The Enzyme Database

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EC 1.5.1.3     
Accepted name: dihydrofolate reductase
Reaction: 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+
For diagram of folate-coenzyme interconversions, click here
Other name(s): tetrahydrofolate dehydrogenase; DHFR; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; folic acid reductase; folic reductase; dihydrofolic acid reductase; dihydrofolic reductase; 7,8-dihydrofolate reductase; NADPH-dihydrofolate reductase
Systematic name: 5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase
Comments: The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9002-03-3
References:
1.  Blakley, R.L. and MacDougall, B.M. Dihydrofolic reductase from Streptococcus faecalis R. J. Biol. Chem. 236 (1961) 1163.
2.  Bolin, J.T., Filman, D.J., Matthews, D.A. and Kraut, J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J. Biol. Chem. 257 (1982) 13650–13662. [PMID: 6815178]
3.  Kaufman, B.T. and Gardiner, R.C. Studies on dihydrofolic reductase. I. Purification and properties of dihydrofolic reductase from chicken liver. J. Biol. Chem. 241 (1966) 1319–1328. [PMID: 4379915]
4.  Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401–411. [DOI] [PMID: 4306838]
[EC 1.5.1.3 created 1961, modified 1976 (EC 1.5.1.4 created 1961, incorporated 1976)]
 
 
EC 1.5.1.30     
Accepted name: flavin reductase (NADPH)
Reaction: reduced riboflavin + NADP+ = riboflavin + NADPH + H+
For diagram of riboflavin biosynthesis (late stages), click here
Other name(s): NADPH:flavin oxidoreductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase; flavin mononucleotide reductase; flavine mononucleotide reductase; FMN reductase (NADPH); NADPH-dependent FMN reductase; NADPH-flavin reductase; NADPH-FMN reductase; NADPH-specific FMN reductase; riboflavin mononucleotide reductase; riboflavine mononucleotide reductase; NADPH2 dehydrogenase (flavin); NADPH2:riboflavin oxidoreductase
Systematic name: reduced-riboflavin:NADP+ oxidoreductase
Comments: The enzyme reduces riboflavin, and, less efficiently, FMN and FAD. NADH is oxidized less efficiently than NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56626-29-0
References:
1.  Yubisui, T., Tamura, M. and Takeshita, M. Characterization of a second form of NADPH-flavin reductase purified from human erythrocytes. Biochem. Int. 15 (1987) 1–8. [PMID: 3453680]
2.  Cunningham, O., Gore, M.G. and Mantle, T.J. Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXβ reductase (BVR-B). Biochem. J. 345 (2000) 393–399. [PMID: 10620517]
[EC 1.5.1.30 created 1982 as EC 1.6.8.2, transferred 2002 to EC 1.5.1.30, modified 2011]
 
 
EC 1.5.1.31     
Accepted name: berberine reductase
Reaction: (R)-canadine + 2 NADP+ = berberine + 2 NADPH + H+
For diagram of canadine biosynthesis, click here
Other name(s): (R)-canadine synthase
Systematic name: (R)-tetrahydroberberine:NADP+ oxidoreductase
Comments: Involved in alkaloid biosynthesis in Corydalis cava to give (R)-canadine with the opposite configuration to the precursor of berberine (see EC 1.3.3.8 tetrahydroberberine oxidase). Also acts on 7,8-dihydroberberine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bauer, W. and Zenk, M.H. Formation of (R)-configurated tetrahydroprotoberberine alkaloids in vivo and in vitro. Tetrahedron Lett. 32 (1991) 487–490.
[EC 1.5.1.31 created 2002]
 
 
EC 1.5.1.32     
Accepted name: vomilenine reductase
Reaction: 1,2-dihydrovomilenine + NADP+ = vomilenine + NADPH + H+
For diagram of ajmaline, vinorine, vomilenine and raucaffricine biosynthesis, click here
Systematic name: 1,2-dihydrovomilenine:NADP+ oxidoreductase
Comments: Forms part of the ajmaline biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 462127-03-3
References:
1.  von Schumann, G., Gao, S. and Stöckigt, J. Vomilenine reductase - a novel enzyme catalyzing a crucial step in the biosynthesis of the therapeutically applied antiarrhythmic alkaloid ajmaline. J. Bioorg. Med. Chem. 10 (2002) 1913–1918. [DOI] [PMID: 11937349]
[EC 1.5.1.32 created 2002]
 
