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. 1995 Dec;39(12):2593–2601. doi: 10.1128/aac.39.12.2593

Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure.

J R Knox 1
PMCID: PMC162995  PMID: 8592985

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Selected References

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  1. Adachi H., Ohta T., Matsuzawa H. Site-directed mutants, at position 166, of RTEM-1 beta-lactamase that form a stable acyl-enzyme intermediate with penicillin. J Biol Chem. 1991 Feb 15;266(5):3186–3191. [PubMed] [Google Scholar]
  2. Ambler R. P., Coulson A. F., Frère J. M., Ghuysen J. M., Joris B., Forsman M., Levesque R. C., Tiraby G., Waley S. G. A standard numbering scheme for the class A beta-lactamases. Biochem J. 1991 May 15;276(Pt 1):269–270. doi: 10.1042/bj2760269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blazquez J., Baquero M. R., Canton R., Alos I., Baquero F. Characterization of a new TEM-type beta-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli. Antimicrob Agents Chemother. 1993 Oct;37(10):2059–2063. doi: 10.1128/aac.37.10.2059. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Boissinot M., Levesque R. C. Nucleotide sequence of the PSE-4 carbenicillinase gene and correlations with the Staphylococcus aureus PC1 beta-lactamase crystal structure. J Biol Chem. 1990 Jan 15;265(2):1225–1230. [PubMed] [Google Scholar]
  5. Bonomo R. A., Currie-McCumber C., Shlaes D. M. OHIO-1 beta-lactamase resistant to mechanism-based inactivators. FEMS Microbiol Lett. 1992 Apr 1;71(1):79–82. doi: 10.1016/0378-1097(92)90545-y. [DOI] [PubMed] [Google Scholar]
  6. Bonomo R. A., Dawes C. G., Knox J. R., Shlaes D. M. Complementary roles of mutations at positions 69 and 242 in a class A beta-lactamase. Biochim Biophys Acta. 1995 Feb 22;1247(1):113–120. doi: 10.1016/0167-4838(94)00187-l. [DOI] [PubMed] [Google Scholar]
  7. Bonomo R. A., Dawes C. G., Knox J. R., Shlaes D. M. beta-Lactamase mutations far from the active site influence inhibitor binding. Biochim Biophys Acta. 1995 Feb 22;1247(1):121–125. doi: 10.1016/0167-4838(94)00188-m. [DOI] [PubMed] [Google Scholar]
  8. Bradford P. A., Urban C., Jaiswal A., Mariano N., Rasmussen B. A., Projan S. J., Rahal J. J., Bush K. SHV-7, a novel cefotaxime-hydrolyzing beta-lactamase, identified in Escherichia coli isolates from hospitalized nursing home patients. Antimicrob Agents Chemother. 1995 Apr;39(4):899–905. doi: 10.1128/aac.39.4.899. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Bush K. Characterization of beta-lactamases. Antimicrob Agents Chemother. 1989 Mar;33(3):259–263. doi: 10.1128/aac.33.3.259. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Chanal C., Poupart M. C., Sirot D., Labia R., Sirot J., Cluzel R. Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase genes. Antimicrob Agents Chemother. 1992 Sep;36(9):1817–1820. doi: 10.1128/aac.36.9.1817. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Charlier P., Buisson G., Dideberg O., Wierenga J., Keck W., Laible G., Hakenbeck R. Crystallization of a genetically engineered water-soluble primary penicillin target enzyme. The high molecular mass PBP2x of Streptococcus pneumoniae. J Mol Biol. 1993 Aug 5;232(3):1007–1009. doi: 10.1006/jmbi.1993.1452. [DOI] [PubMed] [Google Scholar]
  12. Chen C. C., Herzberg O. Inhibition of beta-lactamase by clavulanate. Trapped intermediates in cryocrystallographic studies. J Mol Biol. 1992 Apr 20;224(4):1103–1113. doi: 10.1016/0022-2836(92)90472-v. [DOI] [PubMed] [Google Scholar]
