EC number:2.1.1.67

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.67
Description:Thiopurine S-methyltransferase.
Cath: 3.40.50.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.67
BRENDA Enzyme Link: BRENDA 2.1.1.67
KEGG Enzyme Link: KEGG2.1.1.67
BioCyc Enzyme Link: BioCyc 2.1.1.67
ExPASy Enzyme Link: ExPASy2.1.1.67
EC2PDB Enzyme Link: EC2PDB 2.1.1.67
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.67
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.67
IntEnz Enzyme Link: IntEnz 2.1.1.67
MEDLINE Enzyme Link: MEDLINE 2.1.1.67

EC number:2.1.1.67

MSA:

2.1.1.67;
Phylogenetic Tree:

2.1.1.67;
Uniprot:
M-CSA:
RHEA:56580 6-thioguanine + S-adenosyl-L-methionine = 6-methylthioguanine + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[nH;+0:6]:[c;H0;+0:7](:[*:8])=[S;H0;+0:9]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[n;H0;+0:6]:[c;H0;+0:7](:[*:8])-[S;H0;+0:9]-[CH3;+0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Human erythrocyte thiopurine methyltransferase: radiochemical microassay and biochemical properties.Weinshilboum RM, Raymond FA, Pazmiño PA1978 May 2657528
RHEA:12609 mercaptopurine + S-adenosyl-L-methionine = 6-methylthiopurine + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[nH;+0:6]:[c;H0;+0:7](=[S;H0;+0:8]):[*:9]1:[*:10]:[n;H0;+0:11]:[*:12]:[nH;+0:13]:1>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[n;H0;+0:6]:[c;H0;+0:7](-[S;H0;+0:8]-[CH3;+0:4]):[*:9]1:[*:10]:[nH;+0:11]:[*:12]:[n;H0;+0:13]:1
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Human erythrocyte thiopurine methyltransferase: radiochemical microassay and biochemical properties.Weinshilboum RM, Raymond FA, Pazmiño PA1978 May 2657528
Structural basis of substrate recognition in thiopurine s-methyltransferase.Peng Y, Feng Q, Wilk D, Adjei AA, Salavaggione OE, Weinshilboum RM, Yee VC2008 Jun 1018484748