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
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1.3.1.2
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5-fluorouracil
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thymidine
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phosphorylase
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uridine
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medicine
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phosphoribosyltransferase
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orotate
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2.4.2.4
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thymidylate
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fluoropyrimidine
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fdurd
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2.7.1.21
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beta-ureidopropionase
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urdpase
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dihydropyrimidinase
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beta-alanine
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drug development
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analysis
- 1.3.1.2
- 5-fluorouracil
- thymidine
- phosphorylase
- uridine
- medicine
-
phosphoribosyltransferase
- orotate
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2.4.2.4
- thymidylate
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fluoropyrimidine
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fdurd
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2.7.1.21
- beta-ureidopropionase
- urdpase
- dihydropyrimidinase
- beta-alanine
- drug development
- analysis
Reaction
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
Advanced search results
Engineering
Engineering on EC 1.3.1.2 - dihydropyrimidine dehydrogenase (NADP+)
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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
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natural mutation, marked decrease in enzyme affinity to NADPH, reduction of Vmax for 5-fluorouracil degrading activity
R235Q
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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
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natural mutation identified in healthy Japanese volunteer, rapid loss of enzyme activity
A551T
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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
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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
S670A
site-directed mutagenesis, active site loop residue, the mutant shows reduced activity compared to the wild-type enzyme
additional information
C671A
mutation eliminates the proton-coupled electron transfer required to reduce pyrimidine substrates
mutation of the pyrimidine site candidate general acid, slows the turnover of the enzyme by approximately 60fold for uracil and 1600fold for thymine
C671S
variant exhibits both delineation of reductive activation into two phases at low pH values and exceptionally slow turnover with thymine
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PCR and sequence analysis of point mutations occurring in patients, modified cofactor binding and electron transport with exchanges: S201R, P86L, S492L, D949V, H978R, reduced activity in mutants
additional information
natural mutant IVS11+1G to T leads to a cryptic splice site within exon 11 that results in loss of amino acid residues 400-446 in enzyme primary sequence