  13. Chen C. C., Rahil J., Pratt R. F., Herzberg O. Structure of a phosphonate-inhibited beta-lactamase. An analog of the tetrahedral transition state/intermediate of beta-lactam hydrolysis. J Mol Biol. 1993 Nov 5;234(1):165–178. doi: 10.1006/jmbi.1993.1571. [DOI] [PubMed] [Google Scholar]
  14. Davies J. Inactivation of antibiotics and the dissemination of resistance genes. Science. 1994 Apr 15;264(5157):375–382. doi: 10.1126/science.8153624. [DOI] [PubMed] [Google Scholar]
  15. Delaire M., Labia R., Samama J. P., Masson J. M. Site-directed mutagenesis at the active site of Escherichia coli TEM-1 beta-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis. J Biol Chem. 1992 Oct 15;267(29):20600–20606. [PubMed] [Google Scholar]
  16. Delaire M., Lenfant F., Labia R., Masson J. M. Site-directed mutagenesis on TEM-1 beta-lactamase: role of Glu166 in catalysis and substrate binding. Protein Eng. 1991 Oct;4(7):805–810. doi: 10.1093/protein/4.7.805. [DOI] [PubMed] [Google Scholar]
  17. Dideberg O., Charlier P., Wéry J. P., Dehottay P., Dusart J., Erpicum T., Frère J. M., Ghuysen J. M. The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution. Biochem J. 1987 Aug 1;245(3):911–913. doi: 10.1042/bj2450911. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ellerby L. M., Escobar W. A., Fink A. L., Mitchinson C., Wells J. A. The role of lysine-234 in beta-lactamase catalysis probed by site-directed mutagenesis. Biochemistry. 1990 Jun 19;29(24):5797–5806. doi: 10.1021/bi00476a022. [DOI] [PubMed] [Google Scholar]
  19. Escobar W. A., Tan A. K., Lewis E. R., Fink A. L. Site-directed mutagenesis of glutamate-166 in beta-lactamase leads to a branched path mechanism. Biochemistry. 1994 Jun 21;33(24):7619–7626. doi: 10.1021/bi00190a015. [DOI] [PubMed] [Google Scholar]
  20. Ferreira L. C., Schwarz U., Keck W., Charlier P., Dideberg O., Ghuysen J. M. Properties and crystallization of a genetically engineered, water-soluble derivative of penicillin-binding protein 5 of Escherichia coli K12. Eur J Biochem. 1988 Jan 15;171(1-2):11–16. doi: 10.1111/j.1432-1033.1988.tb13751.x. [DOI] [PubMed] [Google Scholar]
  21. Ghuysen J. M. Molecular structures of penicillin-binding proteins and beta-lactamases. Trends Microbiol. 1994 Oct;2(10):372–380. doi: 10.1016/0966-842x(94)90614-9. [DOI] [PubMed] [Google Scholar]
  22. Gibson R. M., Christensen H., Waley S. G. Site-directed mutagenesis of beta-lactamase I. Single and double mutants of Glu-166 and Lys-73. Biochem J. 1990 Dec 15;272(3):613–619. doi: 10.1042/bj2720613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Hall A., Knowles J. R. Directed selective pressure on a beta-lactamase to analyse molecular changes involved in development of enzyme function. Nature. 1976 Dec 23;264(5588):803–804. doi: 10.1038/264803a0. [DOI] [PubMed] [Google Scholar]
  24. Healey W. J., Labgold M. R., Richards J. H. Substrate specificities in class A beta-lactamases: preference for penams vs. cephems. The role of residue 237. Proteins. 1989;6(3):275–283. doi: 10.1002/prot.340060310. [DOI] [PubMed] [Google Scholar]
  25. Herzberg O., Kapadia G., Blanco B., Smith T. S., Coulson A. Structural basis for the inactivation of the P54 mutant of beta-lactamase from Staphylococcus aureus PC1. Biochemistry. 1991 Oct 1;30(39):9503–9509. doi: 10.1021/bi00103a017. [DOI] [PubMed] [Google Scholar]
  26. Herzberg O. Refined crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.0 A resolution. J Mol Biol. 1991 Feb 20;217(4):701–719. doi: 10.1016/0022-2836(91)90527-d. [DOI] [PubMed] [Google Scholar]
