EzCatDB: S00339

DB codeS00339
CATH domainDomain 13.40.50.720Catalytic domain
E.C.1.5.1.34
CSA1dhr

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,S00336,S00334,T00219,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

P09417P11348
Protein nameDihydropteridine reductaseDihydropteridine reductase6,7-dihydropteridine reductase
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
SynonymsEC 1.5.1.34
HDHPR
Quinoid dihydropteridine reductase
EC 1.5.1.34
HDHPR
Quinoid dihydropteridine reductase

KEGG pathways
MAP codePathways
MAP00633Trinitrotoluene degradation
MAP00790Folate biosynthesis

Swiss-prot:Accession NumberP09417P11348
Entry nameDHPR_HUMANDHPR_RAT
ActivityA 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H.A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H.
SubunitHomodimer.Homodimer.
Subcellular location

Cofactor



SubstratesProducts
KEGG-idC00272C00003C00006C00268C00080C00004C00005
Compound5,6,7,8-TetrahydrobiopterinNAD+NADP+6,7-DihydrobiopterinH+NADHNADPH
Typeamide group,amine group,aromatic ring (with nitrogen atoms),carbohydrateamide group,amine group,nucleotideamide group,amine group,nucleotideamide group,amine group,aromatic ring (with nitrogen atoms),carbohydrateothersamide group,amine group,nucleotideamide group,amine group,nucleotide
1dhrAUnboundBound:NADUnboundUnbound
UnboundUnbound
1dirAUnboundBound:NADUnboundUnbound
UnboundUnbound
1dirBUnboundBound:NADUnboundUnbound
UnboundUnbound
1dirCUnboundBound:NADUnboundUnbound
UnboundUnbound
1dirDUnboundBound:NADUnboundUnbound
UnboundUnbound
1hdrAUnboundBound:NADUnboundUnbound
UnboundUnbound

Active-site residues
resource
Swiss-prot;P09417, P11348 & literature [15] & [18]
pdbCatalytic residues
1dhrATYR 146;LYS 150
1dirATYR 146;LYS 150
1dirBTYR 146;LYS 150
1dirCTYR 146;LYS 150
1dirDTYR 146;LYS 150
1hdrATYR 149;LYS 153

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[10]Fig.4, p.120
[15]p.5583-5585
[18]Fig.5

