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Literature summary for 1.3.1.14 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
Search for more literature for 1.3.1.14

Application

Application Comment Organism
medicine
-
 Lactococcus lactis
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
nutrition applications in the dairy industry Lactococcus lactis
nutrition applications in the dairy industry Enterococcus faecalis
pharmacology drug design based upon selective enzyme inhibition Faecalicatena orotica

Crystallization (Commentary)

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
 Lactococcus lactis

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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
(S)-dihydroorotate + NAD+ NAD+ as ultimate electron acceptor Bacillus subtilis orotate + NADH + H+
-
 ?
(S)-dihydroorotate + NAD+ NAD+ as ultimate electron acceptor Lactococcus lactis orotate + NADH + H+
-
 r
(S)-dihydroorotate + NAD+ NAD+ as ultimate electron acceptor Enterococcus faecalis orotate + NADH + H+
-
 ?
(S)-dihydroorotate + NAD+ NAD+ as ultimate electron acceptor Faecalicatena orotica orotate + NADH + H+
-
 r
(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
dihydroorotate + NAD+ fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway Lactococcus lactis orotate + NADH + H+
-
 r
dihydroorotate + NAD+ fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway Enterococcus faecalis orotate + NADH + H+
-
 r
dihydroorotate + NAD+ fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway Faecalicatena orotica orotate + NADH + H+
-
 r
additional information
-
 Faecalicatena orotica ?
-
 ?
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

Subunits Comment Organism
heterotetramer
-
 Faecalicatena orotica
heterotetramer alpha subunit is named PyrDB, beta subunit is named PyrK Bacillus subtilis
heterotetramer alpha subunit is named PyrDB, beta subunit is named PyrK Lactococcus lactis
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

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

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center
-
 Bacillus subtilis
4Fe-4S-center
-
 Enterococcus faecalis
4Fe-4S-center
-
 Faecalicatena orotica
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
FAD
-
 Bacillus subtilis
FAD
-
 Enterococcus faecalis
FAD
-
 Faecalicatena orotica
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
FAD FAD is located on the beta subunit Lactococcus lactis
FMN
-
 Bacillus subtilis
FMN
-
 Enterococcus faecalis
FMN
-
 Faecalicatena orotica
FMN two tightly bound FMN per heterotetrameric enzyme, detailed way of binding Lactococcus lactis
FMN FMN is located on the alpha subunit Lactococcus lactis