PURIFICATION AND PROPERTIES OF SACCHAROMYCES-CEREVISIAE CYSTATHIONINE BETA-SYNTHASE

被引：28

作者：

ONO, BI ^{[1
]}

KIJIMA, K ^{[1
]}

INOUE, T ^{[1
]}

MIYOSHI, SI ^{[1
]}

MATSUDA, A ^{[1
]}

SHINODA, S ^{[1
]}

机构：

[1] ASAHI CHEM IND CO LTD,DIV PHARMACEUT RES & DEV,FUJI 416,SHIZUOKA,JAPAN

来源：

YEAST | 1994年 / 10卷 / 03期

关键词：

CYSTATHIONINE; BETA-SYNTHASE; ENZYME PURIFICATION; AMINO ACID SEQUENCE ANALYSIS; CATALYTIC PROPERTIES; SACCHAROMYCES CEREVISIAE;

D O I：

10.1002/yea.320100306

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cystathionine beta-synthase (beta-CTSase), which catalyses cystathionine synthesis from serine and homocysteine, was purified to homogeneity from Saccharomyces cerevisiae. The molecular mass of the enzyme was estimated to be 235 kDa by gel filtration and 55 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, indicating that it is a homotetramer. The N-terminal amino acid sequence of the enzyme perfectly coincided with that deduced from the nucleotide sequence of CYS4, except for the absence of initiation methionine. The purified beta-CTSase catalysed cysteine synthesis from serine (or O-acetylserine) and H2S. From this finding, we discuss the multifunctional nature and evolutionary divergence of S-metabolizing enzymes.

引用

页码：333 / 339

页数：7

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