|
type |
Journal Article |
authors |
Kanzaki, H.; Kobayashi, M.; Nagasawa, T.; Yamada, H. |
title |
Purification and characterization of cystathionine gamma-synthase type II from Bacillus sphaericus |
journal |
Eur J Biochem |
Activity |
2.5.1.48 |
ui |
87133554 |
year |
(1987) |
volume |
163 |
number |
1 |
pages |
105-12. |
| |
keywords |
Bacillus/*enzymology |
abstract |
Cystathionine gamma-synthase type II, which catalyzes L-cystathionine synthesis from O-acetyl-L-homoserine and L-cysteine was purified from Bacillus sphaericus (IFO 3536) in seven steps. The purified enzyme appeared to be homogeneous by the results of polyacrylamide electrophoresis and ampholyte electrofocusing. The enzyme is a typical pyridoxal-P dependent enzyme, has a molecular mass of 165 kDa and consists of four subunits identical in molecular mass. The enzyme catalyzed the gamma-replacement reaction and the elimination reaction was hardly detected even when a large amount of enzyme was added. In the replacement reaction, O-acetyl-L-homoserine and the following thiol compounds: L and D-cysteine, L and D-homocysteine, sodium sulfide, various alkyl and aryl mercaptans, acted as the most suitable substrate to produce L-cystathionine and the corresponding S-substituted L- homocysteine derivatives. |
last changed |
2003/03/17 15:03 |
|