EzCatDB: S00219

DB codeS00219
CATH domainDomain 13.20.20.70Catalytic domain
E.C.1.6.99.1
CSA1oya
MACiEM0319

CATH domainRelated DB codes (homologues)
3.20.20.70S00215,S00217,S00218,S00532,S00198,S00220,S00745,S00537,S00538,S00539,S00826,S00841,S00235,S00239,S00240,S00243,S00244,S00199,S00200,S00201,S00221,S00222,S00847,S00224,S00225,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,D00863,T00089

Enzyme Name
Swiss-protKEGG

Q02899
Protein nameNADPH dehydrogenase 1NADPH dehydrogenase
NADPH2 diaphorase
NADPH diaphorase
OYE
diaphorase
dihydronicotinamide adenine dinucleotide phosphate dehydrogenase
NADPH-dehydrogenase
NADPH-diaphorase
NADPH2-dehydrogenase
old yellow enzyme
reduced nicotinamide adenine dinucleotide phosphate dehydrogenase
TPNH dehydrogenase
TPNH-diaphorase
triphosphopyridine diaphorase
triphosphopyridine nucleotide diaphorase
NADPH2 dehydrogenase
NADPH:(acceptor) oxidoreductase
SynonymsEC 1.6.99.1
Old yellow enzyme 1


Swiss-prot:Accession NumberQ02899
Entry nameOYE1_SACPS
ActivityNADPH + acceptor = NADP(+) + reduced acceptor.
SubunitHomodimer or heterodimer.
Subcellular location
CofactorFMN.


CofactorsSubstratesProducts
KEGG-idC00061C00005C02395C00007C00080C00006C00414C00027
CompoundFMNNADPHCyclohex-2-enoneO2H+NADP+CyclohexanoneH2O2
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotidecarbohydrateothersothersamide group,amine group,nucleotidecarbohydrateothers
1bwkABound:FMNUnboundUnboundUnbound
UnboundUnboundUnbound
1bwlABound:FMNUnboundUnboundUnbound
UnboundUnboundUnbound
1k02ABound:FMNUnboundUnboundUnbound
UnboundUnboundUnbound
1k03ABound:FMNUnboundAnalogue:HBAUnbound
UnboundUnboundUnbound
1oyaABound:FMNUnboundUnboundUnbound
UnboundUnboundUnbound
1oybABound:FMNUnboundAnalogue:HBAUnbound
UnboundUnboundUnbound
1oycABound:FMNUnboundUnboundUnbound
UnboundUnboundUnbound

Active-site residues
resource
PDB;1bwk, 1bwl & literature;[3], [5], [6]
pdbCatalytic residuescomment
1bwkA       ;ASN 194;TYR 196
mutant H191N
1bwlA       ;       ;TYR 196
mutant H191N;N194N
1k02AHIS 191;ASN 194;TYR 196
mutant Q114N
1k03AHIS 191;ASN 194;TYR 196
mutant Q114N
1oyaAHIS 191;ASN 194;TYR 196

1oybAHIS 191;ASN 194;TYR 196

1oycAHIS 191;ASN 194;TYR 196


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Scheme I6
[4]p.1523-15251
[5]

[6]Fig.1, Fig.7, p.32768-327705
[7]Fig.2
[8]p.3561
[9]Scheme 11, Scheme 12, p.294-295
[10]Scheme 1, Scheme 3, p.10738
[11]Fig.1, Fig.4
[12]Scheme 1
[14]Fig.5, p.21443
[17]p.1609-1612

