Purification of properties of Saccharomyces cerevisiae cystathionine β‐synthase

Bun‐Ichiro ‐I Ono, Kazuyasu Kijima, Toyomi Inoue, Shin‐Ichi ‐I Miyoshi, Akio Matsuda, Sumio Shinoda

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)


Cystathionine β‐synthase (β‐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 β‐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.

Original languageEnglish
Pages (from-to)333-339
Number of pages7
Issue number3
Publication statusPublished - Mar 1994


  • Cystathionine
  • Saccharomyces cerevisiae
  • amino acid sequence analysis
  • catalytic properties
  • enzyme purification
  • β‐synthase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Genetics


Dive into the research topics of 'Purification of properties of Saccharomyces cerevisiae cystathionine β‐synthase'. Together they form a unique fingerprint.

Cite this