A disulfide bridge near the active site of carbapenem-hydrolyzing class A β-lactamases might explain their unusual substrate profile

Proteins: Structure, Function and Genetics

Volumn 27, Issue 1, 1997, Pages 47-58

  Raquet, Xavier ^a   Lamotte Brasseur, Josette ^a   Bouillenne, Fabrice ^a   Frère, Jean Marie ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

lactamase; carbapenems; disulfide bridge; homology modeling; kinetics

Indexed keywords

AMPICILLIN; BETA LACTAMASE; CEFALORIDINE; CEFALOTIN; CEFOXITIN; IMIPENEM; NITROCEFIN; PENICILLIN G; TEMOCILLIN; TICARCILLIN;

ANTIBIOTIC RESISTANCE; ARTICLE; DISULFIDE BOND; ENTEROBACTER CLOACAE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SERRATIA MARCESCENS;

AMINO ACID SEQUENCE; BETA-LACTAMASES; BINDING SITES; CARBAPENEMS; DISULFIDES; HYDROLYSIS; KINETICS; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ENTEROBACTER CLOACAE; SERRATIA MARCESCENS;

EID: 0031036293     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199701)27:1<47::AID-PROT6>3.0.CO;2-K     Document Type: Article

References (48)

1. Raquet, X., Lamotte-Brasseur, J., Fonzé, E., Goussard, S., Courvalin, P., Frère, J.M. TEM mutants hydrolysing third generation cephalosporins: A kinetic and molecular modeling analysis. J. Mol. Biol. 244:625-639, 1994.
2. Saves, I., Burlet-Schiltz, O., Maveyraud, L., Samama, J.P., Promé, J.C., Masson, J.M. Mass spectral kinetic study of acylation and deacylation during the hydrolysis of penicillins and cefotaxime by β-lactamase TEM-1 and the G238S mutant. Biochemistry 34:11660-11667, 1995.
3. Matagne, A., Lamotte-Brasseur, J., Dive, G., Knox, J.R., Frere, J.M. Interactions between active-site serine beta-lactamases and compounds bearing a methoxy side chain on the alpha-face of the beta-lactam ring: Kinetic and molecular modeling studies. Biochem. J. 293:607-611, 1993.
4. Davies, J. Inactivation of antibiotics and the dissemination of resistance genes. Science 264:375-382, 1994.
5. Payne, D.J. Metallo-β-lactamases: A new therapeutic challenge. J. Med. Microbiol. 39:93-99, 1993.
6. Yang, Y., Wu, P., Livermore, D.M. Biochemical characterization of a β-lactamase that hydrolyses penems and carbapenems from two Serratia marcescens isolates. Antimicrob. Agents Chemother. 34:755-758, 1990.
7. Naas, T., Vandel, L., Sougakoff W., Livermore, D.M., Nordmann, P. Cloning and sequence analysis of the gene for a carbapenem-hydrolysing class A β-lactamase, Sme-1, from Serratia marcescens S6. Antimicrob. Agents Chemother. 38:1262-1270, 1994.
8. Nordmann, P., Mariotte, S., Naas, T., Labia, R., Nicolas, M.H. Biochemical properties of a carbapenem-hydrolysing β-lactamase from Enterobacter cloacae and cloning of the gene into Escherichia coli. Antimicrob. Agents Chemother. 37:939-946, 1993.
9. Naas, T., Nordmann, P. Analysis of a carbapenem-hydrolysing class A β-lactamase from Enterobacter cloacae and of its Lys-R type regulatory protein. Proc. Natl. Acad. Sci. USA, 91:7693-7697, 1994.
10. Amman, E., Brosius, J., Ptashne, M. Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in E. coli. Gene 25:167-178, 1983.
11. Cantor, C.R., Schimmel, P.R. In: "Biophysical Chemistry." Part II. New York: W.H. Freeman, 1980.
12. Riddles, P.W., Blakeley, R.L., Zerner, B. Reassessment of Cleland's reagent. Methods Enzymol. 91:49, 1983.