references
[1]
PubMed ID3091069
JournalBiochemistry
Year1986
Volume25
Pages4077-84
AuthorsPeterson DM, Fisher J
TitleAutocatalytic quinone methide formation from mitomycin c.
[2]
PubMed ID8230231
JournalJ Mol Biol
Year1993
Volume234
Pages502-7
AuthorsFox KM, Karplus PA
TitleCrystallization of Old Yellow Enzyme illustrates an effective strategy for increasing protein crystal size.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID95187711
PubMed ID7881908
JournalStructure
Year1994
Volume2
Pages1089-105
AuthorsFox KM, Karplus PA
TitleOld yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins.
Related PDB1oya,1oyb,1oyc
Related Swiss-protQ02899
[4]
PubMed ID8529830
JournalFASEB J
Year1995
Volume9
Pages1518-26
AuthorsKarplus PA, Fox KM, Massey V
TitleFlavoprotein structure and mechanism. 8. Structure-function relations for old yellow enzyme.
[5]
CommentsX-ray crystallography
PubMed ID9830019
JournalJ Biol Chem
Year1998
Volume273
Pages32753-62
AuthorsBrown BJ, Deng Z, Karplus PA, Massey V
TitleOn the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194.
Related PDB1bwk,1bwl
[6]
PubMed ID9830020
JournalJ Biol Chem
Year1998
Volume273
Pages32763-70
AuthorsKohli RM, Massey V
TitleThe oxidative half-reaction of Old Yellow Enzyme. The role of tyrosine 196.
[7]
PubMed ID10092614
JournalJ Biol Chem
Year1999
Volume274
Pages9357-62
AuthorsFox KM, Karplus PA
TitleThe flavin environment in old yellow enzyme. An evaluation of insights from spectroscopic and artificial flavin studies.
[8]
PubMed ID10097075
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages3556-61
AuthorsXu D, Kohli RM, Massey V
TitleThe role of threonine 37 in flavin reactivity of the old yellow enzyme.
[9]
PubMed ID10961912
JournalBiochem Soc Trans
Year2000
Volume28
Pages283-96
AuthorsMassey V
TitleThe chemical and biological versatility of riboflavin.
[10]
PubMed ID10995477
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages10733-8
AuthorsMeah Y, Massey V
TitleOld yellow enzyme: stepwise reduction of nitro-olefins and catalysis of aci-nitro tautomerization.
[11]
PubMed ID10694883
JournalTrends Biochem Sci
Year2000
Volume25
Pages126-32
AuthorsFraaije MW, Mattevi A
TitleFlavoenzymes: diverse catalysts with recurrent features.
[12]
PubMed ID11438708
JournalProc Natl Acad Sci U S A
Year2001
Volume98
Pages8560-5
AuthorsMeah Y, Brown BJ, Chakraborty S, Massey V
TitleOld yellow enzyme: reduction of nitrate esters, glycerin trinitrate, and propylene 1,2-dinitrate.
[13]
CommentsHomologous enzyme
PubMed ID11377202
JournalStructure (Camb)
Year2001
Volume9
Pages419-29
AuthorsBreithaupt C, Strassner J, Breitinger U, Huber R, Macheroux P, Schaller A, Clausen T
TitleX-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE.
[14]
PubMed ID11668181
JournalJ Biol Chem
Year2002
Volume277
Pages2138-45
AuthorsBrown BJ, Hyun JW, Duvvuri S, Karplus PA, Massey V
TitleThe role of glutamine 114 in old yellow enzyme.
[15]
PubMed ID12186866
JournalJ Biol Chem
Year2002
Volume277
Pages41507-16
AuthorsChakraborty S, Massey V
TitleReaction of reduced flavins and flavoproteins with diphenyliodonium chloride.
[16]
PubMed ID12417633
JournalJ Exp Med
Year2002
Volume196
Pages1241-51
AuthorsKubata BK, Kabututu Z, Nozaki T, Munday CJ, Fukuzumi S, Ohkubo K, Lazarus M, Maruyama T, Martin SK, Duszenko M, Urade Y
TitleA key role for old yellow enzyme in the metabolism of drugs by Trypanosoma cruzi.
[17]
PubMed ID12055282
JournalMicrobiology
Year2002
Volume148
Pages1607-14
AuthorsWilliams RE, Bruce NC
TitleNew uses for an Old Enzyme'--the Old Yellow Enzyme family of flavoenzymes.

comments
This enzyme catalyzes two separate reactions, reductive half-reaction and oxidative half-reaction. In the reductive half-reaction, NADPH is reduced to be NADP+. In the oxidative half-reaction, O2 or alpha,beta-unsaturated ketone/aldehyde is oxidized to be H2O2 or reduced ketone/aldehyde, respectively (see [6]).
Reductive half-reaction:
(A) Hydride transfer from NADPH to FMN, giving NADP+ and FMNH2:
Oxidative half-reaction:
(B) Hydride transfer from FMNH2 to unsaturated ketone/aldehyde, giving FMN and reduced ketone/aldehyde:
or
(C) Hydride transfer from FMNH2 to O2, giving FMN and H2O2:

createdupdated
2004-08-042009-02-26
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)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.