Purification and properties of Saccharomyces cerevisiae cystathionine beta-synthase.
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.
Laboratory of Environmental Hygiene Chemistry, Faculty of Pharmaceutical Sciences, Okayama University, Japan.
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B
Ono
K
K
Kijima
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T
Inoue
S
S
Miyoshi
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A
Matsuda
S
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Shinoda
D000595:Amino Acid Sequence; D005075:Biological Evolution; D003541:Cystathionine beta-Synthase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D004789:Enzyme Activation; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D017421:Sequence Analysis; D017385:Sequence Homology
D003541:Cystathionine beta-Synthase