Open AccessA Single Amino Acid Substitution Converts γ-Glutamyltranspeptidase to a Class IV Cephalosporin Acylase (Glutaryl-7-Aminocephalosporanic Acid Acylase)
Author(s) -
Hideyuki Suzuki,
Chinatsu Miwa,
Sayaka Ishihara,
Hidehiko Kumagai
Publication year - 2004
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.70.10.6324-6328.2004
Subject(s) - residue (chemistry) , cephalosporin c , cephalosporin , escherichia coli , chemistry , penicillin amidase , amino acid substitution , stereochemistry , cephalosporin antibiotic , biochemistry , mutation , antibiotics , gene
The aspartyl residue at position 433 of gamma-glutamyltranspeptidase of Escherichia coli K-12 was replaced by an asparaginyl residue. This substitution enabled gamma-glutamyltranspeptidase to deacylate glutaryl-7-aminocephalosporanic acid, producing 7-aminocephalosporanic acid, which is a starting material for the synthesis of semisynthetic cephalosporins.