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Article

Dihydrooxonate is a substrate of dihydroorotate dehydrogenase (DHOD) providing evidence for involvement of cysteine and serine residues in base catalysis.

Archives of biochemistry and biophysics - 15 Jul 2001

Björnberg O, Jordan D B, Palfey B A, Jensen K F

Abstract excerpt

The flavoprotein dihydroorotate dehydrogenase (DHOD) catalyzes the oxidation of dihydroorotate to orotate. Dihydrooxonate is an analogue of dihydroorotate in which the C5 carbon is substituted by a nitrogen atom. We have investigated dihydrooxonate as a substrate of three DHODs, each representing a distinct evolutionary class of the enzyme, namely the two family 1 enzymes from Lactococcus lactis, DHODA and DHODB,...

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PMID: 11437361
DOI: 10.1006/abbi.2001.2409

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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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