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1.3.1.2: dihydropyrimidine dehydrogenase (NADP+)

This is an abbreviated version!
For detailed information about dihydropyrimidine dehydrogenase (NADP+), go to the full flat file.

Word Map on EC 1.3.1.2

Reaction

5,6-dihydrouracil
+
NADP+
=
Uracil
+
NADPH
+
H+

Synonyms

4,5-dihydrothymine: oxidoreductase, dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide phosphate), DHPDH, DHPDHase, DHU dehydrogenase, dihydropyrimidine dehydrogenase, dihydrothymine dehydrogenase, Dihydrouracil dehydrogenase, dihydrouracil dehydrogenase (NADP), dihydrouracil dehydrogenase (NADP+), DPD, DPYD, hydropyrimidine dehydrogenase

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.2 dihydropyrimidine dehydrogenase (NADP+)

Engineering

Engineering on EC 1.3.1.2 - dihydropyrimidine dehydrogenase (NADP+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A551T
natural mutation identified in a patient with complete loss of enzymic activity
E244V
natural mutation identified in a patient with complete loss of enzymic activity
G366A
-
natural mutation, marked decrease in enzyme affinity to NADPH, reduction of Vmax for 5-fluorouracil degrading activity
R235Q
-
the mutation is expected to weaken the binding of the FAD ring system and to change the electronic environment and hence, the redox potential of the cofactor
T768K
-
natural mutation identified in healthy Japanese volunteer, rapid loss of enzyme activity
A551T
-
natural mutation identified in a human with complete loss of enzymic activity. Crystallization data of Sus scrofa recombinant mutant, mutation might prevent binding of the prosthetic group FMN and affect folding of the enzyme protein
C126A
site-directed mutagenesis, a potential [4Fe-4S]-cluster binding residue, the mutant shows slightly increased activity compared to the wild-type enzyme
C671A
C671S
E244V
-
natural mutation identified in a human with complete loss of enzymic activity. Crystallization data of Sus scrofa recombinant mutant, mutation interferes with the electron flow between NADPH and the pyrimidine binding site of the enzyme
H673N
site-directed mutagenesis, active site loop residue, the mutant shows reduced activity compared to the wild-type enzyme
H673Q
site-directed mutagenesis, active site loop residue, the mutant shows reduced activity compared to the wild-type enzyme
Q156E
site-directed mutagenesis, [4Fe-4S]-cluster binding residue, inactive mutant
R235A
site-directed mutagenesis, FAD binding residue, inactive mutant
R235K
site-directed mutagenesis, FAD binding residue, inactive mutant
S670A
site-directed mutagenesis, active site loop residue, the mutant shows reduced activity compared to the wild-type enzyme
additional information