Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.5.2 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

Application Comment Organism
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

Protein Variants Comment Organism
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

Organism UniProt Comment Textmining
Homo sapiens Q02127
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DHOD
-
Homo sapiens

Cofactor

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