Thiopurine S-Methyltransferase (TPMT) Human Recombinant Protein

This gene encodes the enzyme that metabolizes thiopurine drugs via S-adenosyl-L-methionine as the S-methyl donor and S-adenosyl-L-homocysteine as a byproduct. Thiopurine drugs such as 6-mercaptopurine are used as chemotherapeutic agents. Genetic polymorphisms that affect this enzymatic activity are correlated with variations in sensitivity and toxicity to such drugs within individuals, causing thiopurine S-methyltransferase deficiency. Related pseudogenes have been identified on chromosomes 3, 18 and X. [provided by RefSeq, Aug 2014]

TPMT: Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine. Defects in TPMT are the cause of thiopurine S- methyltransferase deficiency (TPMT deficiency). TPMT is an enzyme involved in the normal metabolic inactivation of thiopurine drugs. These drugs are generally used as immunosupressants or cytotoxic drugs and are prescribed for a variety of clinical conditions including leukemia, autoimmune disease and organ transplantation. Patients with intermediate or no TPMT activity are at risk of toxicity after receiving standard doses of thiopurine drugs and it is shown that inter-individual differences in response to these drugs are largely determined by genetic variation at the TPMT locus. Belongs to the methyltransferase superfamily. TPMT family.

Protein type: EC 2.1.1.67; Xenobiotic Metabolism - drug metabolism - other enzymes; Methyltransferase

Chromosomal Location of Human Ortholog: 6p22.3

Cellular Component: cytosol

Molecular Function: thiopurine S-methyltransferase activity

Biological Process: methylation; xenobiotic metabolic process; nucleobase, nucleoside, nucleotide and nucleic acid metabolic process

Disease: Thiopurine S-methyltransferase Deficiency