  27. Huang W., Le Q. Q., LaRocco M., Palzkill T. Effect of threonine-to-methionine substitution at position 265 on structure and function of TEM-1 beta-lactamase. Antimicrob Agents Chemother. 1994 Oct;38(10):2266–2269. doi: 10.1128/aac.38.10.2266. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Huletsky A., Knox J. R., Levesque R. C. Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type beta-lactamases probed by site-directed mutagenesis and three-dimensional modeling. J Biol Chem. 1993 Feb 15;268(5):3690–3697. [PubMed] [Google Scholar]
  29. Imtiaz U., Billings E. M., Knox J. R., Mobashery S. A structure-based analysis of the inhibition of class A beta-lactamases by sulbactam. Biochemistry. 1994 May 17;33(19):5728–5738. doi: 10.1021/bi00185a009. [DOI] [PubMed] [Google Scholar]
  30. Imtiaz U., Manavathu E. K., Mobashery S., Lerner S. A. Reversal of clavulanate resistance conferred by a Ser-244 mutant of TEM-1 beta-lactamase as a result of a second mutation (Arg to Ser at position 164) that enhances activity against ceftazidime. Antimicrob Agents Chemother. 1994 May;38(5):1134–1139. doi: 10.1128/aac.38.5.1134. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Jacob-Dubuisson F., Lamotte-Brasseur J., Dideberg O., Joris B., Frère J. M. Arginine 220 is a critical residue for the catalytic mechanism of the Streptomyces albus G beta-lactamase. Protein Eng. 1991 Oct;4(7):811–819. doi: 10.1093/protein/4.7.811. [DOI] [PubMed] [Google Scholar]
  32. Jacob F., Joris B., Frère J. M. Active-site serine mutants of the Streptomyces albus G beta-lactamase. Biochem J. 1991 Aug 1;277(Pt 3):647–652. doi: 10.1042/bj2770647. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Jacob F., Joris B., Lepage S., Dusart J., Frère J. M. Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis. Biochem J. 1990 Oct 15;271(2):399–406. doi: 10.1042/bj2710399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Jacoby G. A. Genetics of extended-spectrum beta-lactamases. Eur J Clin Microbiol Infect Dis. 1994;13 (Suppl 1):S2–11. doi: 10.1007/BF02390679. [DOI] [PubMed] [Google Scholar]
  35. Jacoby G. A., Medeiros A. A. More extended-spectrum beta-lactamases. Antimicrob Agents Chemother. 1991 Sep;35(9):1697–1704. doi: 10.1128/aac.35.9.1697. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Jelsch C., Mourey L., Masson J. M., Samama J. P. Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution. Proteins. 1993 Aug;16(4):364–383. doi: 10.1002/prot.340160406. [DOI] [PubMed] [Google Scholar]
  37. Juteau J. M., Billings E., Knox J. R., Levesque R. C. Site-saturation mutagenesis and three-dimensional modelling of ROB-1 define a substrate binding role of Ser130 in class A beta-lactamases. Protein Eng. 1992 Oct;5(7):693–701. doi: 10.1093/protein/5.7.693. [DOI] [PubMed] [Google Scholar]
  38. Kelly J. A., Knox J. R., Moews P. C., Hite G. J., Bartolone J. B., Zhao H., Joris B., Frère J. M., Ghuysen J. M. 2.8-A Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with beta-lactams. J Biol Chem. 1985 May 25;260(10):6449–6458. [PubMed] [Google Scholar]
  39. Kelly J. A., Knox J. R., Zhao H., Frère J. M., Ghaysen J. M. Crystallographic mapping of beta-lactams bound to a D-alanyl-D-alanine peptidase target enzyme. J Mol Biol. 1989 Sep 20;209(2):281–295. doi: 10.1016/0022-2836(89)90277-5. [DOI] [PubMed] [Google Scholar]
  40. Kelly J. A., Moews P. C., Knox J. R., Frère J. M., Ghuysen J. M. Penicillin target enzyme and the antibiotic binding site. Science. 1982 Oct 29;218(4571):479–481. doi: 10.1126/science.7123246. [DOI] [PubMed] [Google Scholar]
