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Article

Substrate Binding Mode and Molecular Basis of a Specificity Switch in Oxalate Decarboxylase.

Biochemistry - 12 Apr 2016

Zhu Wen, Easthon Lindsey M, Reinhardt Laurie A, Tu Chingkuang, Cohen Steven E, Silverman David N, Allen Karen N, Richards Nigel G J

Abstract excerpt

Oxalate decarboxylase (OxDC) catalyzes the conversion of oxalate into formate and carbon dioxide in a remarkable reaction that requires manganese and dioxygen. Previous studies have shown that replacing an active-site loop segment Ser(161)-Glu(162)-Asn(163)-Ser(164) in the N-terminal domain of OxDC with the cognate residues Asp(161)-Ala(162)-Ser-(163)-Asn(164) of an evolutionarily related, Mn-dependent oxalate...

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Identifiers

PMID: 27014926
DOI: 10.1021/acs.biochem.6b00043
PMCID: PMC4854488

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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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