escherichia coli K-12: Assignments of functions to products of the yjf-sga and yia-sgb operons Journal of Bacteriology. 184: 302-306. PMID 11741871 DOI: 10.1128/Jb.184.1.302-306.2002 |
0.351 |
|
| 2002 |
Kenyon GL, Gerlt JA. Bioorganic Chemistry: Introduction Bioorganic Chemistry. 30: 1-2. DOI: 10.1006/Bioo.2002.1236 |
0.503 |
|
| 2001 |
Gulick AM, Schmidt DM, Gerlt JA, Rayment I. Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis. Biochemistry. 40: 15716-24. PMID 11747448 DOI: 10.1021/Bi011641P |
0.743 |
|
| 2001 |
Schmidt DMZ, Hubbard BK, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: Functional assignment of unknown proteins in bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases Biochemistry. 40: 15707-15715. PMID 11747447 DOI: 10.1021/Bi011640X |
0.696 |
|
| 2001 |
Gulick AM, Hubbard BK, Gerlt JA, Rayment I. Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli. Biochemistry. 40: 10054-62. PMID 11513584 DOI: 10.1021/Bi010733B |
0.688 |
|
| 2001 |
Taylor EA, Palmer DRJ, Gerlt JA. The lesser "burden borne" by o-succinylbenzoate synthase: An "easy" reaction involving a carboxylate carbon acid [1] Journal of the American Chemical Society. 123: 5824-5825. PMID 11403626 DOI: 10.1021/Ja010882H |
0.703 |
|
| 2001 |
Gerlt JA, Babbitt PC. Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies Annual Review of Biochemistry. 70: 209-246. PMID 11395407 DOI: 10.1146/Annurev.Biochem.70.1.209 |
0.468 |
|
| 2001 |
Holden HM, Benning MM, Haller T, Gerlt JA. The crotonase superfamily: Divergently related enzymes that catalyze different reactions involving acyl coenzyme a thioesters Accounts of Chemical Research. 34: 145-157. PMID 11263873 DOI: 10.1021/Ar000053L |
0.695 |
|
| 2000 |
Gerlt JA, Babbitt PC. Can sequence determine function? Genome Biology. 1: REVIEWS0005. PMID 11178260 DOI: 10.1186/Gb-2000-1-5-Reviews0005 |
0.353 |
|
| 2000 |
Babbitt PC, Gerlt JA. New functions from old scaffolds: how nature reengineers enzymes for new functions. Advances in Protein Chemistry. 55: 1-28. PMID 11050931 DOI: 10.1016/S0065-3233(01)55001-9 |
0.343 |
|
| 2000 |
Thompson TB, Garrett JB, Taylor EA, Meganathan R, Gerlt JA, Rayment I. Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate. Biochemistry. 39: 10662-76. PMID 10978150 DOI: 10.1021/Bi000855O |
0.734 |
|
| 2000 |
Benning MM, Haller T, Gerlt JA, Holden HM. New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli. Biochemistry. 39: 4630-9. PMID 10769118 DOI: 10.1021/Bi9928896 |
0.669 |
|
| 2000 |
Haller T, Buckel T, Rétey J, Gerlt JA. Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli. Biochemistry. 39: 4622-9. PMID 10769117 DOI: 10.1021/Bi992888D |
0.655 |
|
| 2000 |
Gulick AM, Hubbard BK, Gerlt JA, Rayment I. Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli. Biochemistry. 39: 4590-602. PMID 10769114 DOI: 10.1021/Bi992782I |
0.709 |
|
| 2000 |
Gerlt JA. New wine from old barrels. Nature Structural Biology. 7: 171-3. PMID 10700266 DOI: 10.1038/73249 |
0.327 |
|
| 1999 |
Palmer DR, Garrett JB, Sharma V, Meganathan R, Babbitt PC, Gerlt JA. Unexpected divergence of enzyme function and sequence: "N-acylamino acid racemase" is o-succinylbenzoate synthase. Biochemistry. 38: 4252-8. PMID 10194342 DOI: 10.1021/Bi990140P |
