EC number:3.3.1.2

Enzyme

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     3. Hydrolases
        3.3 Acting on ether bonds
            3.3.1 Thioether and trialkylsulfonium hydrolases
ID:3.3.1.2
Description:S-adenosyl-L-methionine hydrolase (L-homoserine-forming).
Alternative Name: S-adenosylmethionine hydrolase.
S-adenosylmethionine cleaving enzyme.
S-adenosyl-L-methionine hydrolase (L-homoserine-forming).
S-adenosyl-L-methionine hydrolase.
Methylmethionine-sulfonium-salt hydrolase.
Adenosylmethionine hydrolase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.3.1.2
BRENDA Enzyme Link: BRENDA 3.3.1.2
KEGG Enzyme Link: KEGG3.3.1.2
BioCyc Enzyme Link: BioCyc 3.3.1.2
ExPASy Enzyme Link: ExPASy3.3.1.2
EC2PDB Enzyme Link: EC2PDB 3.3.1.2
ExplorEnz Enzyme Link: ExplorEnz 3.3.1.2
PRIAM enzyme-specific profiles Link: PRIAM 3.3.1.2
IntEnz Enzyme Link: IntEnz 3.3.1.2
MEDLINE Enzyme Link: MEDLINE 3.3.1.2

EC number:3.3.1.2

MSA:

3.3.1.2;
Phylogenetic Tree:

3.3.1.2;
Uniprot:
M-CSA:
RHEA:14645 H2O + S-adenosyl-L-methionine = H(+) + L-homoserine + S-methyl-5'-thioadenosine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH2;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[CH2;+0:4]-[OH;+0:6].[*:1]-[S;H0;+0:2]-[*:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Decomposition of methyl methionine sulfonium salts by a bacterial enzyme.Mazelis M, Levin B, Mallinson N1965 Jul 295849106