  41. Knap A. K., Pratt R. F. Chemical modification of the RTEM-1 thiol beta-lactamase by thiol-selective reagents: evidence for activation of the primary nucleophile of the beta-lactamase active site by adjacent functional groups. Proteins. 1989;6(3):316–323. doi: 10.1002/prot.340060314. [DOI] [PubMed] [Google Scholar]
  42. Knox J. R., Moews P. C. Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis of hydration. J Mol Biol. 1991 Jul 20;220(2):435–455. doi: 10.1016/0022-2836(91)90023-y. [DOI] [PubMed] [Google Scholar]
  43. Knox J. R., Moews P. C., Escobar W. A., Fink A. L. A catalytically-impaired class A beta-lactamase: 2 A crystal structure and kinetics of the Bacillus licheniformis E166A mutant. Protein Eng. 1993 Jan;6(1):11–18. doi: 10.1093/protein/6.1.11. [DOI] [PubMed] [Google Scholar]
  44. Kuzin A. P., Liu H., Kelly J. A., Knox J. R. Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases. Biochemistry. 1995 Jul 25;34(29):9532–9540. doi: 10.1021/bi00029a030. [DOI] [PubMed] [Google Scholar]
  45. Labia R., Morand A., Tiwari K., Sirot J., Sirot D., Petit A. Interactions of new plasmid-mediated beta-lactamases with third-generation cephalosporins. Rev Infect Dis. 1988 Jul-Aug;10(4):885–891. doi: 10.1093/clinids/10.4.885. [DOI] [PubMed] [Google Scholar]
  46. Laible G., Hakenbeck R. Five independent combinations of mutations can result in low-affinity penicillin-binding protein 2x of Streptococcus pneumoniae. J Bacteriol. 1991 Nov;173(21):6986–6990. doi: 10.1128/jb.173.21.6986-6990.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Lamotte-Brasseur J., Dive G., Dideberg O., Charlier P., Frère J. M., Ghuysen J. M. Mechanism of acyl transfer by the class A serine beta-lactamase of Streptomyces albus G. Biochem J. 1991 Oct 1;279(Pt 1):213–221. doi: 10.1042/bj2790213. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Lamotte-Brasseur J., Knox J., Kelly J. A., Charlier P., Fonzé E., Dideberg O., Frére J. M. The structures and catalytic mechanisms of active-site serine beta-lactamases. Biotechnol Genet Eng Rev. 1994;12:189–230. doi: 10.1080/02648725.1994.10647912. [DOI] [PubMed] [Google Scholar]
  49. Lee K. Y., Hopkins J. D., O'Brien T. F., Syvanen M. Gly-238-Ser substitution changes the substrate specificity of the SHV class A beta-lactamases. Proteins. 1991;11(1):45–51. doi: 10.1002/prot.340110106. [DOI] [PubMed] [Google Scholar]
  50. Leung Y. C., Robinson C. V., Aplin R. T., Waley S. G. Site-directed mutagenesis of beta-lactamase I: role of Glu-166. Biochem J. 1994 May 1;299(Pt 3):671–678. doi: 10.1042/bj2990671. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Lobkovsky E., Billings E. M., Moews P. C., Rahil J., Pratt R. F., Knox J. R. Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog. Biochemistry. 1994 Jun 7;33(22):6762–6772. doi: 10.1021/bi00188a004. [DOI] [PubMed] [Google Scholar]
  52. Lobkovsky E., Moews P. C., Liu H., Zhao H., Frere J. M., Knox J. R. Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11257–11261. doi: 10.1073/pnas.90.23.11257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Mabilat C., Courvalin P. Development of "oligotyping" for characterization and molecular epidemiology of TEM beta-lactamases in members of the family Enterobacteriaceae. Antimicrob Agents Chemother. 1990 Nov;34(11):2210–2216. doi: 10.1128/aac.34.11.2210. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Matagne A., Frère J. M. Contribution of mutant analysis to the understanding of enzyme catalysis: the case of class A beta-lactamases. Biochim Biophys Acta. 1995 Jan 19;1246(2):109–127. doi: 10.1016/0167-4838(94)00177-i. [DOI] [PubMed] [Google Scholar]