0.406 |
|
| 1999 |
Wieczorek SJ, Kalivoda KA, Clifton JG, Ringe D, Petsko GA, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: Identification of a 'new' general acid catalyst in the active site of D- galactonate dehydratase from Escherichia coli Journal of the American Chemical Society. 121: 4540-4541. DOI: 10.1021/Ja990500W |
0.358 |
|
| 1998 |
Gerlt JA, Babbitt PC. Mechanistically diverse enzyme superfamilies: the importance of chemistry in the evolution of catalysis. Current Opinion in Chemical Biology. 2: 607-12. PMID 9818186 DOI: 10.1016/S1367-5931(98)80091-4 |
0.454 |
|
| 1998 |
Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry. 37: 14369-75. PMID 9772162 DOI: 10.1021/Bi981124F |
0.656 |
|
| 1998 |
Gulick AM, Palmer DR, Babbitt PC, Gerlt JA, Rayment I. Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida. Biochemistry. 37: 14358-68. PMID 9772161 DOI: 10.1021/Bi981123N |
0.428 |
|
| 1998 |
Palmer DR, Hubbard BK, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: partitioning of reactive intermediates by (D)-glucarate dehydratase from Pseudomonas putida. Biochemistry. 37: 14350-7. PMID 9772160 DOI: 10.1021/Bi981122V |
0.681 |
|
| 1998 |
Cleland WW, Frey PA, Gerlt JA. The low barrier hydrogen bond in enzymatic catalysis. The Journal of Biological Chemistry. 273: 25529-32. PMID 9748211 DOI: 10.1074/Jbc.273.40.25529 |
0.492 |
|
| 1998 |
Hasson MS, Schlichting I, Moulai J, Taylor K, Barrett W, Kenyon GL, Babbitt PC, Gerlt JA, Petsko GA, Ringe D. Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase. Proceedings of the National Academy of Sciences of the United States of America. 95: 10396-401. PMID 9724714 DOI: 10.1073/Pnas.95.18.10396 |
0.636 |
|
| 1998 |
Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, Gerlt JA, Kenyon GL, Petsko GA, Ringe D. The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry. 37: 9918-30. PMID 9665697 DOI: 10.1021/Bi973047E |
0.622 |
|
| 1997 |
Babbitt PC, Gerlt JA. Understanding enzyme superfamilies. Chemistry As the fundamental determinant in the evolution of new catalytic activities. The Journal of Biological Chemistry. 272: 30591-4. PMID 9388188 DOI: 10.1074/Jbc.272.49.30591 |
0.392 |
|
| 1997 |
Gerlt JA, Kreevoy MM, Cleland W, Frey PA. Understanding enzymic catalysis: the importance of short, strong hydrogen bonds. Chemistry & Biology. 4: 259-67. PMID 9195866 DOI: 10.1016/S1074-5521(97)90069-7 |
0.561 |
|
| 1997 |
Palmer DRJ, Wieczorek SJ, Hubbard BK, Mrachko GT, Gerlt JA. Importance of mechanistic imperatives in enzyme-catalyzed β-elimination reactions: Stereochemical consequences of the dehydration reactions catalyzed by D-galactonate dehydratase from Escherichia coli and D-glucarate dehydratase from Pseudomonas putida Journal of the American Chemical Society. 119: 9580-9581. DOI: 10.1021/Ja970977C |
0.671 |
|
| 1996 |
Babbitt PC, Hasson MS, Wedekind JE, Palmer DR, Barrett WC, Reed GH, Rayment I, Ringe D, Kenyon GL, Gerlt JA. The enolase superfamily: a general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids. Biochemistry. 35: 16489-501. PMID 8987982 DOI: 10.1021/Bi9616413 |
0.675 |
|
| 1996 |
Schafer SL, Barrett WC, Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant. Biochemistry. 35: 5662-9. PMID 8639525 DOI: 10.1021/Bi960174M |
