1.1.1.252: tetrahydroxynaphthalene reductase
This is an abbreviated version!
For detailed information about tetrahydroxynaphthalene reductase, go to the full flat file.
Word Map on EC 1.1.1.252
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1.1.1.252
-
melanin
-
lunata
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curvularia
-
tetralin
-
cochliobolus
-
tricyclazole
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1,8-dihydroxynaphthalene
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lysr-type
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teleomorph
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homology-built
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17beta-hydroxysteroid
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17beta-hsdcl
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drug development
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lagenarium
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flaviolin
-
pentaketide
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agriculture
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medicine
- 1.1.1.252
- melanin
- lunata
- curvularia
- tetralin
- cochliobolus
- tricyclazole
- 1,8-dihydroxynaphthalene
-
lysr-type
-
teleomorph
-
homology-built
-
17beta-hydroxysteroid
- 17beta-hsdcl
- drug development
- lagenarium
- flaviolin
-
pentaketide
- agriculture
- medicine
Reaction
Synonyms
1,3,6,8-tetrahydroxynaphthalene reductase, 1,3,8-trihydroxynaphthalene reductase, 3HNR, 4HN, BdsA, EC 1.3.1.50, hydroxynaphthalene reductase, MGG_02252, NADPH-dependent naphthol reductase, naphthol reductase, reductase, naphthol, reductase, naphthol (Magnaporthe grisea clone pAV501 precursor reduced), T4HN reductase, T4HNR, tetrahydroxynaphthalene reductase (Magnaporthe grisea clone pAV501), THNR, trihydroxynaphthalene reductase
ECTree
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Reference
Reference on EC 1.1.1.252 - tetrahydroxynaphthalene reductase
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Wheeler, M.H.; Greenblatt, G.A.
The inhibition of melanin biosynthetic reactions in Pyricularia oryzae by compounds that prevent rice blast disease
Exp. Mycol.
12
151-160
1988
Pyricularia oryzae
-
Vidal-Cros, A.; Viviani, F.; Labesse, G.; Boccara, M.; Gaudry, M.
Polyhydroxynaphthalene reductase involved in melanin biosynthesis in Magnaporthe grisea. Purification, cDNA cloning and sequencing
Eur. J. Biochem.
219
985-992
1994
Pyricularia grisea
Thompson, J.E.; Basarab, G.S.; Andersson, A.; Lindqvist, Y.; Jordan, D.B.
Trihydroxynaphthalene reductase from Magnaporthe grisea: realization of an active center inhibitor and elucidation of the kinetic mechanism
Biochemistry
36
1852-1860
1997
Pyricularia grisea
Andersson, A.; Jordan, D.; Schneider, G.; Valent, B.; Lindqvist, Y.
Crystallization and preliminary X-ray diffraction study of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea
Proteins Struct. Funct. Genet.
24
525-527
1996
Pyricularia grisea
Perpetua, N.S.; Kubo, Y.; Yasuda, N.; Takano, Y.; Furusawa, I.
Cloning and characterization of a melanin biosynthetic THR1 reductase gene essential for appressorial penetration of Colletotrichum lagenarium
Mol. Plant Microbe Interact.
9
323-329
1996
Colletotrichum lagenaria
Ichinose, K.; Kiyono, J.; Ebizuka, Y.; Sankawa, U.
Post-aromatic deoxygenation in polyketide biosynthesis: reduction of aromatic rings in the biosynthesis of fungal melanin and anthraquinone
Chem. Pharm. Bull.
41
2015-2021
1993
Phialocephala lagerbergii
Viviani, F.; Vors, J.P.; Gaudry, M.; Marquet, A.
Deoxygenation of polyphenols by ascomycetes: kinetic behavior of the NADPH-dependent naphthol dehydrogenase and inhibition by tricyclazole and its analogues
Bull. Soc. Chim. Fr.
130
395-404
1993
Pyricularia oryzae
-
Andersson, A.; Jordan, D.; Schneider, G.; Lindqvist, Y.
Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor
Structure
4
1161-1170
1996
Pyricularia grisea
Thompson, J.E.; Basarab, G.S.; Pierce, J.; Hodge, C.N.; Jordan, D.B.
2,3-Dihydro-2,5-dihydroxy-4H-benzopyran-4-one: a nonphysiological substrate for fungal melanin biosynthetic enzymes
Anal. Biochem.
