PROSITE documentation PDOC00603S-adenosyl-L-homocysteine hydrolase signatures
S-adenosyl-L-homocysteine hydrolase (EC 3.3.1.1) (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 [1] 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). | |
PubMed ID | 1631127 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)