ExplorEnz: EC 3.13.2.3

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3.13.2.3

Accepted name:

(R)-S-adenosyl-L-methionine hydrolase (adenosine-forming)

Reaction:

(R)-S-adenosyl-L-methionine + H₂O = adenosine + L-methionine

Other name(s):

SAM hydroxide adenosyltransferase

Systematic name:

(R)-S-adenosyl-L-methionine hydrolase (adenosine-forming)

Comments:

The enzyme, found in bacteria and archaea, is involved in removing the (R) isomer of S-adenosyl-L-methionine from the cell. It catalyses a nucleophilic attack of water at the C5′ carbon of S-adenosyl-L-methionine to generate adenosine and L-methionine.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Eustaquio, A.S., Harle, J., Noel, J.P. and Moore, B.S. S-Adenosyl-L-methionine hydrolase (adenosine-forming), a conserved bacterial and archaeal protein related to SAM-dependent halogenases. ChemBioChem 9 (2008) 2215–2219. [DOI] [PMID: 18720493]
2.	Deng, H., McMahon, S.A., Eustaquio, A.S., Moore, B.S., Naismith, J.H. and O'Hagan, D. Mechanistic insights into water activation in SAM hydroxide adenosyltransferase (duf-62). ChemBioChem 10 (2009) 2455–2459. [DOI] [PMID: 19739191]
3.	Kornfuehrer, T., Romanowski, S., de Crecy-Lagard, V., Hanson, A.D. and Eustaquio, A.S. An enzyme containing the conserved domain of unknown function DUF62 acts as a stereoselective (Rs ,Sc)-S-adenosylmethionine hydrolase. Chembiochem 21 (2020) 3495–3499. [DOI] [PMID: 32776704]

[EC 3.13.2.3 created 2018 as EC 3.13.1.8, transferred 2022 to EC 3.13.2.3]