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