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EC 1.5.1.33 Details

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EC number

1.5.1.33

Accepted name

pteridine reductase

Reaction

5,6,7,8-tetrahydrobiopterin + 2 NADP⁺ = biopterin + 2 NADPH + 2 H⁺

Other name(s)

PTR1, pteridine reductase 1

Systematic name

5,6,7,8-tetrahydrobiopterin:NADP⁺ oxidoreductase

CAS registry number

131384-61-7

Comment

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.

History

created 1999 as EC 1.1.1.253, transferred 2003 to EC 1.5.1.33

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.3.1 With NAD⁺ or NADP⁺ as acceptor

1.3.2 With a cytochrome as acceptor

1.3.3 With oxygen as acceptor

1.3.4 With a disulfide as acceptor

1.3.5 With a quinone or related compound as acceptor

1.3.7 With an iron-sulfur protein as acceptor

1.3.8 With a flavin as acceptor

1.3.98 With other, known, physiological acceptors

1.3.99 With unknown physiological acceptors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.5.1 With NAD⁺ or NADP⁺ as acceptor

1.5.1.1 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H]

1.5.1.2 pyrroline-5-carboxylate reductase

1.5.1.3 dihydrofolate reductase

1.5.1.4 created 1961, deleted 1976

1.5.1.5 methylenetetrahydrofolate dehydrogenase (NADP⁺)

1.5.1.6 formyltetrahydrofolate dehydrogenase

1.5.1.7 saccharopine dehydrogenase (NAD⁺, L-lysine-forming)

1.5.1.8 saccharopine dehydrogenase (NADP⁺, L-lysine-forming)

1.5.1.9 saccharopine dehydrogenase (NAD⁺, L-glutamate-forming)

1.5.1.10 saccharopine dehydrogenase (NADP⁺, L-glutamate-forming)

1.5.1.11 D-octopine dehydrogenase

1.5.1.12 1-pyrroline-5-carboxylate dehydrogenase

1.5.1.13 created 1972, deleted 2004

1.5.1.14 created 1976, deleted 1989

1.5.1.15 methylenetetrahydrofolate dehydrogenase (NAD⁺)

1.5.1.16 D-lysopine dehydrogenase

1.5.1.17 alanopine dehydrogenase

1.5.1.18 ephedrine dehydrogenase

1.5.1.19 D-nopaline dehydrogenase

1.5.1.20 methylenetetrahydrofolate reductase [NAD(P)H]

1.5.1.21 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)

1.5.1.22 strombine dehydrogenase

1.5.1.23 tauropine dehydrogenase

1.5.1.24 N⁵-(carboxyethyl)ornithine synthase

1.5.1.25 thiomorpholine-carboxylate dehydrogenase

1.5.1.26 β-alanopine dehydrogenase

1.5.1.27 1,2-dehydroreticulinium reductase (NADPH)

1.5.1.28 opine dehydrogenase

1.5.1.29 FMN reductase [NAD(P)H]

1.5.1.30 flavin reductase (NADPH)

1.5.1.31 berberine reductase

1.5.1.32 vomilenine reductase

1.5.1.33 pteridine reductase

1.5.1.34 6,7-dihydropteridine reductase

1.5.1.35 1-pyrroline dehydrogenase

1.5.1.36 flavin reductase (NADH)

1.5.1.37 FAD reductase (NADH)

1.5.1.38 FMN reductase (NADPH)

1.5.1.39 FMN reductase [NAD(P)H]

1.5.1.40 8-hydroxy-5-deazaflavin:NADPH oxidoreductase

1.5.1.41 riboflavin reductase [NAD(P)H]

1.5.1.42 FMN reductase (NADH)

1.5.1.43 carboxynorspermidine synthase

1.5.1.44 festuclavine dehydrogenase

1.5.1.45 FAD reductase [NAD(P)H]

1.5.1.46 agroclavine dehydrogenase

1.5.1.47 dihydromethanopterin reductase [NAD(P)⁺]

1.5.1.48 2-methyl-1-pyrroline reductase

1.5.1.49 1-pyrroline-2-carboxylate reductase [NAD(P)H]

1.5.1.50 dihydromonapterin reductase

1.5.1.51 N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase

1.5.1.52 staphylopine dehydrogenase

1.5.1.53 methylenetetrahydrofolate reductase (NADPH)

1.5.1.54 methylenetetrahydrofolate reductase (NADH)

1.5.3 With oxygen as acceptor

1.5.4 With a disulfide as acceptor

1.5.5 With a quinone or similar compound as acceptor

1.5.7 With an iron-sulfur protein as acceptor

1.5.8 With a flavin or flavoprotein as acceptor

1.5.98 With other, known, physiological acceptors

1.5.99 With unknown physiological acceptors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.10.1 With NAD⁺ or NADP⁺ as acceptor

1.10.2 With a cytochrome as acceptor

1.10.3 With oxygen as acceptor

1.10.5 With a quinone or related compound as acceptor

1.10.9 With a copper protein as acceptor

1.10.99 With unknown physiological acceptors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.15.1 Acting on superoxide as acceptor (only sub-subclass identified to date)

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

3.1 Acting on ester bonds

3.2 Glycosylases

3.3 Acting on ether bonds

3.4 Acting on peptide bonds (peptidases)

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.6 Acting on acid anhydrides

3.7 Acting on carbon-carbon bonds

3.8 Acting on halide bonds

3.9 Acting on phosphorus-nitrogen bonds

3.10 Acting on sulfur-nitrogen bonds

3.11 Acting on carbon-phosphorus bonds

3.12 Acting on sulfur-sulfur bonds

3.13 Acting on carbon-sulfur bonds

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Release 2023.1 (January 2023)