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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC00603
S-adenosyl-L-homocysteine hydrolase signatures


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00603

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.

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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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