13. Matagne, A., Misselyn-Bauduin, A.M., Joris, B., Erpicum, T., Granier, B., Frère, J.M. The diversity of the catalytic properties of class A β-lactamases. Biochem. J. 265:131-146, 1990.
14. De Meester, F., Joris, B., Reckinger, G., Bellefroid-Bourguignon, C., Frère, J.M., Waley, S.G. Automated analysis of enzyme inactivation phenomena. Biochem. Pharmacol. 36:2393-2403, 1987.
15. Devereux, J., Haeberli, P., Smithies, O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acid Res. 12:387-395, 1984.
16. Sutcliffe, M.J., Haneef, I., Carney, D., Blundell, T.L. Knowledge based modelling of homologous proteins. Part I: Three-dimensional frameworks derived from simultaneous superpositon of multiple structures. Prot. Eng. 1:377-384, 1987.
17. Sutcliffe, M.J., Hayes, F.R.F., Blundell, T.L. Knowledge based modelling of homologous proteins. Part II: Rules for the conformations of substituted sidechains. Prot. Eng. 1:385-392, 1987.
18. Herzberg, O. Refined crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.0 Å resolution. J. Mol. Biol. 217:701-719, 1991.
19. Dideberg, O., Charlier, P., Wery, J.P., Dehottay, P., Dusart, J., Erpicum, T., Frère, J.M., Ghuysen, J.M. The crystal structure of the β-lactamase of Streptomyces albus G at 0.3 nm resolution. Biochem. J. 245:911-913, 1987.
20. Knox, J.R., Moews, P.C. Beta-Lactamase of Bacillus licheniformis 749/C refinement at two A resolution and analysis of hydration. J. Mol. Biol. 220:435-455, 1991.
21. Jelsch, C., Lenfant, F., Masson, J.M., Samama, J.P. β-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 Å resolution. FEBS Lett. 299:135-142, 1992.
22. Strynadka, N.C.J., Adachi, H., Jensen, S.E., Johns, K., Sielecki, A., Betzel, C., Sutoh, K., James, M.N.J. Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution. Nature 359:700-705, 1992.
23. Fonzé, E., Charlier, P., To'th, Y., Vermeire, M., Raquet, X., Dubus, A., Frère, J.M. TEM-1 β-lactamase structure solved by molecular replacement and refined structure of the S235A mutant. Acta Crystallogr. D51:682-694, 1995.
24. Dewar, M.J.S., Zoebisch, E.G., Healy, E.F., Stewart, J.J.P. AM1: A new general purpose quantum mechanical molecular model. J. Am. Chem. Soc. 107:3902-3909, 1985.
25. Weiner, S.J., Kollman, P.A., Case, D.A., Singh, U.C., Ghio, G., Alalonga, G., Profeta, S.J., Weiner, P. A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc. 106:765-784, 1984.
26. Joris, B., Ghuysen, J.M., Dive, G., Renard, A., Dideberg, O., Charlier, P., Frère, J.M., Kelly, J., Boyington, J., Moews, P., Knox, J. The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family. Biochem. J. 250:313-324, 1988.
27. Fisher, J., Belasco, J.G., Khosla, S., Knowles, J.R. β-lactamase proceeds via an acyl-enzyme intermediate: Interaction of the E. coli RTEM enzyme with cefoxitin. Biochemistry 19:2895-2901, 1980.
28. Jelsch, C., Mourey, L., Masson, J.M., Samama, J.P. Crystal structure of E. coli TEM-1 β-lactamase. Proteins 16: 364-383, 1993.
29. Moews, P.C., Knox, J.R., Dideberg, O., Charlier, P., Frère, J.M. β-Lactamase of Bacilus licheniformis 749/C at 2 Å resolution. Proteins 7:156-171, 1990.
30. 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 β-lactamase. Prot. Eng. 4:811-819, 1991.
31. Zafaralla, G., Manavathu, E.K., Lerner, S.A., Mobashery, S. Elucidation of the role of arginine-244 in the turnover processes of class A β-lactamases. Biochemistry 31:3847-3852, 1992.
