| Description | Adenosylhomocysteinase (S-adenosyl-L-homocysteine hydrolase, ) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. This enzyme is ubiquitous, highly conserved, and may play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. AdoHcyase requires NAD+ as a cofactor and contains a central glycine-rich region which is thought to be involved in NAD-binding. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+ [ , , , ].This entry represents two highly conserved regions. The first pattern is located in the N-terminal section; the second is derived from a glycine-rich region in the central part of S-adenosyl-L-homocysteine hydrolase, a region thought to be involved in NAD-binding. | Name | S-adenosyl-L-homocysteine hydrolase, conserved site |
| Short Name | S-Ado-L-homoCys_hydrolase_CS | Type | Conserved_site |
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