references
[1]
PubMed ID3718470
JournalBiochem J
Year1986
Volume234
Pages335-42
AuthorsArmarego WL, Ohnishi A, Taguchi H
TitleNew pteridine substrates for dihydropteridine reductase and horseradish peroxidase.
[2]
PubMed ID3711040
JournalJ Biochem (Tokyo)
Year1986
Volume99
Pages645-52
AuthorsNakanishi N, Hasegawa H, Akino M, Yamada S
TitleCatalytic properties of NADPH-specific dihydropteridine reductase from bovine liver.
[3]
PubMed ID3949795
JournalJ Biol Chem
Year1986
Volume261
Pages3891-3
AuthorsMatthews DA, Webber S, Whiteley JM
TitlePreliminary x-ray diffraction characterization of crystalline rat liver dihydropteridine reductase.
[4]
PubMed ID3569272
JournalEur J Biochem
Year1987
Volume164
Pages403-9
AuthorsArmarego WL, Ohnishi A
TitleInactivation of dihydropteridine reductase (human brain) by platinum(II) complexes.
[5]
PubMed ID3508913
JournalJ Enzyme Inhib
Year1987
Volume1
Pages223-9
AuthorsShen RS, Abell CW
TitleRat striatal synaptosomes as a model system for studying the inhibition of dihydropteridine reductase activity.
[6]
CommentsMUTAGENESIS.
Medline ID91378400
PubMed ID1898002
JournalArch Biochem Biophys
Year1991
Volume287
Pages234-9
AuthorsMatthews DA, Varughese KI, Skinner M, Xuong NH, Hoch J, Trach K, Schneider M, Bray T, Whiteley JM
TitleRole of aspartate-37 in determining cofactor specificity and binding in rat liver dihydropteridine reductase.
Related Swiss-protP11350
[7]
PubMed ID1639779
JournalJ Biol Chem
Year1992
Volume267
Pages15334-9
AuthorsGrimshaw CE, Matthews DA, Varughese KI, Skinner M, Xuong NH, Bray T, Hoch J, Whiteley JM
TitleCharacterization and nucleotide binding properties of a mutant dihydropteridine reductase containing an aspartate 37-isoleucine replacement.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID92335241
PubMed ID1631094
JournalProc Natl Acad Sci U S A
Year1992
Volume89
Pages6080-4
AuthorsVarughese KI, Skinner MM, Whiteley JM, Matthews DA, Xuong NH
TitleCrystal structure of rat liver dihydropteridine reductase.
Related PDB1dhr
Related Swiss-protP11356
[9]
PubMed ID8304094
JournalAdv Exp Med Biol
Year1993
Volume338
Pages123-6
AuthorsVarughese KI, Su Y, Skinner MM, Xuong NH, Matthews DA, Whiteley JM
TitleTwo crystal structures of rat liver dihydropteridine reductase.
[10]
PubMed ID8304093
JournalAdv Exp Med Biol
Year1993
Volume338
Pages115-21
AuthorsWhiteley JM, Xuong NH, Varughese KI
TitleIs dihydropteridine reductase an anomalous dihydrofolate reductase, a flavin-like enzyme, or a short-chain dehydrogenase?
[11]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID94086485
PubMed ID8262916
JournalJ Biol Chem
Year1993
Volume268
Pages26836-41
AuthorsSu Y, Varughese KI, Xuong NH, Bray TL, Roche DJ, Whiteley JM
TitleThe crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue.
Related PDB1hdr
Related Swiss-protP09417
[12]
PubMed ID8433887
JournalPediatr Res
Year1993
Volume33
Pages125-8
AuthorsPonzone A, Guardamagna O, Dianzani I, Ponzone R, Ferrero GB, Spada M, Cotton RG
TitleCatalytic activity of tetrahydrobiopterin in dihydropteridine reductase deficiency and indications for treatment.
[13]
CommentsX-ray crystallography
JournalActa Crystallogr D Biol Crystallogr
Year1994
Volume50
Pages884-8
AuthorsSu Y, Skinner MM, Xuong NH, Matthews DA, Whiteley JM, Varughese KI
TitleCrystal structure of a monoclinic form of dihydropteridine reductase from rat liver.
Related PDB1dir
[14]
PubMed ID7822105
JournalInt J Pept Protein Res
Year1994
Volume44
Pages278-87
AuthorsVarughese KI, Xuong NH, Whiteley JM
TitleStructural and mechanistic implications of incorporating naturally occurring aberrant mutations of human dihydropteridine reductase into a rat model.
[15]
PubMed ID8202530
JournalProc Natl Acad Sci U S A
Year1994
Volume91
Pages5582-6
AuthorsVarughese KI, Xuong NH, Kiefer PM, Matthews DA, Whiteley JM
TitleStructural and mechanistic characteristics of dihydropteridine reductase: a member of the Tyr-(Xaa)3-Lys-containing family of reductases and dehydrogenases.
[16]
PubMed ID8554609
JournalBiochem Biophys Res Commun
Year1995
Volume217
Pages859-68
AuthorsTsigelny I, Baker ME
TitleStructures stabilizing the dimer interface on human 11 beta-hydroxysteroid dehydrogenase types 1 and 2 and human 15-hydroxyprostaglandin dehydrogenase and their homologs.
[17]
CommentsREVIEW ON VARIANTS.
Medline ID95353277
PubMed ID7627180
JournalHum Mutat
Year1995
Volume5
Pages279-84
AuthorsSmooker PM, Cotton RG
TitleMolecular basis of dihydropteridine reductase deficiency.
Related Swiss-protP09417
[18]
PubMed ID8631945
JournalJ Biol Chem
Year1996
Volume271
Pages3437-44
AuthorsKiefer PM, Varughese KI, Su Y, Xuong NH, Chang CF, Gupta P, Bray T, Whiteley JM
TitleAltered structural and mechanistic properties of mutant dihydropteridine reductases.
[19]
PubMed ID10352712
JournalAdv Exp Med Biol
Year1999
Volume463
Pages403-10
AuthorsChang CF, Bray T, Varughese KI, Whiteley JM
TitleComparative properties of three pteridine reductases.
[20]
CommentsHomologous enzyme
PubMed ID11373620
JournalNat Struct Biol
Year2001
Volume8
Pages521-5
AuthorsGourley DG, Schuttelkopf AW, Leonard GA, Luba J, Hardy LW, Beverley SM, Hunter WN
TitlePteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites.


createdupdated
2003-10-312009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
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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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