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• W2044667002 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." @default.
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• W2044667002 date "1987-02-01" @default.
• W2044667002 modified "2023-10-16" @default.
• W2044667002 title "Purification and characterization of cystathionine gamma-synthase type II from Bacillus sphaericus" @default.
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• W2044667002 doi "https://doi.org/10.1111/j.1432-1033.1987.tb10742.x" @default.
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