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Audrey L. Lamb, PhD - Publications

Affiliations: 
Molecular Biosciences University of Kansas, Lawrence, KS, United States 
Area:
Iron uptake
Website:
http://www.molecularbiosciences.ku.edu/audrey-lamb
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51 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Glockzin K, Meneely KM, Hughes R, Maatouk SW, Piña GE, Suthagar K, Clinch K, Buckler JN, Lamb AL, Tyler PC, Meek TD, Katzfuss A. Kinetic and Structural Characterization of Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferases and Repurposing of Transition-State Analogue Inhibitors. Biochemistry. 62: 2182-2201. PMID 37418678 DOI: 10.1021/acs.biochem.3c00116  0.767
2023 Meneely KM, McFarlane JS, Wright CL, Vela K, Swint-Kruse L, Fenton AW, Lamb AL. The 2.4 Å structure of Zymomonas mobilis pyruvate kinase: Implications for stability and regulation. Archives of Biochemistry and Biophysics. 744: 109679. PMID 37393983 DOI: 10.1016/j.abb.2023.109679  0.798
2022 Kenjić N, Meneely KM, Wherritt DJ, Denler MC, Jackson TA, Moran GR, Lamb AL. Evidence for the Chemical Mechanism of RibB (3,4-Dihydroxy-2-butanone 4-phosphate Synthase) of Riboflavin Biosynthesis. Journal of the American Chemical Society. PMID 35802469 DOI: 10.1021/jacs.2c03376  0.77
2022 Shelton CL, Meneely KM, Ronnebaum TA, Chilton AS, Riley AP, Prisinzano TE, Lamb AL. Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 35513576 DOI: 10.1007/s00775-022-01941-8  0.784
2021 Fenton KD, Meneely KM, Wu T, Martin TA, Swint-Kruse L, Fenton AW, Lamb AL. Substitutions at a rheostat position in human aldolase A cause a shift in the conformational population. Protein Science : a Publication of the Protein Society. PMID 34734672 DOI: 10.1002/pro.4222  0.754
2021 Smith MM, Beaupre BA, Fourozesh DC, Meneely KM, Lamb AL, Moran GR. Finding Ways to Relax: A Revisionistic Analysis of the Chemistry of GTP Cyclohydrolase II. Biochemistry. 60: 3027-3039. PMID 34569786 DOI: 10.1021/acs.biochem.1c00511  0.77
2020 Rudeen AJ, Douglas JT, Xing M, McDonald WH, Lamb AL, Neufeld KL. The 15-aa repeat region of Adenomatous polyposis coli is intrinsically disordered and retains conformational flexibility upon binding β-catenin. Biochemistry. PMID 32941008 DOI: 10.1021/Acs.Biochem.0C00479  0.31
2020 Forbes D, Meneely KM, Chilton A, Lamb AL, Ellis HR. 3-His Metal Coordination Site Promotes the Coupling of Oxygen Activation to Cysteine Oxidation in Cysteine Dioxygenase. Biochemistry. PMID 32368901 DOI: 10.1021/Acs.Biochem.9B01085  0.794
2019 McFarlane JS, Zhang J, Wang S, Lei X, Moran GR, Lamb AL. Staphylopine and pseudopaline dehydrogenase from bacterial pathogens catalyze reversible reactions and produce stereospecific metallophores. The Journal of Biological Chemistry. PMID 31615895 DOI: 10.1074/Jbc.Ra119.011059  0.789
2019 McFarlane JS, Ronnebaum TA, Meneely KM, Chilton A, Fenton AW, Lamb AL. Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-π bond. Acta Crystallographica. Section F, Structural Biology Communications. 75: 461-469. PMID 31204694 DOI: 10.1107/S2053230X19007209  0.787
2019 Kenjić N, Hoag MR, Moraski GC, Caperelli CA, Moran GR, Lamb AL. PvdF of pyoverdin biosynthesis is a structurally unique N-formyltetrahydrofolate-dependent formyltransferase. Archives of Biochemistry and Biophysics. 664: 40-50. PMID 30689984 DOI: 10.1016/j.abb.2019.01.028  0.421
2019 McFarlane JS, Hagen RA, Chilton AS, Forbes DL, Lamb AL, Ellis HR. Not as easy as pi : An insertional residue does not explain the pi-helix gain-of-function in two-component FMN reductases. Protein Science. 28: 123-134. DOI: 10.2210/Pdb6Dqp/Pdb  0.826
2018 Ronnebaum TA, McFarlane JS, Prisinzano TE, Booker SJ, Lamb AL. Stuffed Methyltransferase Catalyzes Penultimate Step of Pyochelin Biosynthesis. Biochemistry. PMID 30525512 DOI: 10.1021/Acs.Biochem.8B00716  0.773
