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ID 10571
Eprint ID
10571
FullText URL
Author
Tashiro (Yamada), Yuriko
Tanaka, Hidehiko
Abstract
Some properties of D-amino scid acetyltransferase purified from Saccharomyces cerevisiae were investigated. The enzyme was purified to homogeneity by ammonium sulfate fractionation, column chromatographies on DEAE-Toyopearl 650M, Sephacryl S-200, QAE-Toyopearl 550C and affinity chromatography with D-glutamate as a ligand. The molecular weight was estimated to be about 53,000 by gel filtration. Relative molecular mass studies indicated that the enzyme was a monomer structure. The purified enzyme had an optimum pH of 8.4 and an optimum temperature of 40C. The Km values of the purified enzyme determined with tryptophan and acetyl-CoA were 4.5 * 10 -3M, respectively. The 20 residues of N-terminal amino acid sequence were analyzed.
Keywords
D-amino acid acetyltransferase
Saccharomyces cerevisiae
acyl donor
affinity chromatography
Published Date
2004-02
Publication Title
岡山大学農学部学術報告
Publication Title Alternative
Scientific reports of the Faculty of Agriculture, Okayama University
Volume
volume93
Issue
issue1
Publisher
岡山大学農学部
Publisher Alternative
Faculty of Agriculture,Okayama University
Start Page
13
End Page
18
ISSN
0474-0254
NCID
AN00033029
Content Type
Departmental Bulletin Paper
language
日本語
File Version
publisher
Refereed
False
Eprints Journal Name
srfa