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PMID: 3128280 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.

The Biochemical journal ·Vol. 250 ·No. 2 ·1988-03-01 ·Pages 313-24

Joris B, Ghuysen JM, Dive G, Renard A, Dideberg O, Charlier P, Frère JM, Kelly JA, Boyington JC, Moews PC

Abstract

Homology searches and amino acid alignments, using the Streptomyces R61 DD-peptidase/penicillin-binding protein as reference, have been applied to the beta-lactamases of classes A and C, the Oxa-2 beta-lactamase (considered as the first known member of an additional class D), the low-Mr DD-peptidases/penicillin-binding proteins (protein no. 5 of Escherichia coli and Bacillus subtilis) and penicillin-binding domains of the high-Mr penicillin-binding proteins (PBP1A, PBP1B, PBP2 and PBP3 of E. coli). Though the evolutionary distance may vary considerably, all these penicillin-interactive proteins and domains appear to be members of a single superfamily of active-site-serine enzymes distinct from the classical trypsin or subtilisin families. The amino acid alignments reveal several conserved boxes that consist of strict identities or homologous amino acids. The significance of these boxes is highlighted by the known results of X-ray crystallography, chemical derivatization and site-directed-mutagenesis experiments.

MeSH Terms
Amino Acid Sequence Bacterial Proteins Binding Sites Biological Evolution Carrier Proteins Escherichia coli Proteins Hexosyltransferases Molecular Sequence Data Muramoylpentapeptide Carboxypeptidase Penicillin-Binding Proteins Penicillins/metabolism Peptide Hydrolases Peptidoglycan Glycosyltransferase Peptidyl Transferases Protein Conformation Serine Serine-Type D-Ala-D-Ala Carboxypeptidase Streptomyces/enzymology beta-Lactamases
Chemicals
Bacterial Proteins Carrier Proteins Escherichia coli Proteins Penicillin-Binding Proteins Penicillins Serine Peptidyl Transferases Hexosyltransferases Peptidoglycan Glycosyltransferase penicillin-binding protein 1B, E coli Peptide Hydrolases Serine-Type D-Ala-D-Ala Carboxypeptidase Muramoylpentapeptide Carboxypeptidase beta-Lactamases
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Joris B
Service de Microbiologie, Université de Liège, Belgium.
Ghuysen J M
Dive G
Renard A
Dideberg O
Charlier P
Frère J M
Kelly J A
Boyington J C
Moews P C
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42 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2500313
Published
1988-03-01
Pages
313-24
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1148858
Subset
IM
Grants
NIGMS NIH HHS · GM-37742 · United States
NCRR NIH HHS · RR-01955 · United States
External Links
PubMed source DOI: 10.1042/bj2500313 PMC Full Text View journal details
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