2018 McFarlane JS, Hagen R, Chilton AS, Forbes D, Lamb A, Ellis HR. Not as easy as π: an insertional residue does not explain the π-helix gain-of-function in two component FMN reductases. Protein Science : a Publication of the Protein Society. PMID 30171650 DOI: 10.1002/Pro.3504  0.825
2018 McFarlane JS, Davis CL, Lamb AL. Staphylopine, pseudopaline and yersinopine dehydrogenases: a structural and kinetic analysis of a new functional class of opine dehydrogenase. The Journal of Biological Chemistry. PMID 29618515 DOI: 10.1074/Jbc.Ra118.002007  0.839
2018 Shelton CL, Lamb AL. Unraveling the Structure and Mechanism of the MST(ery) Enzymes. Trends in Biochemical Sciences. PMID 29573882 DOI: 10.1016/J.Tibs.2018.02.011  0.488
2018 Ronnebaum TA, Lamb AL. Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study. Current Opinion in Structural Biology. 53: 1-11. PMID 29455106 DOI: 10.1016/J.Sbi.2018.01.015  0.778
2017 McFarlane JS, Lamb AL. Biosynthesis of an Opine Metallophore by Pseudomonas aeruginosa. Biochemistry. PMID 29091735 DOI: 10.1021/Acs.Biochem.7B00804  0.802
2016 Beaupre BA, Roman JV, Hoag MR, Meneely KM, Silvaggi NR, Lamb AL, Moran GR. Ligand binding phenomena that pertain to the metabolic function of renalase. Archives of Biochemistry and Biophysics. PMID 27769837 DOI: 10.1016/J.Abb.2016.10.011  0.784
2016 Meneely KM, Ronnebaum TA, Riley AP, Prisinzano TE, Lamb AL. Holo-structure and steady state kinetics of the thiazolinyl imine reductases for siderophore biosynthesis. Biochemistry. PMID 27601130 DOI: 10.1021/Acs.Biochem.6B00735  0.818
2016 Meneely KM, Sundlov JA, Gulick AM, Moran GR, Lamb AL. An Open and Shut Case: The Interaction of Magnesium with MST Enzymes. Journal of the American Chemical Society. PMID 27373320 DOI: 10.1021/Jacs.6B05134  0.794
2015 Lamb AL. Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy. Biochimica Et Biophysica Acta. 1854: 1054-70. PMID 25970810 DOI: 10.1016/J.Bbapap.2015.05.001  0.318
2014 Chilton AS, Ellis AL, Lamb AL. Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis. Acta Crystallographica. Section F, Structural Biology Communications. 70: 1328-32. PMID 25286934 DOI: 10.1107/S2053230X14018962  0.496
2014 Meneely KM, Luo Q, Riley AP, Taylor B, Roy A, Stein RL, Prisinzano TE, Lamb AL. Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism. Bioorganic & Medicinal Chemistry. 22: 5961-9. PMID 25282647 DOI: 10.1016/J.Bmc.2014.09.010  0.783
2014 Lothrop AP, Snider GW, Flemer S, Ruggles EL, Davidson RS, Lamb AL, Hondal RJ. Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis. Biochemistry. 53: 664-74. PMID 24490974 DOI: 10.1021/Bi4007258  0.428
2014 Frederick RE, Ojha S, Lamb A, Dubois JL. How pH modulates the reactivity and selectivity of a siderophore-associated flavin monooxygenase. Biochemistry. 53: 2007-16. PMID 24490904 DOI: 10.1021/Bi401256B  0.347
2013 Meneely KM, Luo Q, Lamb AL. Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities Archives of Biochemistry and Biophysics. 539: 70-80. PMID 24055536 DOI: 10.1016/J.Abb.2013.09.007  0.809
2013 Meneely KM, Luo Q, Dhar P, Lamb AL. Lysine221 is the general base residue of the isochorismate synthase from Pseudomonas aeruginosa (PchA) in a reaction that is diffusion limited Archives of Biochemistry and Biophysics. 538: 49-56. PMID 23942051 DOI: 10.1016/J.Abb.2013.07.026  0.816
2012 Meneely KM, Lamb AL. Two structures of a thiazolinyl imine reductase from yersinia enterocolitica provide insight into catalysis and binding to the nonribosomal peptide synthetase module of HMWP1 Biochemistry. 51: 9002-9013. PMID 23066849 DOI: 10.1021/Bi3011016  0.806
2012 Olucha J, Meneely KM, Lamb AL. Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB Biochemistry. 51: 7525-7532. PMID 22970849 DOI: 10.1021/Bi300472N  0.795
2012 Olucha J, Meneely KM, Lamb AL. Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB Biochemistry. 51: 7525-7532. PMID 22970849 DOI: 10.1021/bi300472n  0.306
2011 Olucha J, Lamb AL. Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases Bioorganic Chemistry. 39: 171-177. PMID 21871647 DOI: 10.1016/J.Bioorg.2011.07.006  0.812