0.593 |
|
| 1996 |
Bhagwat M, Gerlt JA. 3'- and 5'-strand cleavage reactions catalyzed by the Fpg protein from Escherichia coli occur via successive beta- and delta-elimination mechanisms, respectively. Biochemistry. 35: 659-65. PMID 8555240 DOI: 10.1021/Bi9522662 |
0.421 |
|
| 1996 |
Highbarger LA, Gerlt JA, Kenyon GL. Mechanism of the reaction catalyzed by acetoacetate decarboxylase. Importance of lysine 116 in determining the pKa of active-site lysine 115. Biochemistry. 35: 41-6. PMID 8555196 DOI: 10.1021/Bi9518306 |
0.566 |
|
| 1996 |
Palmer DRJ, Gerlt JA. Evolution of enzymatic activities: Multiple pathways for generating and partitioning a common enolic intermediate by glucarate dehydratase from Pseudomonas putida Journal of the American Chemical Society. 118: 10323-10324. DOI: 10.1021/Ja962126V |
0.341 |
|
| 1996 |
Sargent AL, Rollog ME, Almlöf JE, Gassman PG, Gerlt JA. Enzyme-catalyzed enolization reactions: A theoretical study on the energetics of concerted and stepwise pathways Journal of Molecular Structure: Theochem. 388: 145-159. DOI: 10.1016/S0166-1280(96)80028-5 |
0.407 |
|
| 1995 |
Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant. Biochemistry. 34: 2788-97. PMID 7893690 |
0.587 |
|
| 1995 |
Mitra B, Kallarakal AT, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317. Biochemistry. 34: 2777-87. PMID 7893689 DOI: 10.1021/Bi00009A006 |
0.638 |
|
| 1995 |
Babbitt PC, Mrachko GT, Hasson MS, Huisman GW, Kolter R, Ringe D, Petsko GA, Kenyon GL, Gerlt JA. A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids. Science (New York, N.Y.). 267: 1159-61. PMID 7855594 DOI: 10.1126/Science.7855594 |
0.658 |
|
| 1995 |
Kenyon GL, Gerlt JA, Petsko GA, Kozarich JW. Mandelate Racemase: Structure-Function Studies of a Pseudosymmetric Enzyme Accounts of Chemical Research. 28: 178-186. DOI: 10.1021/Ar00052A003 |
0.595 |
|
| 1994 |
Landro JA, Gerlt JA, Kozarich JW, Koo CW, Shah VJ, Kenyon GL, Neidhart DJ, Fujita S, Petsko GA. The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate. Biochemistry. 33: 635-43. PMID 8292591 DOI: 10.1021/Bi00169A003 |
0.545 |
|
| 1994 |
Gerlt JA. Protein engineering to study enzyme catalytic mechanisms Current Opinion in Structural Biology. 4: 593-600. DOI: 10.1016/S0959-440X(94)90223-2 |
0.404 |
|
| 1993 |
Petsko GA, Kenyon GL, Gerlt JA, Ringe D, Kozarich JW. On the origin of enzymatic species. Trends in Biochemical Sciences. 18: 372-6. PMID 8256284 DOI: 10.1016/0968-0004(93)90091-Z |
0.604 |
|
| 1993 |
Mitra B, Gerlt JA, Babbitt PC, Koo CW, Kenyon GL, Joseph D, Petsko GA. A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida. Biochemistry. 32: 12959-67. PMID 8241149 DOI: 10.1021/Bi00211A003 |
0.549 |
|
| 1993 |
Gerlt JA, Gassman PG. Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters. Biochemistry. 32: 11943-52. PMID 8218268 DOI: 10.1021/Bi00096A001 |
0.409 |
|
| 1993 |
Petsko G, Ringe D, Allen K, Lavie A, Gerhart-Mueller E, Clifton J, Hasson M, Fujita S, Sugio S, Xhang X, Davenport R, Lolis E, Neidhart D, Kenyon G, Gerlt J, et al. The structural enzymology of proton-transfer reactions Protein Engineering, Design and Selection. 6: 37. DOI: 10.1093/Protein/6.Supplement.37-A |