 
EC 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
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 131384-61-7
References:
1.  Nare, B., Hardy, L. and Beverley, S.M. The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major. J. Biol. Chem. 272 (1997) 13883–13891. [DOI] [PMID: 9153248]
2.  Gourley, D.G., Schüttelkopf, A.W., Leonard, G.A., Luba, J., Hardy, L.W., Beverley, S.M. and Hunter, W.N. Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites. Nat. Struct. Biol. 8 (2001) 521–525. [DOI] [PMID: 11373620]
3.  Fitzpatrick, P.F. The aromatic amino acid hydroxylases. Adv. Enzymol. Relat. Areas Mol. Biol. 74 (2000) 235–294. [PMID: 10800597]
[EC 1.5.1.33 created 1999 as EC 1.1.1.253, transferred 2003 to EC 1.5.1.33]
 
 
EC 1.5.1.34     
Accepted name: 6,7-dihydropteridine reductase
Reaction: a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H + H+
For diagram of biopterin biosynthesis, click here
Other name(s): 6,7-dihydropteridine:NAD(P)H oxidoreductase; DHPR; NAD(P)H:6,7-dihydropteridine oxidoreductase; NADH-dihydropteridine reductase; NADPH-dihydropteridine reductase; NADPH-specific dihydropteridine reductase; dihydropteridine (reduced nicotinamide adenine dinucleotide) reductase; dihydropteridine reductase; dihydropteridine reductase (NADH); 5,6,7,8-tetrahydropteridine:NAD(P)H+ oxidoreductase
Systematic name: 5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase
Comments: The substrate is the quinonoid form of dihydropteridine. Not identical with EC 1.5.1.3 dihydrofolate reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9074-11-7
References:
1.  Harano, T. New diaphorases from Bombyx silkworm eggs. NADH/NADPH cytochrome c reductase activity mediated with 6,7-dimethyltetrahydropterin. Insect Biochem. 2 (1972) 385–399.
2.  Hasegawa, H. Dihydropteridine reductase from bovine liver. Purification, crystallization, and isolation of a binary complex with NADH. J. Biochem. (Tokyo) 81 (1977) 169–177. [PMID: 191436]
3.  Kaufman, S. Phenylalanine hydroxylase. Methods Enzymol. 5 (1962) 809–816.
4.  Lind, K.E. Dihydropteridine reductase. Investigation of the specificity for quinoid dihydropteridine and the inhibition by 2,4-diaminopteridines. Eur. J. Biochem. 25 (1972) 560–562. [DOI] [PMID: 4402916]
5.  Nakanishi, N., Hasegawa, H. and Watabe, S. A new enzyme, NADPH-dihydropteridine reductase in bovine liver. J. Biochem. (Tokyo) 81 (1977) 681–685. [PMID: 16875]
[EC 1.5.1.34 created 1972 as EC 1.6.99.7, modified 1981 (EC 1.6.99.10 created 1978, incorporated 1981), transferred 2003 to EC 1.5.1.34]
 
 
EC 1.5.1.35      
Deleted entry: 1-pyrroline dehydrogenase. The enzyme is identical to EC 1.2.1.19, aminobutyraldehyde dehydrogenase, as the substrates 1-pyrroline and 4-aminobutanal are interconvertible
[EC 1.5.1.35 created 2006, deleted 2007]
 
 
EC 1.5.1.36     
Accepted name: flavin reductase (NADH)
Reaction: reduced flavin + NAD+ = flavin + NADH + H+
Other name(s): NADH-dependent flavin reductase; flavin:NADH oxidoreductase
Systematic name: flavin:NAD+ oxidoreductase
Comments: The enzyme from Escherichia coli W catalyses the reduction of free flavins by NADH. The enzyme has similar affinity to FAD, FMN and riboflavin. Activity with NADPH is more than 2 orders of magnitude lower than activity with NADH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Galan, B., Diaz, E., Prieto, M.A. and Garcia, J.L. Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new Flavin:NAD(P)H reductase subfamily. J. Bacteriol. 182 (2000) 627–636. [DOI] [PMID: 10633095]
[EC 1.5.1.36 created 2011]
 
