EC |
3.13.2.1 |
Accepted name: |
adenosylhomocysteinase |
Reaction: |
S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine |
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For diagram of reaction mechanism, click here |
Other name(s): |
S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase (ambiguous); adenosylhomocysteine hydrolase; S-adenosylhomocysteinase; SAHase; AdoHcyase |
Systematic name: |
S-adenosyl-L-homocysteine hydrolase |
Comments: |
The enzyme contains one tightly bound NAD+ per subunit. This appears to bring about a transient oxidation at C-3′ of the 5′-deoxyadenosine residue, thus labilizing the thioether bond [2] (for mechanism, click here), cf. EC 5.5.1.4, inositol-3-phosphate synthase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9025-54-1 |
References: |
1. |
de la Haba, G. and Cantoni, G.L. The enzymatic synthesis of S-adenosyl-L-homocysteine from adenosine and homocysteine. J. Biol. Chem. 234 (1959) 603–608. [PMID: 13641268] |
2. |
Palmer, J.L. and Abeles, R.H. The mechanism of action of S-adenosylhomocysteinase. J. Biol. Chem. 254 (1979) 1217–1226. [PMID: 762125] |
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[EC 3.13.2.1 created 1961 as EC 3.3.1.1, modified 2004, transferred 2022 to EC 3.13.2.1] |
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