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Article

Crystal structure of wild-type and mutant human Ap4A hydrolase.

Biochemical and biophysical research communications - 1 Mar 2013

Ge Honghua, Chen Xiaofang, Yang Weili, Niu Liwen, Teng Maikun

Abstract excerpt

Ap4A hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 3.6.1.17), an enzyme involved in a number of biological processes, is characterized as cleaving the polyphosphate chain at the fourth phosphate from the bound adenosine moiety. This paper presents the crystal structure of wild-type and E58A mutant human Ap4A hydrolase. Similar to the canonical Nudix fold, human Ap4A hydrolase shows the common...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 23384440
DOI: 10.1016/j.bbrc.2013.01.095
PMCID: PMC7092880

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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