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Literature summary for 1.3.98.1 extracted from

  • McDonald, C.A.; Palfey, B.A.
    Substrate binding and reactivity are not linked: grafting a proton-transfer network into a Class 1A dihydroorotate dehydrogenase (2011), Biochemistry, 50, 2714-2716.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
L71F reaction is somehow slower than for wild-type, binding of dihydroorotate is much tighter than with wild-type Lactococcus lactis
L71F/C130S/V133T addition of the two residues comprising the conserved proton-transfer network of Class 2 dihydroorotate dehydrogenase from Escherichia coli to the C130S Class 1A enzyme of Lactococcus lacits. Mutation does not did not restore the function of the active site base or rapid flavin reduction. Kd for dihydroorotate is about three times tighter than the wild-type Lactococcus lactis
L71F/V133T reaction is drastically slower forwith wild-type, Kd for dihydroorotate is iabout eight-fold tighter than the wild-type Lactococcus lactis
V133T reaction is somehow slower than for wild-type, binding of dihydroorotate is much weaker than with wild-type Lactococcus lactis

Organism

Organism UniProt Comment Textmining
Lactococcus lactis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-dihydroorotate + fumarate
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Lactococcus lactis orotate + succinate
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