1. Meneely KM, McFarlane JS, Wright CL, Vela K, Swint-Kruse L, Fenton AW, Lamb AL. (2023) The 2.4 Å structure of Zymomonas mobilis pyruvate kinase: Implications for stability and regulation. Archives of Biochemistry and Biophysics 744, 109679. DOI:10.1016/j.abb.2023.109679
  2. Glockzin K, Meneely KM, Hughes R, Maatouk SW, Piña GE, Suthagar K, Clinch K, Buckler JN, Lamb AL, Tyler PC, Meek TD, Katzfuss A. (2023). Kinetic and Structural Characterization of Trypanosoma cruzi Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferases and Repurposing of Transition-State Analogue Inhibitors. Biochemistry 62, 2182-2201. PMC10357585. DOI:10.1021/acs.biochem.3c00116
  3. Page B, Martin T, Wright CL, Fenton LA, VIllar MT, Artigues A, Tang Q, Lamb AL, Fenton AW, Swint-Kruse L. (2022) Odd one out? Functional tuning of Zymomonas mobilis pyruvate kinase is narrower than its allosteric, human counterpart. Protein Science 31:e4336. PMC9202079. DOI:10.1002/pro.4336
  4. Shelton CL, Meneely KM, Ronnebaum TA, Chilton AS, Riley AP, Prisinzano TE, Lamb AL. (2022) Rational Inhibitor Design for Pseudomonas aeruginosa Salicylate Adenylation Enzyme PchD. Journal of Biological Inorganic Chemistry 27, 541-551. PMC9470617. DOI:10.1007/s00775-022-01941-8
  5. Kenjić N, Meneely KM, Wherritt DJ, Denler MC, Jackson TA, Moran GR, Lamb AL. (2022) Evidence for the Chemical Mechanism of RibB (3,4-Dihydroxy-2-butanone 4-phosphate Synthase) of Riboflavin Biosynthesis. Journal of the American Chemical Society 144, 12769-12780. PMC9305975. DOI:10.1021/jacs.2c03376
  6. Fenton KD, Meneely KM, Wu T, Martin TA, Swint-Kruse L, Fenton AW, Lamb AL. (2022) Substitutions at a rheostat position in human aldolase A cause a shift in the conformational population. Protein Science 31, 357-370. PMC8819835. DOI:10.1002/pro.4222
  7. Smith MM, Beaupre BA, Fourozesh DC, Meneely KM, Lamb AL, Moran GR. (2021) Finding ways to relax: a revisionistic analysis of the chemistry of E. coli GTP cyclohydrolase II. Biochemistry 60, 3027-3039. DOI:10.1021/acs.biochem.1c00511
  8. Rudeen AJ, Douglas JT, Xing M, McDonald WH, Lamb AL, Neufeld KL. (2020) The 15-amino acid repeat region of Adenomatous polyposis coli is intrinsically disordered and retains conformational flexibility upon binding β-catenin. Biochemistry 59, 4049-4050. PMC8771494. DOI:10.1021/acs.biochem.0c00479
  9. McFarlane JS, Lamb AL. (2020) Opine metallophore biosynthesis. Invited Book Chapter in Comprehensive Natural Products III: Chemistry and Biology, 5.16, 395-414. eBook ISBN:9780081026915
  10. Forbes DL, Meneely KM, Chilton AS, Lamb AL, Ellis HR. (2020) The 3-His Metal Coordination Site Promotes the Coupling of Oxygen Activation to Cysteine Oxidation in Cysteine Dioxygenase. Biochemistry 59, 2022-2031. PMC7363009. DOI:10.1021/acs.biochem.9b01085
  11. McFarlane JS, Zhang J, Wang S, Lei X, Moran GR, Lamb AL. (2019) Staphylopine and pseudopaline dehydrogenases catalyze reversible reactions and produce stereospecific metallophores. Journal of Biological Chemistry 294, 17988-18001. PMC6879343. DOI:10.1074/jbc.RA119.011059
  12. McFarlane JS, Ronnebaum TA, Meneely KM, Chilton AS, Fenton AW, Lamb AL. (2019) Changes in an allosteric site of human pyruvate kinase upon activator binding includes breaking an intersubunit cation-π bond. Acta Crystallographica Section F75, 461- 469. PMC 6572093. DOI:10.1107/S2053230X19007209