0.624 |
|
| 1993 |
Gerlt JA, Gassman PG. An explanation for rapid enzyme-catalyzed proton abstraction from carbon acids: Importance of late transition states in concerted mechanisms Journal of the American Chemical Society. 115: 11552-11568. DOI: 10.1021/Ja00077A062 |
0.399 |
|
| 1992 |
Gerlt JA, Gassman PG. Understanding enzyme-catalyzed proton abstraction from carbon acids: Details of stepwise mechanisms for β-elimination reactions Journal of the American Chemical Society. 114: 5928-5934. DOI: 10.1021/Ja00041A004 |
0.387 |
|
| 1992 |
Gerlt JA, Kozarich JW, Kenyon GL, Gassman PG. Electrophilic catalysis can explain the unexpected acidity of carbon acids in enzyme-catalyzed reactions. [Erratum to document cited in CA115(25):274439b] Journal of the American Chemical Society. 114: 4016-4016. DOI: 10.1021/Ja00036A083 |
0.575 |
|
| 1992 |
Gerlt JA. 3 Phosphate Ester Hydrolysis Enzymes. 20: 95-139. DOI: 10.1016/S1874-6047(08)60021-9 |
0.356 |
|
| 1992 |
Gerlt JA, Kenyon GL, Kozarich JW, Neidhart DJ, Petsko GA, Powers VM. Mandelate racemase and class-related enzymes Current Opinion in Structural Biology. 2: 736-742. DOI: 10.1016/0959-440X(92)90209-P |
0.585 |
|
| 1991 |
Baldisseri DM, Torchia DA, Poole LB, Gerlt JA. Deletion of the omega-loop in the active site of staphylococcal nuclease. 2. Effects on protein structure and dynamics. Biochemistry. 30: 3628-33. PMID 2015220 DOI: 10.1021/Bi00229A006 |
0.399 |
|
| 1991 |
Poole LB, Loveys DA, Hale SP, Gerlt JA, Stanczyk SM, Bolton PH. Deletion of the omega-loop in the active site of staphylococcal nuclease. 1. Effect on catalysis and stability. Biochemistry. 30: 3621-7. PMID 2015219 DOI: 10.1021/Bi00229A005 |
0.404 |
|
| 1991 |
Withka JM, Wilde JA, Bolton PH, Mazumder A, Gerlt JA. Characterization of conformational features of DNA heteroduplexes containing aldehydic abasic sites. Biochemistry. 30: 9931-40. PMID 1911785 DOI: 10.1021/Bi00105A017 |
0.305 |
|
| 1991 |
Landro JA, Kallarakal AT, Ransom SC, Gerlt JA, Kozarich JW, Neidhart DJ, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant. Biochemistry. 30: 9274-81. PMID 1909893 DOI: 10.1021/Bi00102A020 |
0.616 |
|
| 1991 |
Neidhart DJ, Howell PL, Petsko GA, Powers VM, Li RS, Kenyon GL, Gerlt JA. Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and possible catalytic residues. Biochemistry. 30: 9264-73. PMID 1892834 DOI: 10.1021/Bi00102A019 |
0.593 |
|
| 1991 |
Powers VM, Koo CW, Kenyon GL, Gerlt JA, Kozarich JW. Mechanism of the reaction catalyzed by mandelate racemase. 1. Chemical and kinetic evidence for a two-base mechanism. Biochemistry. 30: 9255-63. PMID 1892833 DOI: 10.1021/Bi00102A018 |
0.564 |
|
| 1991 |
Mazumder A, Gerlt JA, Absalon MJ, Stubbe J, Cunningham RP, Withka J, Bolton PH. Stereochemical studies of the beta-elimination reactions at aldehydic abasic sites in DNA: endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys. Biochemistry. 30: 1119-26. PMID 1846560 DOI: 10.1021/Bi00218A033 |
0.399 |
|
| 1991 |
Gerlt JA, Kozarich JW, Kenyon GL, Gassman PG. Electrophilic catalysis can explain the unexpected acidity of carbon acids in enzyme-catalyzed reactions Journal of the American Chemical Society. 113: 9667-9669. DOI: 10.1021/Ja00025A039 |
