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Literature summary extracted from

  • Small, Y.A.; Guallar, V.; Soudackov, A.V.; Hammes-Schiffer, S.
    Hydrogen bonding pathways in human dihydroorotate dehydrogenase (2006), J. Phys. Chem. B, 110, 19704-19710.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.3.5.2 additional information three types of hydrogen bonding pathways, hydrogen bonding of the active base serine to a water molecule, which is hydrogen bonded to the substrate carboxylate group or a threonine residue, the threonine residue is positioned to enable proton transfer to another water molecule leading to the bulk solvent Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.3.5.2 S215C increase of the average donor-acceptor distances for proton and hydride transfer and disruption of the hydrogen bonding pathways observed for the wild-type enzyme, significant decrease in enzyme activity Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.2 Homo sapiens Q02127
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.2 dihydroorotate + acceptor
-
 Homo sapiens orotate + reduced acceptor
-
 ?
1.3.5.2 additional information computational method to investigate potential proton relay pathways in the active site of the enzyme Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.5.2 DHOD
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.2 flavin
-
 Homo sapiens
1.3.5.2 FMN Lys100 and Lys225 enhance the structural stability of the active site by hydrogen bonding to the FMN cofactor Homo sapiens