Page last updated: 2024-08-07 12:55:42

Dihydropteridine reductase

A dihydropteridine reductase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P09417]

Synonyms

EC 1.5.1.34;
HDHPR;
Quinoid dihydropteridine reductase;
Short chain dehydrogenase/reductase family 33C member 1

Research

Bioassay Publications (1)

TimeframeStudies on this Protein(%)All Drugs %
pre-19901 (100.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Compounds (4)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridineHomo sapiens (human)IC505,100.000022
4-phenylpyridineHomo sapiens (human)IC502,400.000011
1-methyl-4-(4-chlorophenyl)-1,2,3,6-tetrahydropyridineHomo sapiens (human)IC502,700.000011
4-phenyl-1,2,3,6-tetrahydropyridineHomo sapiens (human)IC5012,000.000011

Enables

This protein enables 4 target(s):

TargetCategoryDefinition
6,7-dihydropteridine reductase activitymolecular functionCatalysis of the reaction: NADP+ + 5,6,7,8-tetrahydropteridine = NADPH + H+ + 6,7-dihydropteridine. [EC:1.5.1.34]
electron transfer activitymolecular functionA molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways. [Wikipedia:Electron_transfer]
NADH bindingmolecular functionBinding to the reduced form, NADH, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. [GOC:mah]
NADPH bindingmolecular functionBinding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. [GOC:mah]

Located In

This protein is located in 3 target(s):

TargetCategoryDefinition
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
extracellular exosomecellular componentA vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894]

Active In

This protein is active in 1 target(s):

TargetCategoryDefinition
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]

Involved In

This protein is involved in 4 target(s):

TargetCategoryDefinition
amino acid metabolic processbiological processThe chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups. [ISBN:0198506732]
dihydrobiopterin metabolic processbiological processThe chemical reactions and pathways involving a dihydrobiopterin, a reduced pteridine derivative related to folic acid; it acts as an electron carrier in tyrosine biosynthesis and its quinoid form is produced by oxidation of tetrahydrobiopterin in several biological hydroxylation reactions. [PMID:2557335]
tetrahydrobiopterin biosynthetic processbiological processThe chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine. [ISBN:0198506732]
L-phenylalanine catabolic processbiological processThe chemical reactions and pathways resulting in the breakdown of phenylalanine, 2-amino-3-phenylpropanoic acid. [GOC:go_curators]