Abstract
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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Substitution
-
Base Sequence
-
DNA, Bacterial / genetics
-
Escherichia coli K12 / enzymology
-
Escherichia coli K12 / genetics
-
Hydrogen-Ion Concentration
-
Magnetic Resonance Spectroscopy
-
Mutagenesis, Site-Directed
-
Penicillin Amidase / chemistry
-
Penicillin Amidase / genetics*
-
Penicillin Amidase / metabolism*
-
Substrate Specificity
-
gamma-Glutamyltransferase / chemistry
-
gamma-Glutamyltransferase / genetics*
-
gamma-Glutamyltransferase / metabolism*
Substances
-
DNA, Bacterial
-
gamma-Glutamyltransferase
-
Penicillin Amidase
-
glutarylamidocephalosporanic acid acylase