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| PROSITE documentation PDOC00603 [for PROSITE entry PS00739] |
S-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.
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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 |
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