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Article

Divalent metal ion-based catalytic mechanism of the Nudix hydrolase Orf153 (YmfB) from Escherichia coli.

Acta crystallographica. Section D, Biological crystallography - 1 May 2014

Hong Myoung-Ki, Ribeiro António J M, Kim Jin-Kwang, Ngo Ho-Phuong-Thuy, Kim Jiyoung, Lee Choong Hwan, Ahn Yeh-Jin, Fernandes Pedro Alexandrino, Li Qing, Ramos Maria Joao, Kang Lin-Woo

Abstract excerpt

YmfB from Escherichia coli is the Nudix hydrolase involved in the metabolism of thiamine pyrophosphate, an important compound in primary metabolism and a cofactor of many enzymes. In addition, it hydrolyzes (d)NTPs to (d)NMPs and inorganic orthophosphates in a stepwise manner. The structures of YmfB alone and in complex with three sulfates and two manganese ions determined by X-ray crystallography, when compared...

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PMID: 24816099
DOI: 10.1107/S1399004714002570

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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