KEGG   ENZYME: 1.10.99.2Help
Entry
EC 1.10.99.2                Enzyme                                 

Name
ribosyldihydronicotinamide dehydrogenase (quinone);
NRH:quinone oxidoreductase 2;
NQO2;
NQO2;
NAD(P)H:quinone oxidoreductase-2 (misleading);
QR2;
quinone reductase 2;
N-ribosyldihydronicotinamide dehydrogenase (quinone);
NAD(P)H:quinone oxidoreductase2 (misleading)
Class
Oxidoreductases;
Acting on diphenols and related substances as donors;
With other, unknown, acceptors
BRITE hierarchy
Sysname
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide:quinone oxidoreductase
Reaction(IUBMB)
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone [RN:R07361]
Reaction(KEGG)
Substrate
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide [CPD:C15497];
quinone [CPD:C15602]
Product
1-(beta-D-ribofuranosyl)nicotinamide [CPD:C03150];
hydroquinone [CPD:C15603]
Comment
A flavoprotein. Unlike EC 1.6.5.2, NAD(P)H dehydrogenase (quinone), this quinone reductase cannot use NADH or NADPH; instead it uses N-ribosyl- and N-alkyldihydronicotinamides. Polycyclic aromatic hydrocarbons, such as benz[a]anthracene, and the oestrogens 17beta-estradiol and diethylstilbestrol are potent inhibitors, but dicoumarol is only a very weak inhibitor [2]. This enzyme can catalyse both 2-electron and 4-electron reductions, but one-electron acceptors, such as potassium ferricyanide, cannot be reduced [3].
History
EC 1.10.99.2 created 2005
Orthology
K08071  
ribosyldihydronicotinamide dehydrogenase (quinone)
Genes
HSA: 
4835(NQO2)
PTR: 
462395(NQO2)
PPS: 
100992910(NQO2)
GGO: 
101132190(NQO2)
PON: 
100174417(NQO2)
MCC: 
MCF: 
102119230(NQO2)
MMU: 
18105(Nqo2)
RNO: 
291084(Nqo2)
CGE: 
100760827(Nqo2)
HGL: 
101696975(Nqo2)
TUP: 
102501485(NQO2)
CFA: 
606932(NQO2)
AML: 
FCA: 
101085630(NQO2)
PTG: 
102964944(NQO2)
BTA: 
508566(NQO2)
BOM: 
102280064(NQO2)
PHD: 
102339147(NQO2)
CHX: 
102174178(NQO2)
CFR: 
102516140(NQO2)
BACU: 
102998501(NQO2)
LVE: 
103080201(NQO2)
ECB: 
100057868(NQO2)
MYB: 
102244529(NQO2)
MYD: 
102767115(NQO2)
PALE: 
MDO: 
SHR: 
OAA: 
100079677(NQO2)
GGA: 
420886(NQO2)
MGP: 
TGU: 
PHI: 
APLA: 
101801396(NQO2)
FPG: 
101913611(NQO2)
FCH: 
102058647(NQO2)
CLV: 
102093500(NQO2)
ASN: 
102368685(NQO2)
AMJ: 
102572705(NQO2)
ACS: 
PBI: 
103061661(NQO2)
MZE: 
XMA: 
LCM: 
CMK: 
103176305(nqo2)
 » show all
Taxonomy
Reference
1  [PMID:14465018]
  Authors
LIAO S, DULANEY JT, WILLIAMS-ASHMAN HG.
  Title
Purification and properties of a flavoprotein catalyzing the oxidation of reduced ribosyl nicotinamide.
  Journal
J. Biol. Chem. 237 (1962) 2981-7.
  Organism
Bos taurus
Reference
2  [PMID:9050836]
  Authors
Zhao Q, Yang XL, Holtzclaw WD, Talalay P.
  Title
Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase)
  Journal
Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 1669-74.
  Organism
Homo sapiens
  Sequence
[hsa:4835]
Reference
3  [PMID:9367528]
  Authors
Wu K, Knox R, Sun XZ, Joseph P, Jaiswal AK, Zhang D, Deng PS, Chen S.
  Title
Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase.
  Journal
Arch. Biochem. Biophys. 347 (1997) 221-8.
  Organism
Homo sapiens
  Sequence
[hsa:4835]
Reference
4  [PMID:8182056]
  Authors
Jaiswal AK.
  Title
Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression.
  Journal
J. Biol. Chem. 269 (1994) 14502-8.
  Organism
Homo sapiens
  Sequence
[hsa:4835]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
667919-86-0

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