0.596 |
|
| 1990 |
Tsou AY, Ransom SC, Gerlt JA, Buechter DD, Babbitt PC, Kenyon GL. Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry. 29: 9856-62. PMID 2271624 DOI: 10.1021/Bi00494A015 |
0.6 |
|
| 1990 |
Neidhart DJ, Kenyon GL, Gerlt JA, Petsko GA. Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Nature. 347: 692-4. PMID 2215699 DOI: 10.1038/347692A0 |
0.635 |
|
| 1990 |
Pourmotabbed T, Dell'Acqua M, Gerlt JA, Stanczyk SM, Bolton PH. Kinetic and conformational effects of lysine substitutions for arginines 35 and 87 in the active site of staphylococcal nuclease. Biochemistry. 29: 3677-83. PMID 2111164 DOI: 10.1021/Bi00467A013 |
0.429 |
|
| 1990 |
Neidhart DC, Howell PL, Petsko GA, Gerlt JA, Kozarich JW, Powers VM, Kenyon GL. Restructuring catalysis in the mandelate pathway. Biochemical Society Symposium. 57: 135-41. PMID 2099737 |
0.571 |
|
| 1989 |
Hibler DW, Harpold L, Dell'Acqua M, Pourmotabbed T, Gerlt JA, Wilde JA, Bolton PH. Isotopic labeling with hydrogen-2 and carbon-13 to compare conformations of proteins and mutants generated by site-directed mutagenesis, I. Methods in Enzymology. 177: 74-86. PMID 2691847 DOI: 10.1016/0076-6879(89)77006-3 |
0.317 |
|
| 1989 |
Serpersu EH, Hibler DW, Gerlt JA, Mildvan AS. Kinetic and magnetic resonance studies of the glutamate-43 to serine mutant of staphylococcal nuclease. Biochemistry. 28: 1539-48. PMID 2566322 DOI: 10.1021/Bi00430A018 |
0.371 |
|
| 1989 |
Tsou AY, Ransom SC, Gerlt JA, Powers VM, Kenyon GL. Selection and characterization of a mutant of the cloned gene for mandelate racemase that confers resistance to an affinity label by greatly enhanced production of enzyme. Biochemistry. 28: 969-75. PMID 2496759 DOI: 10.1021/Bi00429A008 |
0.563 |
|
| 1989 |
Manoharan M, Ransom SC, Mazumder A, Gerlt JA. Site-specific 13C labeling of DNA to deduce DNA repair mechanisms of uracil-DNA glycosylase and UV endonuclease V Nucleosides and Nucleotides. 8: 879-883. DOI: 10.1080/07328318908054235 |
0.317 |
|
| 1989 |
Mazumder A, Gerlt JA, Rabow L, Absalon MJ, Stubbe J, Bolton PH. UV endonuclease V from bacteriophage T4 catalyzes DNA strand cleavage at aldehydic abasic sites by a syn β-elimination reaction Journal of the American Chemical Society. 111: 8029-8030. DOI: 10.1021/Ja00202A062 |
0.307 |
|
| 1988 |
Neidhart DJ, Powers VM, Kenyon GL, Tsou AY, Ransom SC, Gerlt JA, Petsko GA. Preliminary x-ray data on crystals of mandelate racemase. The Journal of Biological Chemistry. 263: 9268-70. PMID 3132459 |
0.459 |
|
| 1988 |
Wilde JA, Bolton PH, Dell'Acqua M, Hibler DW, Pourmotabbed T, Gerlt JA. Identification of residues involved in a conformational change accompanying substitutions for glutamate-43 in staphylococcal nuclease. Biochemistry. 27: 4127-32. PMID 2843224 DOI: 10.1021/Bi00411A033 |
0.368 |
|
| 1988 |
Ransom SC, Gerlt JA, Powers VM, Kenyon GL. Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putida. Biochemistry. 27: 540-5. PMID 2831968 DOI: 10.1021/Bi00402A006 |
0.553 |
|
| 1987 |
Hibler DW, Stolowich NJ, Reynolds MA, Gerlt JA, Wilde JA, Bolton PH. Site-directed mutants of staphylococcal nuclease. Detection and localization by 1H NMR spectroscopy of conformational changes accompanying substitutions for glutamic acid-43. Biochemistry. 26: 6278-86. PMID 2891375 DOI: 10.1021/Bi00393A048 |