32. Lamotte-Brasseur, J., Dive, G., Dideberg, O., Charlier, P., Frère, J.M., Ghuysen, J.M. Mechanism of acyl transfer by the class A serine β-lactamase of Streptomyces albus G. Biochem. J. 279:213-221, 1991.
33. 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 β-lactamases probed by site-directed mutagenesis and three-dimensional modeling. J. Biol. Chem. 268:3690-3697, 1993.
34. Ambler, R.P., Coulson, A.F.W., 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 β-lactamases. Biochem. J. 276:269-272, 1990.
35. Herzberg, O., Moult, J. Bacterial resistance to β-lactam antibiotics: Crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.5 Å resolution. Science 236:694-701, 1987.
36. Lee, K.Y., Hopkins, J.D., O'Brian, T.F., Syvanen, M. Gly-238-Ser substitution changes the substrate specificity of the SHV class A β-lactamases. Proteins 11:45-51, 1991.
37. Raquet, X., Vanhove, M., Lamotte-Brasseur, J., Goussard, S., Courvalin, P., Frère, J.M. Stability of TEM β-lactamase mutants hydrolysing third generation cephalosporins. Proteins 23:63-72, 1995.
38. Labia, R., Morand, A., Tiwari, K., Sirot, J., Sirot, D., Petit, A. Interactions of new plasmid-mediated β-lactamase with third generation cephalosporins. Rev. Infect. Dis., 10:885-891, 1988.
39. Hall, A., Knowles, J.R. Direct selective pressure on a β-lactamase to analyse molecular changes involved in development of enzyme function. Nature 264:803-804, 1976.
40. Healey, W.J., Labgold, M.R., Richards, J.H. Substrate specificities in class A β-lactamases: preference for penams vs. cephems: The role of residue 237. Proteins 6:275-283, 1989.
41. Parker, A.C., Jeffrey Smith, C. Genetic and biochemical analysis of a novel Ambler class A β-lactamase responsible for cefoxitin resistance in Bacteroides species. Antimicrob. Agents Chemother. 37:1028-1036, 1993.
42. Smith, C.J., Bennet, T.K., Parker, A.C. Molecular and genetic analysis of the Bacteroides uniformis cephalosporinase gene, cblA, encoding the species-specific β-lactamase. Antimicrob. Agents Chemother. 38:1711-1715, 1994.
43. Delaire, M., Labia, R., Samama, J.P., Masson, J.M. Site-directed mutagenesis at the active site of Escherichia coli TEM-1 β-lactamase: Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis. J. Biol. Chem. 267:20600-20606, 1992.
44. Imtiaz, U., Billings, E., Knox, J.R., Manavathu, E.K., Lerner, S.A., Mobashery, S. Inactivation of class A β-lactamases by clavulanic acid: The role of arginine-244 in a proposed nonconcerted sequence of events. J. Am. Chem. Soc. 115:4435-4442, 1993.
45. Vedel, G., Belaaouaj, A., Gilly, L., Labia, R., Philippon, A., Nevot, P., Paul, G. Clinical isolates of Escherichia coli producing TRI β-lactamases: Novel TEM-enzymes conferring resistance to β-lactams inhibitors. J. Antomicrob. Chemother. 30:449-462, 1992.
46. Zafaralla, G., Mobashery, S. Facilitation of the D2-D1 pyrroline tautomerization of carbapenem antibiotics by the highly conserved arginine-244 of class A β-lactamases during the course of turnover. J. Am. Chem. Soc. 114:1505-1506, 1992.
47. Taibi, P., Mobashery, S. Mechanism of turnover of imipenem by the TEM β-lactamase revisited. J. Am. Chem. Soc. 117:7600-7605, 1995.
48. Matagne, A., Lamotte-Brasseur, J., Frère, J.M. Interactions between active-site serine β-lactamases and so-called β-lactamase-stable antibiotics: Kinetic and molecular modeling studies. Eur. J. Biochem. 217:61-67, 1993.