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Literature summary extracted from

  • Pascal, R.A.; Walsh, C.T.
    Mechanistic studies with deuterated dihydroorotates on the dihydroorotate oxidase from Crithidia fasciculata (1984), Biochemistry, 23, 2745-2752.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.98.1 0.001 0.002 ferricyanide pH 6.0 Crithidia fasciculata
1.3.98.1 0.017
-
 S-dihydroorotate pH 9.0 Crithidia fasciculata

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.98.1 60000
-
-
 Crithidia fasciculata

Organism

EC Number Organism UniProt Comment Textmining
1.3.98.1 Crithidia fasciculata
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.98.1 (S)-dihydroorotate + fumarate = orotate + succinate mechanism, pyrimidine biosynthetic pathways Crithidia fasciculata
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.98.1 (S)-dihydroorotate + O2 different dihydroorotate isotopes tested for mechanistic and stereochemical analysis Crithidia fasciculata orotate + H2O2
-
 ?
1.3.98.1 orotate + ferricyanide
-
 Crithidia fasciculata (S)-dihydroorotate + ferrocyanide
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.98.1 231
-
 S-dihydroorotate pH 7.4 Crithidia fasciculata

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.98.1 7.4
-
-
 Crithidia fasciculata

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.98.1 FMN flavoprotein, enzyme contains 1 FMN as prosthetic group Crithidia fasciculata