Purification from Cephalosporium acremonium of the initial enzyme unique to the biosynthesis of penicillins and cephalosporins.
The stability of the unstable enzyme, delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) synthetase from Cephalosporium acremonium C-10, was increased 10-fold which facilitated its purification. The active enzyme was purified over 100 fold to electrophoretic homogeneity by protamine sulfate treatment, ammonium sulfate fractionation, gel filtration and hydrophobic interaction chromatography. It appears to have a minimal size of 360 kDa based on SDS-polyacrylamide gel electrophoresis.
Zhang
J Y
JY
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Demain
A L
AL
D000164:Acremonium / Q000201:enzymology*; D002511:Cephalosporins / Q000096:biosynthesis*; D002845:Chromatography; D008970:Molecular Weight; D010406:Penicillins / Q000096:biosynthesis*; D010453:Peptide Synthases / Q000302:isolation & purification*; D013696:Temperature; D013997:Time Factors
D002511:Cephalosporins; D010406:Penicillins; D010453:Peptide Synthases; C095368:alpha-aminoadipyl-cysteinyl-valine synthetase