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Information on EC 1.5.1.33 - pteridine reductase and Organism(s) no activity in Chaetomium globosum and UniProt Accession Q01782

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EC Tree
     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.33 pteridine reductase
IUBMB Comments
The enzyme from Leishmania (both amastigote and promastigote forms) catalyses the reduction by NADPH of folate and a wide variety of unconjugated pterins, including biopterin, to their tetrahydro forms. It also catalyses the reduction of 7,8-dihydropterins and 7,8-dihydrofolate to their tetrahydro forms. In contrast to EC 1.5.1.3 (dihydrofolate reductase) and EC 1.5.1.34 (6,7-dihydropteridine reductase), pteridine reductase will not catalyse the reduction of the quinonoid form of dihydrobiopterin. The enzyme is specific for NADPH; no activity has been detected with NADH. It also differs from EC 1.5.1.3 (dihydrofolate reductase) in being specific for the Si-face of NADPH.
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no activity in Chaetomium globosum
UNIPROT: Q01782
Word Map
The enzyme appears in selected viruses and cellular organisms
Synonyms
EC 1.1.1.253, H region methotrexate resistance protein, LdPTR1, LmPTR1, NADPH-dependent short-chain dehydrogenase/reductase pteridine reductase, NADPH-dihydropteridine reductase, pteridine reductase, pteridine reductase 1, PTR1, reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide phosphate), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H region methotrexate resistance protein
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NADPH-dihydropteridine reductase
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pteridine reductase 1
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PTR1
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reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide phosphate)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
5,6,7,8-tetrahydrobiopterin:NADP+ oxidoreductase
The enzyme from Leishmania (both amastigote and promastigote forms) catalyses the reduction by NADPH of folate and a wide variety of unconjugated pterins, including biopterin, to their tetrahydro forms. It also catalyses the reduction of 7,8-dihydropterins and 7,8-dihydrofolate to their tetrahydro forms. In contrast to EC 1.5.1.3 (dihydrofolate reductase) and EC 1.5.1.34 (6,7-dihydropteridine reductase), pteridine reductase will not catalyse the reduction of the quinonoid form of dihydrobiopterin. The enzyme is specific for NADPH; no activity has been detected with NADH. It also differs from EC 1.5.1.3 (dihydrofolate reductase) in being specific for the Si-face of NADPH.
CAS REGISTRY NUMBER
COMMENTARY hide
131384-61-7
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