  55. Moews P. C., Knox J. R., Dideberg O., Charlier P., Frère J. M. Beta-lactamase of Bacillus licheniformis 749/C at 2 A resolution. Proteins. 1990;7(2):156–171. doi: 10.1002/prot.340070205. [DOI] [PubMed] [Google Scholar]
  56. NOVICK R. P. ANALYSIS BY TRANSDUCTION OF MUTATIONS AFFECTING PENICILLINASE FORMATION IN STAPHYLOCOCCUS AUREUS. J Gen Microbiol. 1963 Oct;33:121–136. doi: 10.1099/00221287-33-1-121. [DOI] [PubMed] [Google Scholar]
  57. Neu H. C. The crisis in antibiotic resistance. Science. 1992 Aug 21;257(5073):1064–1073. doi: 10.1126/science.257.5073.1064. [DOI] [PubMed] [Google Scholar]
  58. Nukaga M., Haruta S., Tanimoto K., Kogure K., Taniguchi K., Tamaki M., Sawai T. Molecular evolution of a class C beta-lactamase extending its substrate specificity. J Biol Chem. 1995 Mar 17;270(11):5729–5735. doi: 10.1074/jbc.270.11.5729. [DOI] [PubMed] [Google Scholar]
  59. Oefner C., D'Arcy A., Daly J. J., Gubernator K., Charnas R. L., Heinze I., Hubschwerlen C., Winkler F. K. Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis. Nature. 1990 Jan 18;343(6255):284–288. doi: 10.1038/343284a0. [DOI] [PubMed] [Google Scholar]
  60. Oliphant A. R., Struhl K. An efficient method for generating proteins with altered enzymatic properties: application to beta-lactamase. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9094–9098. doi: 10.1073/pnas.86.23.9094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Osuna J., Viadiu H., Fink A. L., Soberón X. Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward different substrates and effects of neighboring residues. J Biol Chem. 1995 Jan 13;270(2):775–780. [PubMed] [Google Scholar]
  62. Palzkill T., Botstein D. Identification of amino acid substitutions that alter the substrate specificity of TEM-1 beta-lactamase. J Bacteriol. 1992 Aug;174(16):5237–5243. doi: 10.1128/jb.174.16.5237-5243.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Palzkill T., Le Q. Q., Venkatachalam K. V., LaRocco M., Ocera H. Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of beta-lactamase. Mol Microbiol. 1994 Apr;12(2):217–229. doi: 10.1111/j.1365-2958.1994.tb01011.x. [DOI] [PubMed] [Google Scholar]
  64. Petit A., Maveyraud L., Lenfant F., Samama J. P., Labia R., Masson J. M. Multiple substitutions at position 104 of beta-lactamase TEM-1: assessing the role of this residue in substrate specificity. Biochem J. 1995 Jan 1;305(Pt 1):33–40. doi: 10.1042/bj3050033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Philippon A., Labia R., Jacoby G. Extended-spectrum beta-lactamases. Antimicrob Agents Chemother. 1989 Aug;33(8):1131–1136. doi: 10.1128/aac.33.8.1131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Raquet X., Lamotte-Brasseur J., Fonzé E., Goussard S., Courvalin P., Frère J. M. TEM beta-lactamase mutants hydrolysing third-generation cephalosporins. A kinetic and molecular modelling analysis. J Mol Biol. 1994 Dec 16;244(5):625–639. doi: 10.1006/jmbi.1994.1756. [DOI] [PubMed] [Google Scholar]
  67. Shlaes D. M., Currie-McCumber C. Mutations altering substrate specificity in OHIO-1, and SHV-1 family beta-lactamase. Biochem J. 1992 Jun 1;284(Pt 2):411–415. doi: 10.1042/bj2840411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Sigal I. S., DeGrado W. F., Thomas B. J., Petteway S. R., Jr Purification and properties of thiol beta-lactamase. A mutant of pBR322 beta-lactamase in which the active site serine has been replaced with cysteine. J Biol Chem. 1984 Apr 25;259(8):5327–5332. [PubMed] [Google Scholar]
