Purification and characterization of O-Acetylserine sulfhydrylase of Corynebacterium glutamicum.
We highly purified O-acetylserine sulfhydrylase from the glutamate-producing bacterium Corynebacterium glutamicum. The molecular mass of the purified enzyme was 34,500 as determined by SDS-polyacrylamide gel electrophoresis, and 70,800 as determined by gel filtration chromatography. It had an apparent Km of 7.0 mM for O-acetylserine and a Vmax of 435 micromol min-1 (mg x protein)-1. This is the first report of the cysteine biosynthetic enzyme of C. glutamicum in purified form.
Wada
Masaru
M
Department of Bioscience, Fukui Prefectural University, 4-1-1 Kenjyojima, Matsuoka-cho, Fukui 910-1195, Japan. wada@chem.agr.hokudai.ac.jp
Awano
Naoki
N
Yamazawa
Hiroyuki
H
Takagi
Hiroshi
H
Nakamori
Shigeru
S
D002850:Chromatography, Gel; D048230:Corynebacterium glutamicum / Q000201:enzymology* / Q000235:genetics; D003547:Cysteine Synthase / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008970:Molecular Weight; D016133:Polymerase Chain Reaction
D004269:DNA, Bacterial; D003547:Cysteine Synthase