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Article

A novel cofactor-binding mode in bacterial IMP dehydrogenases explains inhibitor selectivity.

The Journal of biological chemistry - 27 Feb 2015

Makowska-Grzyska Magdalena, Kim Youngchang, Maltseva Natalia, Osipiuk Jerzy, Gu Minyi, Zhang Minjia, Mandapati Kavitha, Gollapalli Deviprasad R, Gorla Suresh Kumar, Hedstrom Lizbeth, Joachimiak Andrzej

Abstract excerpt

The steadily rising frequency of emerging diseases and antibiotic resistance creates an urgent need for new drugs and targets. Inosine 5'-monophosphate dehydrogenase (IMP dehydrogenase or IMPDH) is a promising target for the development of new antimicrobial agents. IMPDH catalyzes the oxidation of IMP to XMP with the concomitant reduction of NAD(+), which is the pivotal step in the biosynthesis of guanine...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 25572472
DOI: 10.1074/jbc.M114.619767
PMCID: PMC4342496

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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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