|PROSITE documentation PDOC00603 [for PROSITE entry PS00738]|
S-adenosyl-L-homocysteine hydrolase (EC 220.127.116.11) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydratation of S-adenosyl-L-homocysteine into adenosine and homocysteine. AdoHcyase is an ubiquitous enzyme which binds and requires NAD+ as a cofactor.
AdoHcyase is a highly conserved protein  of about 430 to 470 amino acids. As signature patterns, we selected 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 AdoHcyase; a region thought to be involved in NAD-binding.Last update:
April 2006 / Pattern revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Sganga M.W. Aksamit R.R. Cantoni G.L. Bauer C.E.|
|Title||Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 89:6328-6332(1992).|