Literature summary for 1.3.98.1 extracted from

Norager, S.; Jensen, K.F.; Bjornberg, O.; Larsen, S.
E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases (2002), Structure, 10, 1211-1223.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with product orotate	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	deletions of N-terminal residues from 2 down to 40 result in generally unstable proteins with apo protein quickly precipitating and FMN remaining in solution. A truncated protein lacking residues 2 to 30 is sufficiently stable, has near to wild-type activity using molecular oxygen and 20fold lower activity using 2,6-dichlorophenolindophenol as electron acceptor	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Subunits

Subunits	Comment	Organism
monomer	crystallization data	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
FMN	-	Escherichia coli

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Release 2023.1 (January 2023)