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Article

The human ITPA polymorphic variant P32T is destabilized by the unpacking of the hydrophobic core.

Journal of structural biology - 1 Jun 2013

Simone Peter D, Struble Lucas R, Kellezi Admir, Brown Carrie A, Grabow Corinn E, Khutsishvili Irine, Marky Luis A, Pavlov Youri I, Borgstahl Gloria E O

Abstract excerpt

Inosine triphosphate pyrophosphatase (ITPA), a key enzyme involved in maintaining the purity of cellular nucleoside triphosphate pools, specifically recognizes inosine triphosphate and xanthosine triphosphate (including the deoxyribose forms) and detoxifies them by catalyzing the hydrolysis of a phosphoanhydride bond, releasing pyrophosphate. This prevents their inappropriate use as substrates in enzymatic...

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Source

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Identifiers

PMID: 23528839
DOI: 10.1016/j.jsb.2013.03.007
PMCID: PMC4212276

Genes

ITPA

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The human ITPA polymorphic variant P32T is destabilized by the unpacking of the hydrophobic core.PMID 23528839Read ↗

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