  69. Sougakoff W., Petit A., Goussard S., Sirot D., Bure A., Courvalin P. Characterization of the plasmid genes blaT-4 and blaT-5 which encode the broad-spectrum beta-lactamases TEM-4 and TEM-5 in enterobacteriaceae. Gene. 1989 May 30;78(2):339–348. doi: 10.1016/0378-1119(89)90236-9. [DOI] [PubMed] [Google Scholar]
  70. Sowek J. A., Singer S. B., Ohringer S., Malley M. F., Dougherty T. J., Gougoutas J. Z., Bush K. Substitution of lysine at position 104 or 240 of TEM-1pTZ18R beta-lactamase enhances the effect of serine-164 substitution on hydrolysis or affinity for cephalosporins and the monobactam aztreonam. Biochemistry. 1991 Apr 2;30(13):3179–3188. doi: 10.1021/bi00227a004. [DOI] [PubMed] [Google Scholar]
  71. Spratt B. G. Resistance to antibiotics mediated by target alterations. Science. 1994 Apr 15;264(5157):388–393. doi: 10.1126/science.8153626. [DOI] [PubMed] [Google Scholar]
  72. Stemmer W. P. Rapid evolution of a protein in vitro by DNA shuffling. Nature. 1994 Aug 4;370(6488):389–391. doi: 10.1038/370389a0. [DOI] [PubMed] [Google Scholar]
  73. Strynadka N. C., Adachi H., Jensen S. E., Johns K., Sielecki A., Betzel C., Sutoh K., James M. N. Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution. Nature. 1992 Oct 22;359(6397):700–705. doi: 10.1038/359700a0. [DOI] [PubMed] [Google Scholar]
  74. Tamaki M., Nukaga M., Sawai T. Replacement of serine 237 in class A beta-lactamase of Proteus vulgaris modifies its unique substrate specificity. Biochemistry. 1994 Aug 23;33(33):10200–10206. doi: 10.1021/bi00199a049. [DOI] [PubMed] [Google Scholar]
  75. Thunnissen M. M., Fusetti F., de Boer B., Dijkstra B. W. Purification, crystallisation and preliminary X-ray analysis of penicillin binding protein 4 from Escherichia coli, a protein related to class A beta-lactamases. J Mol Biol. 1995 Mar 24;247(2):149–153. doi: 10.1006/jmbi.1994.0128. [DOI] [PubMed] [Google Scholar]
  76. Vedel G., Belaaouaj A., Gilly L., Labia R., Philippon A., Névot P., Paul G. Clinical isolates of Escherichia coli producing TRI beta-lactamases: novel TEM-enzymes conferring resistance to beta-lactamase inhibitors. J Antimicrob Chemother. 1992 Oct;30(4):449–462. doi: 10.1093/jac/30.4.449. [DOI] [PubMed] [Google Scholar]
  77. Venkatachalam K. V., Huang W., LaRocco M., Palzkill T. Characterization of TEM-1 beta-lactamase mutants from positions 238 to 241 with increased catalytic efficiency for ceftazidime. J Biol Chem. 1994 Sep 23;269(38):23444–23450. [PubMed] [Google Scholar]
  78. Viadiu H., Osuna J., Fink A. L., Soberón X. A new TEM beta-lactamase double mutant with broadened specificity reveals substrate-dependent functional interactions. J Biol Chem. 1995 Jan 13;270(2):781–787. [PubMed] [Google Scholar]
  79. Zafaralla G., Manavathu E. K., Lerner S. A., Mobashery S. Elucidation of the role of arginine-244 in the turnover processes of class A beta-lactamases. Biochemistry. 1992 Apr 21;31(15):3847–3852. doi: 10.1021/bi00130a016. [DOI] [PubMed] [Google Scholar]
  80. Zhou X. Y., Bordon F., Sirot D., Kitzis M. D., Gutmann L. Emergence of clinical isolates of Escherichia coli producing TEM-1 derivatives or an OXA-1 beta-lactamase conferring resistance to beta-lactamase inhibitors. Antimicrob Agents Chemother. 1994 May;38(5):1085–1089. doi: 10.1128/aac.38.5.1085. [DOI] [PMC free article] [PubMed] [Google Scholar]

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