EzCatDB: S00336

DB codeS00336
CATH domainDomain 13.40.50.720Catalytic domain
E.C.1.1.1.252
CSA1ybv

CATH domainRelated DB codes (homologues)
3.40.50.720S00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
Swiss-protKEGG

Q12634
Protein nameTetrahydroxynaphthalene reductasetetrahydroxynaphthalene reductase
SynonymsEC 1.1.1.252
T4HN reductase
THNR


Swiss-prot:Accession NumberQ12634
Entry nameT4HR_MAGGR
ActivityScytalone + NADP(+) = 1,3,6,8- tetrahydroxynaphthalene + NADPH.
SubunitHomotetramer.
Subcellular location
Cofactor


SubstratesProductsintermediates
KEGG-idC04033C00005C00080C00779C00006I00095
Compound1,3,6,8-TetrahydroxynaphthaleneNADPHH+scytaloneNADP3-oxo-1,6,8-trihydroxynaphthalene
Typearomatic ring (only carbon atom)amide group,amine group,nucleotideothersaromatic ring (only carbon atom),carbohydrateamide group,amine group,nucleotide
1ybvAUnboundBound:NDP
UnboundUnboundIntermediate-analogue:BEA
1ybvBUnboundBound:NDP
UnboundUnboundIntermediate-analogue:BEA
1dohAUnboundBound:NDP
UnboundUnboundIntermediate-analogue:NID
1dohBUnboundBound:NDP
UnboundUnboundIntermediate-analogue:NID
1g0nAAnalogue:PHHBound:NDP
UnboundUnboundUnbound
1g0nBUnboundBound:NDP
UnboundUnboundUnbound
1g0oAUnboundBound:NDP
UnboundUnboundIntermediate-analogue:PYQ
1g0oBUnboundBound:NDP
UnboundUnboundIntermediate-analogue:PYQ
1g0oCUnboundBound:NDP
UnboundUnboundIntermediate-analogue:PYQ
1g0oDUnboundBound:NDP
UnboundUnboundIntermediate-analogue:PYQ

Active-site residues
resource
literature [9]
pdbCatalytic residuescomment
1ybvASER 164;TYR 178;LYS 182;TYR 223
mutant P2A,S241V,A242Q,H247R
1ybvBSER 164;TYR 178;LYS 182;TYR 223
mutant P2A,S241V,A242Q,H247R
1dohASER 164;TYR 178;LYS 182;TYR 223

1dohBSER 164;TYR 178;LYS 182;TYR 223

1g0nASER 164;TYR 178;LYS 182;TYR 223

1g0nBSER 164;TYR 178;LYS 182;       
invisible 219-235
1g0oASER 164;TYR 178;LYS 182;TYR 223

1g0oBSER 164;TYR 178;LYS 182;TYR 223

1g0oCSER 164;TYR 178;LYS 182;TYR 223

1g0oDSER 164;TYR 178;LYS 182;TYR 223


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.1167-1168
[3]Fig.3, Fig.6, p.1857-1858
[7]Fig.7, p.8701-8702
[9]Fig.7, p.24-25

references
[1]
PubMed ID8860003
JournalProteins
Year1996
Volume24
Pages525-7
AuthorsAndersson A, Jordan D, Schneider G, Valent B, Lindqvist Y
TitleCrystallization and preliminary x-ray diffraction study of 1 ,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID97094973
PubMed ID8939741
JournalStructure
Year1996
Volume4
Pages1161-70
AuthorsAndersson A, Jordan D, Schneider G, Lindqvist Y
TitleCrystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor.
Related PDB1ybv
Related Swiss-protQ12634
[3]
PubMed ID9048570
JournalBiochemistry
Year1997
Volume36
Pages1852-60
AuthorsThompson JE, Basarab GS, Andersson A, Lindqvist Y, Jordan DB
TitleTrihydroxynaphthalene reductase from Magnaporthe grisea: realization of an active center inhibitor and elucidation of the kinetic mechanism.
[4]
PubMed ID9001392
JournalFEBS Lett
Year1997
Volume400
Pages173-6
AuthorsAndersson A, Jordan D, Schneider G, Lindqvist Y
TitleA flexible lid controls access to the active site in 1,3,8-trihydroxynaphthalene reductase.
[5]
PubMed ID10743955
JournalBioorg Med Chem Lett
Year2000
Volume10
Pages491-4
AuthorsLiao DI, Basarab GS, Gatenby AA, Jordan DB
TitleSelection of a potent inhibitor of trihydroxynaphthalene reductase by sorting disease control data.
[6]
PubMed ID10956664
JournalJ Biol Chem
Year2000
Volume275
Pages34867-72
AuthorsThompson JE, Fahnestock S, Farrall L, Liao DI, Valent B, Jordan DB
TitleThe second naphthol reductase of fungal melanin biosynthesis in Magnaporthe grisea: tetrahydroxynaphthalene reductase.
[7]
PubMed ID11467929
JournalBiochemistry
Year2001
Volume40
Pages8696-704
AuthorsLiao DI, Thompson JE, Fahnestock S, Valent B, Jordan DB
TitleA structural account of substrate and inhibitor specificity differences between two naphthol reductases.
[8]
PubMed ID11552692
JournalJ Mol Graph Model
Year2001
Volume19
Pages434-47, 470-1
AuthorsJordan DB, Basarab GS, Liao DI, Johnson WM, Winzenberg KN, Winkler DA
TitleStructure-based design of inhibitors of the rice blast fungal enzyme trihydroxynaphthalene reductase.
[9]
CommentsX-ray crystallography
PubMed ID11342131
JournalStructure (Camb)
Year2001
Volume9
Pages19-27
AuthorsLiao D, Basarab GS, Gatenby AA, Valent B, Jordan DB
TitleStructures of trihydroxynaphthalene reductase-fungicide complexes: implications for structure-based design and catalysis.
Related PDB1doh,1g0n,1g0o

comments
This enzyme was transferred from E.C. 1.3.1.50 to E.C. 1.1.1.252.
This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, along with Drosophia alcohol dehydrogenase (S00319 in EzCatDB). This enzyme has got a catalytic triad composed of conserved residues, Ser, Tyr, and Lys.
In addition to the catalytic triad, another tyrosine residue (Tyr223) is also involved in the active site in this enzyme.
According to the literature [9], this enzyme catalyzes isomerization followed by NADPH-dependent reduction, although the detailed reaction mechanism has not been elucidated so far. Thus, this enzyme seems to catalyze the following reactions:
(A) Isomerization of 1,3,6,8-Tetrahydroxynaphthalene, to form 3-keto intermediate (I00095):
(B) NADPH-dependent Reduction/Hydride transfer reaction:

createdupdated
2004-04-082011-07-04


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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