Purification and characterization of cloned isopenicillin N synthetase.
Isopenicillin N synthetase (IPS) cloned from Cephalosporium acremonium has been isolated from transformed Escherichia coli and purified to homogeneity. The resulting, abundant, recombinant protein, whilst undergoing slightly different N-terminal processing to that observed for the fungally-derived protein, has identical kinetics for the conversion of LLD-aminoadipoyl-cysteinyl-valine to isopenicillin N. Recombinant IPS converts analogue substrates into unusual beta-lactam antibiotics in exactly the same way as the fungal protein.
Baldwin
J E
JE
Killin
S J
SJ
Pratt
A J
AJ
Sutherland
J D
JD
Turner
N J
NJ
Crabbe
M J
MJ
Abraham
E P
EP
Willis
A C
AC
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004798:Enzymes / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D004926:Escherichia coli; D009682:Magnetic Resonance Spectroscopy; D010088:Oxidoreductases; D011994:Recombinant Proteins; D013379:Substrate Specificity
D004798:Enzymes; D011994:Recombinant Proteins; D010088:Oxidoreductases; C038370:isopenicillin N synthetase