The effect of cysteine mutations on recombinant deacetoxycephalosporin C synthase from S. clavuligerus.
Cysteines 100, 155, and 197 of recombinant deacetoxycephalosporin C synthase were mutated to alanine residues. The C100A mutant had properties similar to those of the wild-type enzyme, but mutation of Cys-155 and Cys-197 reduced enzyme activity with penicillin N and penicillin G to different extents.
Lee
H J
HJ
Oxford Centre for Molecular Sciences, Dyson Perrins Laboratory, South Parks Road, Oxford, OX1 3QY, United Kingdom.
Lloyd
M D
MD
Harlos
K
K
Schofield
C J
CJ
D019943:Amino Acid Substitution; D003545:Cysteine; D019751:Intramolecular Transferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D010400:Penicillin G / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
D046915:Penicillin-Binding Proteins; D010406:Penicillins; D011994:Recombinant Proteins; D019751:Intramolecular Transferases; C038371:deacetoxycephalosporin C synthetase; D003545:Cysteine; C006414:penicillin N; D010400:Penicillin G