EC 3.13.1.8 - S-adenosyl-L-methionine hydrolase (adenosine-forming)

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IntEnz Enzyme Nomenclature
EC 3.13.1.8

Names

Accepted name:
S-adenosyl-L-methionine hydrolase (adenosine-forming)
Other name:
SAM hydroxide adenosyltransferase
Systematic name:
S-adenosyl-L-methionine hydrolase (adenosine-forming)

Reaction

Comments:

The enzyme, found in bacteria and archaea, catalyses a nucleophilic attack of water at the C5' carbon of S-adenosyl-L-methionine to generate adenosine and L-methionine. May be involved in regulating SAM levels in the cell. cf. EC 3.3.1.2, S-adenosyl-L-methionine hydrolase (L-homoserine-forming).

The enzyme, found in bacteria and archaea, catalyses a nucleophilic attack of water at the C5' carbon of S-adenosyl-L-methionine to generate adenosine and L-methionine. May be involved in regulating SAM levels in the cell. Cf. EC 3.3.1.2.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Eustaquio, A. S., Harle, J., Noel, J. P., Moore, B. S.
    S-Adenosyl-L-methionine hydrolase (adenosine-forming), a conserved bacterial and archaeal protein related to SAM-dependent halogenases.
    Chembiochem 9: 2215-2219 (2008). [PMID: 18720493]
  2. Deng, H., McMahon, S. A., Eustaquio, A. S., Moore, B. S., Naismith, J. H., O'Hagan, D.
    Mechanistic insights into water activation in SAM hydroxide adenosyltransferase (duf-62).
    Chembiochem 10: 2455-2459 (2009). [PMID: 19739191]

[EC 3.13.1.8 created 2018]