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S ‐Adenosyl‐ l ‐homocysteine hydrolase in yeast: key enzyme of methylation metabolism and coordinated regulation with phospholipid synthesis
Author(s) -
Tehlivets Oksana,
Hasslacher Meinhard,
Kohlwein Sepp D.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.10.057
Subject(s) - methylation , methyltransferase , biochemistry , homocysteine , enzyme , yeast , hydrolase , methionine , biology , metabolism , chemistry , amino acid , gene
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.