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Literature summary extracted from

  • Rowland, P.; Bjornberg, O.; Nielsen, F.S.; Jensen, K.F.; Larsen, S.
    The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymic function (1998), Protein Sci., 7, 1269-1279.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.98.1
-
 Lactococcus lactis
1.3.98.1 dihydroorotate dehydrogenase A, complexed with orotate Lactococcus lactis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.98.1 (S)-dihydroorotate + acceptor Lactococcus lactis fourth step in synthesis of pyrimidine nucleotides orotate + reduced acceptor
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.98.1 Lactococcus lactis
-
-
-
1.3.98.1 Lactococcus lactis
-
 only enzyme A
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.98.1 (S)-dihydroorotate + fumarate = orotate + succinate the active site contains a water filled cavity buried beneath a highly conserved and flexible loop. Orotate is bound by four conserved asparagine side chains. Implications for differences in substrate binding and in the catalytic mechanism between the different enzyme families are given Lactococcus lactis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.98.1 (S)-dihydroorotate + acceptor fourth step in synthesis of pyrimidine nucleotides Lactococcus lactis orotate + reduced acceptor
-
 ?
1.3.98.1 dihydroorotate + acceptor discussion of substrate binding and catalytic mechanism Lactococcus lactis orotate + reduced acceptor
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.98.1 DHOD
-
 Lactococcus lactis

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.98.1 flavin
-
 Lactococcus lactis