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Literature summary extracted from

  • Rowland, P.; Norager, S.; Jensen, K.F.; Larsen, S.
    Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster (2000), Structure, 8, 1227-1238.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.3.1.14 medicine
-
 Lactococcus lactis
1.3.1.14 medicine enzyme is a part of the pyrimidine biosynthesis pathway and plays a role as target for the chemotherapy of parasitic and neoplastic diseases Faecalicatena orotica
1.3.1.14 nutrition applications in the dairy industry Lactococcus lactis
1.3.1.14 nutrition applications in the dairy industry Enterococcus faecalis
1.3.1.14 pharmacology drug design based upon selective enzyme inhibition Faecalicatena orotica

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.14 hanging-drop vapor diffusion Lactococcus lactis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.14 cytosol
-
 Bacillus subtilis 5829
-
1.3.1.14 cytosol
-
 Lactococcus lactis 5829
-
1.3.1.14 cytosol
-
 Enterococcus faecalis 5829
-
1.3.1.14 cytosol
-
 Faecalicatena orotica 5829
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.14 dihydroorotate + NAD+ Lactococcus lactis fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway orotate + NADH + H+
-
 r
1.3.1.14 dihydroorotate + NAD+ Enterococcus faecalis fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway orotate + NADH + H+
-
 r
1.3.1.14 dihydroorotate + NAD+ Faecalicatena orotica fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway orotate + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.14 Bacillus subtilis
-
-
-
1.3.1.14 Enterococcus faecalis
-
 family IB enzyme, also contains family IA enzyme, milk fermenting bacterium
-
1.3.1.14 Faecalicatena orotica
-
 identical with Clostridium oroticum
-
1.3.1.14 Lactococcus lactis
-
 milk-fermenting bacterium
-
1.3.1.14 Lactococcus lactis
-
 family IB enzyme, also contains family IA enzyme
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.14
-
 Lactococcus lactis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.1.14 (S)-dihydroorotate + NAD+ = orotate + NADH + H+ electron transfer mechanism Lactococcus lactis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.14 (S)-dihydroorotate + NAD+ mechanism of dehydrogenation, mechanism of electron transfer: L-dihydroorotate transfers a pair of electrons to FMN via iron-sulfur cluster via FAD to NAD+ Lactococcus lactis orotate + NADH + H+
-
 r
1.3.1.14 (S)-dihydroorotate + NAD+ NAD+ as ultimate electron acceptor Bacillus subtilis orotate + NADH + H+
-
 ?
1.3.1.14 (S)-dihydroorotate + NAD+ NAD+ as ultimate electron acceptor Lactococcus lactis orotate + NADH + H+
-
 r
1.3.1.14 (S)-dihydroorotate + NAD+ NAD+ as ultimate electron acceptor Enterococcus faecalis orotate + NADH + H+
-
 ?
1.3.1.14 (S)-dihydroorotate + NAD+ NAD+ as ultimate electron acceptor Faecalicatena orotica orotate + NADH + H+
-
 r
1.3.1.14 (S)-dihydroorotate + NAD+ at higher pH values reaction favours direction of dihydroorotate oxidation, whereas at lower pH values direction of orotate reduction is favoured Lactococcus lactis orotate + NADH + H+
-
 r
1.3.1.14 dihydroorotate + NAD+ fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway Lactococcus lactis orotate + NADH + H+
-
 r
1.3.1.14 dihydroorotate + NAD+ fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway Enterococcus faecalis orotate + NADH + H+
-
 r
1.3.1.14 dihydroorotate + NAD+ fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway Faecalicatena orotica orotate + NADH + H+
-
 r
1.3.1.14 additional information
-
 Faecalicatena orotica ?
-
 ?
1.3.1.14 additional information NAD+ binding domain in the beta subunit of enzyme, Cys-135 plays a catalytic role and Lys-48 is important for orienting the substrate in the active site and is able to interact with FMN Lactococcus lactis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.14 heterotetramer
-
 Faecalicatena orotica
1.3.1.14 heterotetramer alpha subunit is named PyrDB, beta subunit is named PyrK Bacillus subtilis
1.3.1.14 heterotetramer alpha subunit is named PyrDB, beta subunit is named PyrK Lactococcus lactis
1.3.1.14 heterotetramer alpha2,beta2, alpha subunit with 331 amino acid residues, beta subunit with 262 amino acid residues, two closely interacting PyrDB-PyrK dimers Lactococcus lactis

Synonyms

EC Number Synonyms Comment Organism
1.3.1.14 More family IB dihydroorotate dehydrogenase Lactococcus lactis
1.3.1.14 More family IB dihydroorotate dehydrogenase Faecalicatena orotica

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.14 4Fe-4S-center
-
 Bacillus subtilis
1.3.1.14 4Fe-4S-center
-
 Enterococcus faecalis
1.3.1.14 4Fe-4S-center
-
 Faecalicatena orotica
1.3.1.14 4Fe-4S-center two [2Fe-2S] clusters as cofactors, tightly bound to the beta subunit and located in the interface of the two dimers centered between the FMN and FAD group, Cys-226, Cys-231, Cys-234 and Cys-249 binds the iron-sulfur cluster Lactococcus lactis
1.3.1.14 FAD
-
 Bacillus subtilis
1.3.1.14 FAD
-
 Enterococcus faecalis
1.3.1.14 FAD
-
 Faecalicatena orotica
1.3.1.14 FAD two tightly bound FAD per heterotetrameric enzyme, FAD is necessary for ability to use NAD+ as electron acceptor, detailed way of binding Lactococcus lactis
1.3.1.14 FAD FAD is located on the beta subunit Lactococcus lactis
1.3.1.14 FMN
-
 Bacillus subtilis
1.3.1.14 FMN
-
 Enterococcus faecalis
1.3.1.14 FMN
-
 Faecalicatena orotica
1.3.1.14 FMN two tightly bound FMN per heterotetrameric enzyme, detailed way of binding Lactococcus lactis
1.3.1.14 FMN FMN is located on the alpha subunit Lactococcus lactis