  13. Kenjic N, Hoag MR, Moraski GC, Caperelli CA, Moran GR, Lamb AL. (2019) PvdF of pyoverdin biosynthesis is structurally unique N10-formyltetrahydrofolate-dependent formyltransferase. Archives of Biochemistry and Biophysics 664, 40-50. PMC6402982. DOI:10.1016/j.abb.2019.01.028
  14. McFarlane JS, Hagen R, Chilton AS, Forbes D, Lamb AL, Ellis HR. (2019) Not as easy as π: an insertional residue does not explain the π-helix gain-of-function in two component FMN reductases. Protein Science 28, 123-134. PMC6295896. DOI:10.1002/pro.3504
  15. Ronnebaum TA, McFarlane JS, Prisinzano TE, Booker SJ, Lamb AL. (2019) Stuffed methyltransferase domain catalyzes the penultimate step of pyochelin biosynthesis. Biochemistry 58, 665-678. PMC6372355. DOI:10.1021/acs.biochem.8b00716
  16. McFarlane JS, Davis CL, Lamb AL. (2018) Staphylopine, pseudopaline and yersinopine dehydrogenases: a structural and kinetic analysis of a new functional class of opine dehydrogenase. Journal of Biological Chemistry 293: 8009-8019. PMC5971449. DOI:10.1074/jbc.RA118.002007
  17. Shelton CL, Lamb AL. (2018) Unraveling the structure and mechanism of the MST(ery) enzymes. Trends in Biochemical Sciences 43: 342-357. Invited review. PMC5924575. DOI:10.1016/j.tibs.2018.02.011
  18. Ronnebaum TA, Lamb AL. (2018) Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study. Current Opinion in Structural Biology 53, 1-11. Invited review. PMC6093814. DOI:10.1016/j.sbi.2018.01.015
  19. McFarlane JS, Lamb AL. (2017) Biosynthesis of an opine metallophore by Pseudomonas aeruginosa. Biochemistry 56: 5967-5971. PMC5699221. DOI:10.1021/acs.biochem.7b00804
  20. Beaupre BA, Roman JV, Hoag MR, Meneely KM, Silvaggi NR, Lamb AL, Moran GR. (2016) Ligand binding phenomena that pertain to the metabolic function of renalase. Archives of Biochemistry and Biophysics 612, 46-56. PMC5522708. DOI:10.1016/j.abb.2016.10.011
  21. Meneely KM, Ronnebaum TA, Riley AP, Prisinzano TE, Lamb AL. (2016) Holo-structures and steady state kinetics of the thiazolinyl imine reductases of siderophore biosynthesis. Biochemistry 55, 5423-33. PMC5046821. DOI:10.1021/acs.biochem.6b00735
  22. Meneely KM, Sundlov JA, Gulick AM, Moran GR, Lamb AL.(2016) An open and shut case: the importance of magnesium in MST enzymes. Journal of the American Chemical Society 138, 9277-93. PMC5029964. DOI:10.1021/jacs.6b05134
  23. Lamb AL. (2015) Breaking a pathogen's iron will: inhibiting siderophore biosynthesis as an antimicrobial strategy. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1854, 1054-1070. PMC4457648. DOI:10.1016/j.bbapap.2015.05.001
  24. Lamb AL, Kappock TJ, Silvaggi NR. (2015) You are lost without a map: navigating the sea of protein structures. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1854, 258-268. PMC5051661. DOI:10.1016/j.bbapap.2014.12.021
  25. Meneely KM, Luo Q, Riley AP, Taylor B, Roy A, Stein RL, Prisinzano TE, Lamb AL. (2014) Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism. Bioorganic and Medicinal Chemistry 22, 5961-69. PMC4254016. DOI:10.1016/j.bmc.2014.09.010
  26. Chilton AS, Ellis AL, Lamb AL. (2014) Structure of an Aspergillus fumigatus Old Yellow Enzyme (EasA) involved in Ergot Alkaloid Biosynthesis. Acta Crystallographica F Structural Biology Communications 70, 1328-32. PMC4188074. DOI:10.1107/S2053230X14018962
