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PROSITE documentation PDOC00603 [for PROSITE entry PS00738]

S-adenosyl-L-homocysteine hydrolase signatures





Description

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

ADOHCYASE_1, PS00738; S-adenosyl-L-homocysteine hydrolase signature 1  (PATTERN)

ADOHCYASE_2, PS00739; S-adenosyl-L-homocysteine hydrolase signature 2  (PATTERN)


Reference

1AuthorsSganga M.W. Aksamit R.R. Cantoni G.L. Bauer C.E.
TitleMutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus.
SourceProc. Natl. Acad. Sci. U.S.A. 89:6328-6332(1992).
PubMed ID1631127



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