ID | 10571 |
Eprint ID | 10571
|
FullText URL | |
Author |
Tashiro (Yamada), Yuriko
Tanaka, Hidehiko
Inagaki, Kenji
Kaken ID
researchmap
|
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 |
Japanese
|
File Version | publisher
|
Refereed |
False
|
Eprints Journal Name | srfa
|