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
-
fluoropyrimidine
-
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
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General Information
General Information on EC 1.3.1.2 - dihydropyrimidine dehydrogenase (NADP+)
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metabolism
additional information
the N-terminal half of DPD is a member of a family of FAD-containing NADPH oxidoreductases, which transfer electrons to an acceptor protein or domain through [4Fe-4S] clusters of low to very low potential
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efficacy of the chemotherapeutic drug 5'-fluorouracil is reduced by catabolism to 2'-fluoro-beta-alanine, a three-step reaction in which dihydropyrimidine dehydrogenase catalyzes the ratelimiting step
metabolism
in mammals, the pyrimidines uracil and thymine are metabolised by a three-step reductive degradation pathway. Dihydropyrimidine dehydrogenase catalyses its first and rate-limiting step, reducing uracil and thymine to the corresponding 5,6-dihydropyrimidines in an NADPH-dependent reaction
metabolism
the rate of turnover is not controlled by the protonation state of the general acid, cysteine 671. The initial phase results in the accumulation of charge transfer absorption added to the binding difference spectrum for NADPH. The second phase results in reduction of one of the two flavins. The presumed activated form of the enzyme has the FMN cofactor reduced. Charge transfer arises from the proximity of the NADPH and FAD bases and the ensuing flavin is a result of rapid transfer of electrons to the FMN without accumulation of reduced forms of the FAD or Fe4-S4 centers. The slow rate of turnover of DPD is governed by the movement of a mobile structural feature that carries the C671 residue
metabolism
the reductive activation of DPD results in the reduction of one flavin per dimer consistent with alternating site behavior. During pyrimidine reduction, electron transfer across the flavins and Fe4S4 centers is rapid relative to the other process. The net rate of transmission of electrons from NADPH to the pyrimidine (kcat) must be determined exclusively by the rate of proton transfer from general acid cysteine 671