Standard Numbering Scheme for Class B β-Lactamases

Unlike for classes A and B, a standardized amino acid numbering scheme has not been proposed for the class C (AmpC) β-lactamases, which complicates communication in the field. Here, we propose a scheme developed through a collaborative approach that considers both sequence and structure, preserves traditional numbering of catalytically important residues (Ser64, Lys67, Tyr150, and Lys315), is adaptable to new variants or enzymes yet to be discovered and includes a variation for genetic and epidemiological applications.

[1]  A. MacGowan,et al.  Nucleotide and Amino Acid Sequences of the Metallo-β-Lactamase, ImiS, from Aeromonas veronii bv. sobria , 1998, Antimicrobial Agents and Chemotherapy.

[2]  S. G. Waley,et al.  The production and molecular properties of the zinc beta-lactamase of Pseudomonas maltophilia IID 1275. , 1985, The Biochemical journal.

[3]  M. Malamy,et al.  Sequencing the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus beta-lactamase II , 1990, Journal of bacteriology.

[4]  Y. Gluzman,et al.  Cloning and sequencing of the class B beta-lactamase gene (ccrA) from Bacteroides fragilis TAL3636 , 1990, Antimicrobial Agents and Chemotherapy.

[5]  R. Shaw,et al.  Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene , 1988, Journal of bacteriology.

[6]  O. Massidda,et al.  The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases , 1991, Journal of bacteriology.

[7]  J M Ghuysen,et al.  A standard numbering scheme for the class A beta-lactamases. , 1991, The Biochemical journal.

[8]  J. Frère,et al.  An overview of the kinetic parameters of class B beta-lactamases. , 1993, The Biochemical journal.

[9]  K. Bush,et al.  Carbapenem-hydrolyzing beta-lactamases , 1997, Antimicrobial agents and chemotherapy.

[10]  I. Taylor,et al.  The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution. , 1998, Journal of molecular biology.

[11]  D. Vanderwall,et al.  Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase. , 1998, Chemistry & biology.

[12]  F. Winkler,et al.  Refined crystal structure of β-lactamase from Citrobacter freundiiindicates a mechanism for β-lactam hydrolysis , 1990, Nature.

[13]  A. Carfi The 3-D structure of a zinc metallo-β-lactarnase from Bacillus cereus reveals a new type of protein fold , 1995 .

[14]  N. Woodford,et al.  Carbapenemases of Chryseobacterium(Flavobacterium) meningosepticum: Distribution ofblaB and Characterization of a Novel Metallo-β-Lactamase Gene, blaB3, in the Type Strain, NCTC 10016 , 2000, Antimicrobial Agents and Chemotherapy.

[15]  E. Abraham,et al.  An Enzyme from Bacteria able to Destroy Penicillin , 1940, Nature.

[16]  J. Frère,et al.  Sequence and comparative analysis of three Enterobacter cloacae ampC beta-lactamase genes and their products. , 1988, The Biochemical journal.

[17]  Gianfranco Amicosante,et al.  Structure of In31, ablaIMP-Containing Pseudomonas aeruginosa Integron Phyletically Related to In5, Which Carries an Unusual Array of Gene Cassettes , 1999, Antimicrobial Agents and Chemotherapy.

[18]  J. Frère,et al.  Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile. , 1998, The Biochemical journal.

[19]  J. Frère,et al.  Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor. , 2000, Biochemistry.

[20]  J. Frère,et al.  The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. , 1995, The EMBO journal.

[21]  R. Ambler,et al.  The structure of beta-lactamases. , 1980, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[22]  G. Cornaglia,et al.  Cloning and Characterization of blaVIM, a New Integron-Borne Metallo-β-Lactamase Gene from a Pseudomonas aeruginosa Clinical Isolate , 1999, Antimicrobial Agents and Chemotherapy.

[23]  R. Levesque,et al.  Molecular Heterogeneity of the L-1 Metallo-β-Lactamase Family from Stenotrophomonas maltophilia , 1998, Antimicrobial Agents and Chemotherapy.

[24]  G. Jacoby,et al.  A functional classification scheme for beta-lactamases and its correlation with molecular structure , 1995, Antimicrobial agents and chemotherapy.

[25]  J. Frère,et al.  The 3‐D structure of a zinc metallo‐beta‐lactamase from Bacillus cereus reveals a new type of protein fold. , 1995 .

[26]  J. Frère,et al.  1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus. , 1998, Acta crystallographica. Section D, Biological crystallography.

[27]  K. Watanabe,et al.  Nucleotide sequence of the beta-lactamase gene of alkalophilic Bacillus sp. strain 170. , 1985, Journal of general microbiology.

[28]  G. Cornaglia,et al.  Characterization of the Metallo-β-Lactamase Determinant of Acinetobacter baumannii AC-54/97 Reveals the Existence of blaIMP Allelic Variants Carried by Gene Cassettes of Different Phylogeny , 2000, Antimicrobial Agents and Chemotherapy.

[29]  F. Yoshimura,et al.  Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance , 1994, Antimicrobial Agents and Chemotherapy.

[30]  Timothy R. Walsh,et al.  Sequence analysis of the L1 metallo-β-lactamase from Xanthomonas maltophilia , 1994 .

[31]  Gianfranco Amicosante,et al.  The Legionella (Fluoribacter)gormanii Metallo-β-Lactamase: a New Member of the Highly Divergent Lineage of Molecular-Subclass B3 β-Lactamases , 2000, Antimicrobial Agents and Chemotherapy.

[32]  P. Fitzgerald,et al.  Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution. , 1998, Biochemistry.

[33]  P. Nordmann,et al.  Molecular and Biochemical Heterogeneity of Class B Carbapenem-Hydrolyzing β-Lactamases in Chryseobacterium meningosepticum , 2000, Antimicrobial Agents and Chemotherapy.

[34]  J. Frère,et al.  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. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[35]  O. Herzberg,et al.  Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis , 1996 .

[36]  M. Thaller,et al.  Metallo-β-Lactamase Producers in Environmental Microbiota: New Molecular Class B Enzyme inJanthinobacterium lividum , 2001, Antimicrobial Agents and Chemotherapy.

[37]  S. Ichiyama,et al.  Multifocal outbreaks of metallo-beta-lactamase-producing Pseudomonas aeruginosa resistant to broad-spectrum beta-lactams, including carbapenems , 1996, Antimicrobial agents and chemotherapy.

[38]  F. Winkler,et al.  Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis. , 2001, Nature.

[39]  B. Sutton,et al.  Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme. , 1998, Biochemistry.

[40]  Thierry Naas,et al.  Characterization of VIM-2, a Carbapenem-Hydrolyzing Metallo-β-Lactamase and Its Plasmid- and Integron-Borne Gene from a Pseudomonas aeruginosa Clinical Isolate in France , 2000, Antimicrobial Agents and Chemotherapy.

[41]  J. Frère,et al.  X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form. , 1998, Acta crystallographica. Section D, Biological crystallography.

[42]  O. Herzberg,et al.  Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis. , 1996, Structure.

[43]  P. Nordmann,et al.  Molecular characterization of a carbapenem-hydrolyzing beta-lactamase from Chryseobacterium (Flavobacterium) indologenes. , 1999, FEMS microbiology letters.

[44]  M. Hussain,et al.  Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli , 1985, Journal of bacteriology.