 
EC 1.5.1.37     
Accepted name: FAD reductase (NADH)
Reaction: FADH2 + NAD+ = FAD + NADH + H+
For diagram of FAD biosynthesis, click here
Other name(s): NADH-FAD reductase; NADH-dependent FAD reductase; NADH:FAD oxidoreductase; NADH:flavin adenine dinucleotide oxidoreductase
Systematic name: FADH2:NAD+ oxidoreductase
Comments: The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gisi, M.R. and Xun, L. Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia AC1100. J. Bacteriol. 185 (2003) 2786–2792. [DOI] [PMID: 12700257]
[EC 1.5.1.37 created 2011]
 
 
EC 1.5.1.38     
Accepted name: FMN reductase (NADPH)
Reaction: FMNH2 + NADP+ = FMN + NADPH + H+
For diagram of FAD biosynthesis, click here
Other name(s): FRP; flavin reductase P; SsuE
Systematic name: FMNH2:NADP+ oxidoreductase
Comments: The enzymes from bioluminescent bacteria contain FMN [4], while the enzyme from Escherichia coli does not [8]. The enzyme often forms a two-component system with monooxygenases such as luciferase. Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor [1,2]. While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity [3,6,8].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gerlo, E. and Charlier, J. Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi. Eur. J. Biochem. 57 (1975) 461–467. [DOI] [PMID: 1175652]
2.  Jablonski, E. and DeLuca, M. Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi. Biochemistry 16 (1977) 2932–2936. [PMID: 880288]
3.  Jablonski, E. and DeLuca, M. Studies of the control of luminescence in Beneckea harveyi: properties of the NADH and NADPH:FMN oxidoreductases. Biochemistry 17 (1978) 672–678. [PMID: 23827]
4.  Lei, B., Liu, M., Huang, S. and Tu, S.C. Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme. J. Bacteriol. 176 (1994) 3552–3558. [DOI] [PMID: 8206832]
5.  Tanner, J.J., Lei, B., Tu, S.C. and Krause, K.L. Flavin reductase P: structure of a dimeric enzyme that reduces flavin. Biochemistry 35 (1996) 13531–13539. [DOI] [PMID: 8885832]
6.  Liu, M., Lei, B., Ding, Q., Lee, J.C. and Tu, S.C. Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium. Arch. Biochem. Biophys. 337 (1997) 89–95. [DOI] [PMID: 8990272]
7.  Lei, B. and Tu, S.C. Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase. Biochemistry 37 (1998) 14623–14629. [DOI] [PMID: 9772191]
8.  Eichhorn, E., van der Ploeg, J.R. and Leisinger, T. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 274 (1999) 26639–26646. [DOI] [PMID: 10480865]
[EC 1.5.1.38 created 2011]
 
 
EC 1.5.1.39     
Accepted name: FMN reductase [NAD(P)H]
Reaction: FMNH2 + NAD(P)+ = FMN + NAD(P)H + H+
For diagram of FAD biosynthesis, click here
Other name(s): FRG
Systematic name: FMNH2:NAD(P)+ oxidoreductase
Comments: Contains FMN. The enzyme can utilize NADH and NADPH with similar reaction rates. Different from EC 1.5.1.42, FMN reductase (NADH) and EC 1.5.1.38, FMN reductase (NADPH). The luminescent bacterium Vibrio harveyi possesses all three enzymes [1]. Also reduces riboflavin and FAD, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Watanabe, H. and Hastings, J.W. Specificities and properties of three reduced pyridine nucleotide-flavin mononucleotide reductases coupling to bacterial luciferase. Mol. Cell. Biochem. 44 (1982) 181–187. [PMID: 6981058]
[EC 1.5.1.39 created 2011]
 
 


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