Standard numbering scheme for class B β-lactamases
On the basis of the known sequences, three different lineages, identified as subclasses B1, B2, and B3, can be characterized. Subclass B1 contains most known metallo- beta -lactamases, including the beta -lactamase II (BcII) proteins from Bacillus cereus or other Bacillus spp. and Bacillus sp. strai...
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Published in | Antimicrobial agents and chemotherapy Vol. 45; no. 3; pp. 660 - 663 |
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Main Authors | , , , , , |
Format | Journal Article Web Resource |
Language | English |
Published |
Washington, DC
American Society for Microbiology
01.03.2001
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Subjects | |
Online Access | Get full text |
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Summary: | On the basis of the known sequences, three different lineages, identified as subclasses B1, B2, and B3, can be characterized. Subclass B1 contains most known metallo- beta -lactamases, including the beta -lactamase II (BcII) proteins from Bacillus cereus or other Bacillus spp. and Bacillus sp. strain 170, the CcrA (also named CfiA) proteins of Bacteroides fragilis, the BlaB proteins from Chryseobacterium meningosepticum, the IND-1 enzyme from Chryseobacterium indologenes, the IMP proteins found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens, Klebsiella pneumoniae (GenBank EMBL accession no. D29636), and Acinetobacter baumannii, and the VIM proteins found in some P. aeruginosa clinical isolates. Subclass B2 includes the enzymes produced by various species of Aeromonas (CphA, ImiS, and CphA2) and the Sfh-I beta -lactamase (GenBank accession no. AF197943) from Serratia fonticola. Finally, subclass B3 includes the L1 proteins from Stenotrophomonas maltophilia, the GOB proteins from C. meningosepticum, the FEZ-1 enzyme from Legionella gormanii, and the THIN-B beta -lactamase produced by Janthinobacterium lividum. In order to facilitate the comparative analysis of the structures and of the catalytic mechanisms, we would like to propose a standard numbering scheme for the class B beta -lactamases, the BBL numbering, by analogy with the ABL numbering which has been widely accepted for class A beta -lactamases. For the class B enzymes, the task was complicated by insertions and deletions and by the generally low degree of similarity but facilitated by the availability of some three-dimensional structures, which allowed the identification of homologous secondary structure elements, even when the sequence similarity way not obvious. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 scopus-id:2-s2.0-0035119114 Members are listed in the Appendix. Corresponding author. Mailing address: Centre for Protein Engineering, B6 Sart Tilman, University of Liège, B4000 Liège, Belgium. Phone: 32-043663419. Fax: 32-043663364. E-mail: mgalleni@ulg.ac.be. |
ISSN: | 0066-4804 1098-6596 1098-6596 |
DOI: | 10.1128/AAC.45.3.660-663.2001 |