0.4 |
|
| 1987 |
Gerlt JA. Relationships between enzymatic catalysis and active site structure revealed by applications of site-directed mutagenesis Chemical Reviews. 87: 1079-1105. DOI: 10.1021/Cr00081A010 |
0.326 |
|
| 1986 |
Wilde JA, Bolton PH, Stolowich NJ, Gerlt JA. A method for the observation of selected proton NMR resonances of proteins Journal of Magnetic Resonance (1969). 68: 168-171. DOI: 10.1016/0022-2364(86)90327-6 |
0.331 |
|
| 1984 |
REYNOLDS MA, GERLT JA, DEMOU PC, OPPENHEIMER NJ, KENYON GL. ChemInform Abstract: NITROGEN-15 AND OXYGEN-17 NMR STUDIES OF THE PROTON BINDING SITES IN IMIDODIPHOSPHATE, TETRAETHYL IMIDODIPHOSPHATE, AND ADENYLYL IMIDODIPHOSPHATE Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198404050 |
0.472 |
|
| 1984 |
GERLT JA, REYNOLDS MA, DEMOU PC, KENYON GL. ChemInform Abstract: OXYGEN-17 NMR SPECTRAL PROPERTIES OF PYROPHOSPHATE, SIMPLE PHOSPHONATES, AND THIOPHOSPHATE AND PHOSPHONATE ANALOGUES OF ATP Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198404049 |
0.458 |
|
| 1983 |
Leib TK, Gerlt JA. Evidence for a small catalytic domain in the adenylate cyclase from Salmonella typhimurium. The Journal of Biological Chemistry. 258: 12982-7. PMID 6313684 |
0.303 |
|
| 1983 |
Gerlt JA, Coderre JA, Mehdi S. Oxygen chiral phosphate esters. Advances in Enzymology and Related Areas of Molecular Biology. 55: 291-380. PMID 6312782 DOI: 10.1002/9780470123010.Ch4 |
0.761 |
|
| 1983 |
Mehdi S, Coderre JA, Gerlt JA. Oxygen chiral phosphodiesters-8. Stereochemical course of the base-catalyzed hydrolysis of cyclic 2'-deoxyadenosine 3',5'-[17O, 18O]monophosphate Tetrahedron. 39: 3483-3492. DOI: 10.1016/S0040-4020(01)88658-0 |
0.699 |
|
| 1983 |
Reynolds MA, Gerlt JA, Demou PC, Oppenheimer NJ, Kenyon GL. Nitrogen-15 and oxygen-17 NMR studies of the proton binding sites in imidodiphosphate, tetraethyl imidodiphosphate, and adenylyl imidodiphosphate Journal of the American Chemical Society. 105: 6475-6481. DOI: 10.1002/Chin.198404050 |
0.527 |
|
| 1983 |
Gerlt JA, Reynolds MA, Demou PC, Kenyon GL. Oxygen-17 NMR spectral properties of pyrophosphate, simple phosphonates, and thiophosphate and phosphonate analogues of ATP Journal of the American Chemical Society. 105: 6469-6475. DOI: 10.1002/Chin.198404049 |
0.515 |
|
| 1982 |
Mehdi S, Gerlt JA. Oxygen chiral phosphodiesters. 7. Stereochemical course of a reaction catalyzed by staphylococcal nuclease Journal of the American Chemical Society. 104: 3223-3225. DOI: 10.1002/Chin.198238129 |
0.34 |
|
| 1981 |
Coderre JA, Mehdi S, Demou PC, Weber R, Traficante DD, Gerlt JA. Oxygen chiral phosphodiesters. 3. Use of 17O NMR spectroscopy to demonstrate configurational differences in the diastereomers of cyclic 2′-deoxyadenosine 3′,5′-[17O,18O]monophosphate Journal of the American Chemical Society. 103: 1870-1872. DOI: 10.1021/Ja00397A063 |
0.685 |
|
| 1981 |
Coderre JA, Mehdi S, Gerlt JA. Oxygen chiral phosphodiesters. 4. Stereochemical course of the hydrolysis of 2'-deoxyadenosine cyclic 3',5'-[17O, 18O]monophosphate in water(oxygen-16) catalyzed by bovine heart cyclic nucleotide phosphodiesterase Journal of the American Chemical Society. 103: 1872-1875. DOI: 10.1002/Chin.198128358 |
