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B6db references: 94287710

type Journal Article
authors Ono, B.; Kijima, K.; Inoue, T.; Miyoshi, S.; Matsuda, A.; Shinoda, S.
title Purification and properties of Saccharomyces cerevisiae cystathionine beta-synthase
journal Yeast
ui 94287710
year (1994)
volume 10
number 3
pages 333-9.
keywords Amino Acid Sequence
abstract 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 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.
last changed 2002/11/12 16:17

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