Enzyme

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EC Tree
     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.5
Description:Betaine--homocysteine S-methyltransferase.
Cath: 3.20.20.330;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.5
BRENDA Enzyme Link: BRENDA 2.1.1.5
KEGG Enzyme Link: KEGG2.1.1.5
BioCyc Enzyme Link: BioCyc 2.1.1.5
ExPASy Enzyme Link: ExPASy2.1.1.5
EC2PDB Enzyme Link: EC2PDB 2.1.1.5
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.5
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.5
IntEnz Enzyme Link: IntEnz 2.1.1.5
MEDLINE Enzyme Link: MEDLINE 2.1.1.5
MSA:

2.1.1.5;

Phylogenetic Tree:

2.1.1.5;

Uniprot:
M-CSA:
RHEA:22336 betaine + L-homocysteine = L-methionine + N,N-dimethylglycine
RULE(radius=1) [*:1]-[N+;H0:2](-[*:3])(-[*:4])-[CH3;+0:5].[*:6]-[SH;+0:7]>>[*:1]-[N;H0;+0:2](-[*:3])-[*:4].[*:6]-[S;H0;+0:7]-[CH3;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis.Castro C, Gratson AA, Evans JC, Jiracek J, Collinsová M, Ludwig ML, Garrow TA2004 May 1115122900
Betaine-homocysteine methyltransferase: zinc in a distorted barrel.Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML2002 Sep12220488