0.693 |
|
| 1981 |
Coderre JA, Mehdi S, Demou PC, Weber R, Traficante DD, Gerlt JA. Oxygen Chiral Phosphodiesters. 3. Use Of Oxygen-17 Nmr Spectroscopy To Demonstrate Configurational Differences In The Diastereomers Of Cyclic 2′-Deoxyadenosine 3′,5′-(17O,18O)Monophosphate Cheminform. 12. DOI: 10.1002/Chin.198128357 |
0.687 |
|
| 1980 |
Gerlt JA, Coderre JA, Wolin MS. Mechanism of the adenylate cyclase reaction. Stereochemistry of the reaction catalyzed by the enzyme from Brevibacterium liquefaciens. The Journal of Biological Chemistry. 255: 331-4. PMID 6243273 |
0.572 |
|
| 1980 |
Coderre JA, Gerlt JA. Oxygen chiral phosphodiesters. 2. Enzymatic synthesis and configurational analysis of [α-18O]-2′-deoxyadenosine 5′-diphosphate [27] Journal of the American Chemical Society. 102: 6594-6597. DOI: 10.1021/Ja00541A053 |
0.691 |
|
| 1980 |
Gerlt JA, Coderre JA. Oxygen chiral phosphodiesters. 1. Synthesis and configurational analysis of cyclic [18O]-2'-deoxyadenosine 3',5'-monophosphate Journal of the American Chemical Society. 102: 4531-4533. DOI: 10.1021/Ja00533A045 |
0.69 |
|
| 1980 |
Marsh FJ, Weiner P, Douglas JE, Kollman PA, Kenyon GL, Gerlt JA. Theoretical calculations on the geometric destabilization of 3′,5′- and 2′,3′-cyclic nucleotides Journal of the American Chemical Society. 102: 1660-1665. DOI: 10.1021/Ja00525A034 |
0.494 |
|
| 1980 |
Gerlt JA, Mehdi S, Coderre JA, Rogers WO. Syntheses and configurational assignments of the diastereomers of the 4-nitrophenyl esters of thymidine 3′-(N-phenyl phosphoramidate) and thymidine 5′-(N-phenyl phosphoramidate) Tetrahedron Letters. 21: 2385-2388. DOI: 10.1016/S0040-4039(00)93156-3 |
0.674 |
|
| 1980 |
Gerlt JA, Coderre JA. Oxygen Chiral Phosphodiesters. 1. Synthesis And Configurational Analysis Of Cyclic (18O)-2′-Deoxyadenosine 3′,5′-Monophosphate Cheminform. 11. DOI: 10.1002/Chin.198039073 |
0.689 |
|
| 1980 |
MARSH FJ, WEINER P, DOUGLAS JE, KOLLMANN PA, KENYON GL, GERLT JA. ChemInform Abstract: THEORETICAL CALCULATIONS OF HYDROLYSIS ENERGIES OF “HIGH-ENERGY” MOLECULES. 3. HEORETICAL CALCULATIONS ON THE GEOMETRIC DESTABILIZATION OF 3′,5′- A D 2′,3′-CYCLIC NUCLEOTIDES Chemischer Informationsdienst. 11. DOI: 10.1002/chin.198023068 |
0.459 |
|
| 1979 |
Gerlt JA, Wan WH. Stereochemistry of the hydrolysis of the endo isomer of uridine 2',3'-cyclic phosphorothioate catalyzed by the nonspecific phosphohydrolase from Enterobacter aerogenes. Biochemistry. 18: 4630-8. PMID 227444 DOI: 10.1021/Bi00588A025 |
0.393 |
|
| 1975 |
Gerlt JA, Westheimer FH, Sturtevant JM. The enthalpies of hydrolysis of acyclic, monocyclic, and glycoside cyclic phosphate diesters. The Journal of Biological Chemistry. 250: 5059-67. PMID 168198 |
0.554 |
|
| 1973 |
Gerlt JA, Westheimer FH. Letter: A phosphodiesterase from Enterobacter aerogenes. Journal of the American Chemical Society. 95: 8166-8. PMID 4357681 DOI: 10.1021/Ja00805A035 |
0.487 |
|
| 1973 |
Sturtevan JM, Gerlt JA, Westheimer FH. Enthalpy of hydrolysis of simple phosphate diesters Journal of the American Chemical Society. 95: 8168-8169. DOI: 10.1021/Ja00805A036 |
0.572 |
|
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