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Literature summary for 1.3.5.2 extracted from

  • Fagan, R.L.; Palfey, B.A.
    Roles in binding and chemistry for conserved active site residues in the class 2 dihydroorotate dehydrogenase from Escherichia coli (2009), Biochemistry, 48, 7169-7178.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
N111A large decrease in reduction rate constant Escherichia coli
N111D large decrease in reduction rate constant. Reduction potential is about 100 mV lower than in wild-type Escherichia coli
N172A large decrease in reduction rate constant. Reduction potential is about 25 mV lower than in wild-type Escherichia coli
N172A/N246A large decrease in reduction rate constant. The maximum flavin absorbance is at 453 nm, blue-shifted 3 nm compared to wild type Escherichia coli
N177A large decrease in reduction rate constant. Reduction potential is about 25 mV lower than in wild-type Escherichia coli
N246A large decrease in reduction rate constant Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A7E1
-
-

Reaction

Reaction Comment Organism Reaction ID
(S)-dihydroorotate + a quinone = orotate + a quinol enzyme uses a stepwise mechanism for dihydroorotate oxidation Escherichia coli
a

Cofactor

Cofactor Comment Organism Structure
FMN
-
 Escherichia coli