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B6db references: 87133554

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

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