2011 Lamb AL. Pericyclic reactions catalyzed by chorismate-utilizing enzymes Biochemistry. 50: 7476-7483. PMID 21823653 DOI: 10.1021/Bi2009739  0.487
2011 Olucha J, Meneely KM, Chilton AS, Lamb AL. Two structures of an N-hydroxylating flavoprotein monooxygenase: Ornithine hydroxylase from Pseudomonas aeruginosa Journal of Biological Chemistry. 286: 31789-31798. PMID 21757711 DOI: 10.1074/Jbc.M111.265876  0.815
2011 Olucha J, Ouellette AN, Luo Q, Lamb AL. PH dependence of catalysis by pseudomonas aeruginosa isochorismate - Pyruvate lyase: Implications for transition state stabilization and the role of lysine 42 Biochemistry. 50: 7198-7207. PMID 21751784 DOI: 10.1021/Bi200599J  0.818
2011 Luo Q, Meneely KM, Lamb AL. Entropic and enthalpic components of catalysis in the mutase and lyase activities of pseudomonas aeruginosa PchB Journal of the American Chemical Society. 133: 7229-7233. PMID 21504201 DOI: 10.1021/Ja202091A  0.801
2009 Zaitseva J, Meneely KM, Lamb AL. Structure of escherichia coli malate dehydrogenase at 1.45 Å resolution Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65: 866-869. PMID 19724119 DOI: 10.1107/S1744309109032217  0.768
2009 Hickey JM, Hefty PS, Lamb AL. Expression, purification, crystallization and preliminary X-ray analysis of the DNA-binding domain of a Chlamydia trachomatis OmpR/PhoB-subfamily response regulator homolog, ChxR Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65: 791-794. PMID 19652341 DOI: 10.1107/S1744309109025184  0.352
2009 Luo Q, Olucha J, Lamb AL. Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme Biochemistry. 48: 5239-5245. PMID 19432488 DOI: 10.1021/Bi900456E  0.827
2009 Luo Q, Olucha J, Lamb AL. Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme Biochemistry. 48: 5239-5245. PMID 19432488 DOI: 10.1021/bi900456e  0.387
2009 Meneely KM, Barr EW, Bollinger JM, Lamb AL. Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. Biochemistry. 48: 4371-6. PMID 19368334 DOI: 10.1021/Bi900442Z  0.737
2009 Meneely KM, Barr EW, Bollinger JM, Lamb AL. Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. Biochemistry. 48: 4371-6. PMID 19368334 DOI: 10.1021/Bi900442Z  0.737
2007 Meneely KM, Lamb AL. Biochemical characterization of a flavin adenine dinculeotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism Biochemistry. 46: 11930-11937. PMID 17900176 DOI: 10.1021/Bi700932Q  0.79
2006 Zaitseva J, Lu J, Olechoski KL, Lamb AL. Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa Journal of Biological Chemistry. 281: 33441-33449. PMID 16914555 DOI: 10.1074/Jbc.M605470200  0.568
2001 Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nature Structural Biology. 8: 751-5. PMID 11524675 DOI: 10.1038/Nsb0901-751  0.315
2001 Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nature Structural Biology. 8: 751-5. PMID 11524675 DOI: 10.1038/Nsb0901-751  0.315
2000 Lamb AL, Wernimont AK, Pufahl RA, O'Halloran TV, Rosenzweig AC. Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry. 39: 1589-95. PMID 10677207 DOI: 10.1021/Bi992822I  0.303
2000 Lamb AL, Wernimont AK, Pufahl RA, O'Halloran TV, Rosenzweig AC. Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry. 39: 1589-95. PMID 10677207 DOI: 10.1021/Bi992822I  0.303
1999 Lamb AL, Newcomer ME. The structure of retinal dehydrogenase type II at 2.7 Å resolution: Implications for retinal specificity Biochemistry. 38: 6003-6011. PMID 10320326 DOI: 10.1021/Bi9900471  0.723
1998 Lamb AL, Wang X, Napoli JL, Newcomer ME. Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II. Acta Crystallographica. Section D, Biological Crystallography. 54: 639-42. PMID 9761861 DOI: 10.1107/S0907444997014121  0.676
1998 Lamb AL, Wang X, Napoli JL, Newcomer ME. Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II. Acta Crystallographica. Section D, Biological Crystallography. 54: 639-42. PMID 9761861 DOI: 10.1107/S0907444997014121  0.676
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