Purification of acetyl coenzyme A: deacetylacephalosporin C O-acetyltransferase from Acremonium chrysogenum.
Acetyl CoA: deacetylcephalosporin C O-acetyltransferase, which catalyzes the final step of the biosynthetic pathway to cephalosporin C, was stabilized by a buffer solution containing 7-aminocephalosporanic acid and purified over 1300-fold from Acremonium chrysogenum. The purified enzyme has a molecular weight of 55,000 as measured by gel filtration. SDS-polyacrylamide gel electrophoresis showed two subunit bands corresponding to molecular weights of 27,000 and 14,000. The enzyme has an isoelectoric point at pH 4.0 and optimum activity at pH 7.5.
Matsuyama
K
K
Shiraoi Pharmaceutical Plant, Asahi Chemical Industry Co., Ltd., Hokkaido, Japan.
Matsumoto
H
H
Matsuda
A
A
Sugiura
H
H
Komatsu
K
K
Ichikawa
S
S
D000123:Acetyltransferases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000164:Acremonium / Q000201:enzymology*; D000595:Amino Acid Sequence; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008969:Molecular Sequence Data
D046911:Macromolecular Substances; D000123:Acetyltransferases; C018707:acetyl CoA-deacetylcephalosporin C acetyltransferase