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Article

Structural basis of substrate recognition in thiopurine s-methyltransferase.

Biochemistry - 10 Jun 2008

Peng Yi, Feng Qiping, Wilk Dennis, Adjei Araba A, Salavaggione Oreste E, Weinshilboum Richard M, Yee Vivien C

Abstract excerpt

Thiopurine S-methyltransferase (TPMT) modulates the cytotoxic effects of thiopurine prodrugs such as 6-mercaptopurine by methylating them in a reaction using S-adenosyl- l-methionine as the donor. Patients with TPMT variant allozymes exhibit diminished levels of protein and/or enzyme activity and are at risk for thiopurine drug-induced toxicity. We have determined two crystal structures of murine TPMT, as a...

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Share to Amino Acid Substitution
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 18484748
DOI: 10.1021/bi800102x
PMCID: PMC2447621

Genes

TPMT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Structural basis of substrate recognition in thiopurine s-methyltransferase.PMID 18484748Read ↗

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Characterisation of novel defective thiopurine S-methyltransferase allelic variants.Semantic proximity Read ↗

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