| EC |
2.1.1.67 |
| Accepted name: |
thiopurine S-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether |
| Other name(s): |
mercaptopurine methyltransferase; thiopurine methyltransferase; 6-thiopurine transmethylase; TPMT |
| Systematic name: |
S-adenosyl-L-methionine:thiopurine S-methyltransferase |
| Comments: |
Also acts, more slowly, on thiopyrimidines and aromatic thiols. Not identical with EC 2.1.1.9 thiol S-methyltransferase. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 67339-09-7 |
| References: |
| 1. |
Remy, C.N. Metabolism of thiopyrimidines and thiopurines. S-Methylation with S-adenosylmethionine transmethylase and catabolism in mammalian tissues. J. Biol. Chem. 238 (1963) 1078–1084. [PMID: 13981612] |
| 2. |
Woodson, L.C., Ames, M.M., Selassie, C.D, Hansch, C. and Weinshilbaum, R.M. Thiopurine methyltransferase. Aromatic thiol substrates and inhibition by benzoic acid derivatives. Mol. Pharmacol. 24 (1983) 471–478. [PMID: 6633508] |
| 3. |
Woodson, L.C. and Weinshilbaum, R.M. Human kidney thiopurine methyltransferase. Purification and biochemical properties. Biochem. Pharmacol. 32 (1983) 819–826. [DOI] [PMID: 6838629] |
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| [EC 2.1.1.67 created 1984] |
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