Literature summary extracted from

Williams, N.K.; Manthey, M.K.; Hambley, T.W.; O'Donoghue, S.I.; Keegan, M.; Chapman, B.E.; Christopherson, R.I.
Catalysis by hamster dihydroorotase: zinc binding, site-directed mutagenesis, and interaction with inhibitors (1995), Biochemistry, 34, 11344-11352.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
3.5.2.3	2-oxo-1,2,3,6-tetrahydropyrimidine-4,6-dicarboxylate	-	Cricetinae
3.5.2.3	cis-2-oxohexahydropyrimidine-4,6-dicarboxylate	-	Cricetinae
3.5.2.3	L-6-thiodihydroorotate	-	Cricetinae
3.5.2.3	trans-2-oxohexahydropyrimidine-4,6-dicarboxylate	-	Cricetinae

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
3.5.2.3	0.004	-	L-dihydroorotate	wild type (pure) and E301A	Cricetinae
3.5.2.3	0.007	-	L-dihydroorotate	wild type	Cricetinae
3.5.2.3	0.011	-	L-dihydroorotate	H186A (pure)	Cricetinae
3.5.2.3	0.016	-	L-dihydroorotate	K23R (pure)	Cricetinae
3.5.2.3	0.099	-	L-dihydroorotate	D230E	Cricetinae
3.5.2.3	0.45	-	L-dihydroorotate	K239G (pure)	Cricetinae

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.2.3	Cricetinae	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.5.2.3	from overexpressing Escherichia coli	Cricetinae

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Release 2023.1 (January 2023)