Open AccessPurification of Acetyl Coenzyme A: Deacetylacephalosporin CO-Acetyltransferase fromAcremonium chrysogenum
Author(s) -
Kenji Matsuyama,
Hideyuki Matsumoto,
Akio Matsuda,
Hiroyosi Sugiura,
Kenichi Komatsu,
Sigeaki Ichikawa
Publication year - 1992
Publication title -
bioscience, biotechnology, and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.56.1410
Subject(s) - acremonium , acetyltransferase , chemistry , penicillium chrysogenum , biochemistry , biology , stereochemistry , botany , acetylation , gene
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.