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O-acetylhomoserine (thiol)-lyase activity

Known as: L-methionine formation, direct, from O-acetyl-L-homoserine, O-acetyl-L-homoserine:methanethiol 3-amino-3-carboxypropyltransferase activity, L-methionine synthesis, direct, from O-acetyl-L-homoserine 
Catalysis of the reaction: O-acetyl-L-homoserine + methanethiol = L-methionine + acetate. Also reacts with other thiols and H2S, producing… Expand
National Institutes of Health

Papers overview

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2015
2015
A Ag12(SCH2C10H7)6(CF3CO2)6(CH3CN)6 (1) nanocluster modified using naphthalen-2-yl-methanethiol was synthesized and structurally… Expand
2010
2010
In the present work, methanethiol and dimethyldisulfide were investigated as sulfur source for methionine synthesis in… Expand
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2006
2006
The interaction of methanethiol molecules CH3SH with the Au(111) surface is investigated, and it is found for the first time that… Expand
2003
2003
To gain insight into the evolution of the methionine biosynthesis pathway, in vivo complementation tests were performed. The… Expand
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Highly Cited
1999
Highly Cited
1999
Oxidation of methionine residues in proteins to methionine sulfoxide can be reversed by the enzyme peptide methionine sulfoxide… Expand
1975
1975
Homoserine transacetylase (EC 2.3.1.31), the first enzyme of methionine biosynthesis, has been purified to near homogeneity from… Expand
1975
1975
These experiments compared the metabolism of the N-acetylated derivatives of D- or L-methionine to that of L-methionine. Spargue… Expand
1971
1971
Abstract Cell-free extracts of Bacillus subtilis catalyze the formation of O-acetylhomoserine from acetyl-CoA and L-homoserine… Expand
Highly Cited
1970
Highly Cited
1970
  • T. Wainwright
  • Journal of general microbiology
  • 1970
  • Corpus ID: 31762464
SUMMARY: Methionine-requiring mutants of Saccharomyces cerevisiae produce large amounts of hydrogen sulphide from sulphate… Expand
Highly Cited
1967
Highly Cited
1967
Abstract "Activated" forms of l-homoserine have been shown to be more readily utilized as substrates than homoserine for the… Expand
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