256
1-6
1998
Pyricularia grisea
Andersson, A.; Jordan, D.; Schneider, G.; Lindqvist, Y.
A flexible lid controls access to the active site in 1,3,8-trihydroxynaphthalene reductase
FEBS Lett.
400
173-176
1997
Pyricularia grisea
Tsuji, G.; Sugahara, T.; Fujii, I.; Mori, Y.; Ebizuka, Y.; Shiraishi, T.; Kubo, Y.
Evidence for involvement of two naphthol reductases in the first reduction step of melanin biosynthesis pathway of Colletotrichum lagenarium
Mycol. Res.
107
854-860
2003
Colletotrichum lagenaria
Brunskole, M.; Stefane, B.; Zorko, K.; Anderluh, M.; Stojan, J.; Lanisnik Rizner, T.; Gobec, S.
Towards the first inhibitors of trihydroxynaphthalene reductase from Curvularia lunata: Synthesis of artificial substrate, homology modelling and initial screening
Bioorg. Med. Chem.
16
5881-5889
2008
Curvularia lunata
Rostkowski, M.; Paneth, P.
Analysis of conformer stability for 1,3,8-trihydroxynaphthalene: natural substrate of fungal trihydroxynaphthalene reductase
J. Phys. Chem. B
111
8314-8320
2007
Fungi
Brunskole, M.; Zorko, K.; Kerbler, V.; Martens, S.; Stojan, J.; Gobec, S.; Lanisnik Rizner, T.
Trihydroxynaphthalene reductase of Curvularia lunata--a target for flavonoid action?
Chem. Biol. Interact.
178
259-267
2009
Curvularia lunata
Stojan, J.; Brunskole, M.; Rizner, T.
Simultaneous binding of coenzyme and two ligand molecules into the active site of fungal trihydroxynaphthalene reductase
Chem. Biol. Interact.
178
268-273
2009
Curvularia lunata
Kristan, K.; Brunskole, M.; Stojan, J.; Rizner, T.L.
Two homologous fungal carbonyl reductases with different substrate specificities
Chem. Biol. Interact.
178
295-302
2009
Curvularia lunata
Zhang, C.; Huang, X.; Wang, J.; Zhou, M.
Resistance development in rice blast disease caused by Magnaporthe grisea to tricyclazole
Pestic. Biochem. Physiol.
94
43-47
2009
Pyricularia grisea (Q9HFV6)
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Schaetzle, M.A.; Flemming, S.; Husain, S.M.; Richter, M.; Guenther, S.; Mueller, M.
Tetrahydroxynaphthalene reductase: catalytic properties of an enzyme involved in reductive asymmetric naphthol dearomatization
Angew. Chem. Int. Ed. Engl.
51
2643-2646
2012
Pyricularia grisea
Chen, H.; Han, X.; Qin, N.; Wei, L.; Yang, Y.; Rao, L.; Chi, B.; Feng, L.; Ren, Y.; Wan, J.
Synthesis and biological evaluation of novel inhibitors against 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea
Bioorg. Med. Chem.
24
1225-1230
2016
Pyricularia oryzae (Q12634), Pyricularia oryzae ATCC MYA-4617 (Q12634)
Conradt, D.; Schätzle, M.; Husain, S.; Müller, M.
Diversity in reduction with short-chain dehydrogenases: tetrahydroxynaphthalene reductase, trihydroxynaphthalene reductase, and glucose dehydrogenase
ChemCatChem
7
3116-3120
2015
Pyricularia oryzae
-
Thornton, C.R.; Ryder, L.S.; Le Cocq, K.; Soanes, D.M.
Identifying the emerging human pathogen Scedosporium prolificans by using a species-specific monoclonal antibody that binds to the melanin biosynthetic enzyme tetrahydroxynaphthalene reductase
Environ. Microbiol.
17
1023-1038
2015
Lomentospora prolificans
Sone, Y.; Nakamura, S.; Sasaki, M.; Hasebe, F.; Kim, S.; Funa, N.
Bacterial enzymes catalyzing the synthesis of 1,8-dihydroxynaphthalene, a key precursor of dihydroxynaphthalene melanin, from Sorangium cellulosum
Appl. Environ. Microbiol.
84
e00258
2018
Sorangium cellulosum
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