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PMID: 6795623 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type.

Jaurin B, Grundström T

Abstract

A 1536-nucleotide-long sequence that carries the ampC beta-lactamase gene of the Escherichia coli K-12 chromosome has been determined. This gene codes for a protein of 377 amino acids, of which the first 19 amino acids form a signal peptide. The molecular weight of the mature enzyme was determined to be 39,600. The ampC beta-lactamase with a substrate specificity for cephalosporins showed no significant sequence homologies with beta-lactamases of the penicillinase type or with D-alanine carboxypeptidases. However, because the region around serine-80 of the ampC beta-lactamase has extensive homology with an active-site fragment of the Pseudomonas aeruginosa cephalosporinase, we suggest that the ampC cephalosporinase as well as related cephalosporinases form a distinct group of serine beta-lactamases that have an evolutionary origin different from that of the serine penicillinases and thus constitute a new class of beta-lactamases.

MeSH Terms
Base Sequence Binding Sites Biological Evolution Cephalosporinase/genetics Escherichia coli/enzymology,genetics Genes Genes, Bacterial Genes, Regulator Serine Transcription, Genetic beta-Lactamases/classification,genetics
Chemicals
Serine Cephalosporinase beta-Lactamases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Jaurin B
Grundström T
References (36)
36 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1981-08-00
Pages
4897-901
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC320287
Subset
IM
Databases
GENBANK
J01583, J01611
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