Conserved Site

S-adenosyl-L-homocysteine hydrolase, conserved site (IPR020082)

Short name: S-Ado-L-homoCys_hydrolase_CS


Adenosylhomocysteinase (S-adenosyl-L-homocysteine hydrolase, EC: (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+ [PMID: 9586999,PMID: 16061414,PMID: 11325033,PMID: 15165742].

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.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004013 adenosylhomocysteinase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns
PROSITE patterns