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S-adenosyl-L-homocysteine hydrolase in yeast: key enzyme of methylation metabolism and coordinated regulation with phospholipid synthesis
- Source :
- FEBS letters. 577(3)
- Publication Year :
- 2004
-
Abstract
- S-Adenosyl-l-homocysteine hydrolase (Sah1p, EC 3.3.1.1.) is a key enzyme of methylation metabolism. It catabolizes S-adenosyl-l-homocysteine, which is formed after donation of the activated methyl group of S-adenosyl-l-methionine (AdoMet) to an acceptor, and which acts as strong competitive inhibitor of all AdoMet-dependent methyltransferases. Sah1p is an essential enzyme in yeast and one of the most highly conserved proteins with up to 80% sequence homology throughout all kingdoms of life. SAH1 expression in yeast is subject to the general transcriptional control of phospholipid synthesis. Profound changes in cellular lipid composition upon depletion of Sah1p support the notion of a tight interaction between lipid metabolism and Sah1p function.
- Subjects :
- Genetic Markers
Methyltransferase
Saccharomyces cerevisiae Proteins
Hydrolases
Genes, Fungal
Molecular Sequence Data
Biophysics
Phospholipid
Saccharomyces cerevisiae
Biology
Biochemistry
Methylation
Models, Biological
chemistry.chemical_compound
Structural Biology
S-adenosyl-L-homocysteine hydrolase
Gene Expression Regulation, Fungal
Hydrolase
Consensus Sequence
Genetics
Amino Acid Sequence
Promoter Regions, Genetic
Molecular Biology
Conserved Sequence
Phospholipids
chemistry.chemical_classification
Sequence Homology, Amino Acid
Lipid metabolism
Cell Biology
Lipid
S-Adenosylhomocysteine
Yeast
Enzyme
chemistry
SAH1
Gene Deletion
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 577
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....fd0a06a64a119a428fb6d01426ddf468