  27. Frederick RE, Ojha S, Lamb AL, Dubois JL. (2014) How pH modulates the reactivity and selectivity of a siderophore-associated flavin monooxygenase. Biochemistry, 53, 2007-2016. PMC3985866. DOI:10.1021/bi401256b
  28. Lothrop AP, Snider GW, Flemer S Jr, Ruggles EL, Davidson RS, Lamb AL, Hondal RJ. (2014) Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis. Biochemistry 53, 664-6674. PMC3931472. DOI:10.1021/bi4007258
  29. Meneely KM, Luo Q, Lamb AL. (2013) Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities. Archives of Biochemistry and Biophysics, 539, 70-80. PMC3836504. DOI:10.1016/j.abb.2013.09.007
  30. Meneely KM, Luo Q, Dhar P, Lamb AL. (2013) 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. PMC3784010. DOI:10.1016/j.abb.2013.07.026
  31. Meneely KM, Lamb AL. (2012) Two structures of a thiazolinyl imine reductase from Yersinia enterocolitica (Irp3) provide insight for catalysis and binding to the nonribosomal peptide synthetase module of HMWP1. Biochemistry 52, 9002-13. PMC3491095. DOI:10.1021/bi3011016
  32. Olucha J, Meneely KM, Lamb AL. (2012) 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, 7525-32. PMC3546224. DOI:10.1021/bi300472n
  33. Olucha J, Lamb AL. (2011) Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases. Bioorg. Chem. 39, 171-177. PMC3188341. DOI:10.1016/j.bioorg.2011.07.006
  34. Lamb AL. (2011) Pericyclic reactions catalyzed by chorismate-utilizing enzymes. Biochemistry 50, 7476-7483. Current Topics invited article. PMC3164438. DOI:10.1021/bi2009739
  35. Olucha J, Ouellette AN, Luo Q, Lamb AL. (2011) pH dependence of Pseudomonas aeruginosa isochorismate-pyruvate lyase: implications for transition state stabilization and the role of lysine 42. Biochemistry 50, 7198-7207. PMC3156872. DOI:10.1021/bi200599j
  36. Olucha J, Meneely KM, Chilton AS, Lamb AL. (2011) Two structures of an N-hydroxylating flavoprotein monooxygenase: the ornithine hydroxylase from Pseudomonas aeruginosa. J. Biol. Chem. 286, 31789-31798. PMC3173084. DOI:10.1074/jbc.M111.265876
  37. Luo Q, Meneely KM, Lamb AL. (2011) Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB. J. Amer. Chem. Soc. 133, 7229-7233. PMC3163167. DOI:10.1021/ja202091a
  38. Zaitseva J, Meneely KM, Lamb AL. (2009) Structure of the Escherichia coli malate dehydrogenase to 1.45 Å resolution. Acta Cryst F65, 866-869. PMC2795587. DOI:10.1107/S1744309109032217
  39. Hickey JM, Hefty PS, Lamb AL. (2009) Expression, purification, crystallization, and preliminary X-ray analysis of the DNA-binding domain of Chlamydia trachomatis OmpR/PhoB subfamily response regulator homolog, ChxR. Acta Cryst F65, 791-794. PMC2720335. DOI:10.1107/S1744309109025184
  40. Luo Q, Olucha J, Lamb AL. (2009) 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
  41. Meneely KM, Barr E, Bollinger JM, Lamb AL. (2009) Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. Biochemistry 48, 4371-4376. PMC2710847. DOI:10.1021/bi900442z
  42. Meneely KM, Lamb AL. (2007) Biochemical Characterization of a Flavin Adenine Dinculeotide Dependent Monooxygenase, Ornithine Hydroxylase from Pseudomonas aeruginosa, Suggests a Novel Reaction Mechanism. Biochemistry 46, 11930-7. PMC2597334. DOI:10.1021/bi700932q
  43. Zaitseva J, Lu J, Olechoski KL, Lamb AL. (2006) Two crystal structures of the isochorismate-pyruvate lyase from Pseudomonas aeruginosa. J. Biol. Chem. 281, 33441-33449. PMID:16914555. DOI:10.1074/jbc.M605470200