KEGG   ENZYME: 1.10.5.1
Entry
EC 1.10.5.1                 Enzyme                                 
Name
ribosyldihydronicotinamide dehydrogenase (quinone);
NRH:quinone oxidoreductase 2;
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 a quinone or related compound as acceptor
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 quinol [RN:R07361]
Reaction(KEGG)
R07361
Substrate
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide [CPD:C15497];
quinone [CPD:C15602]
Product
1-(beta-D-ribofuranosyl)nicotinamide [CPD:C03150];
quinol [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 estrogens 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 1.10.5.1 created 2005 as EC 1.10.99.2, transferred 2015 to EC 1.10.5.1
Orthology
K08071  ribosyldihydronicotinamide dehydrogenase (quinone)
Genes
HSA4835(NQO2)
PTR462395(NQO2)
PPS100992910(NQO2)
GGO101132190(NQO2)
PON100174417(NQO2)
NLE100597917(NQO2)
MCC707675(NQO2)
MCF102119230(NQO2)
CSAB103222288(NQO2)
CATY105596425(NQO2)
PANU101010086(NQO2)
TGE112623429(NQO2)
RRO104661230(NQO2)
RBB108514231(NQO2)
TFN117086619(NQO2)
PTEH111548564(NQO2)
CJC100387941(NQO2)
SBQ101047567(NQO2)
CSYR103272006(NQO2)
MMUR105873485(NQO2)
OGA100948509(NQO2)
MMU18105(Nqo2)
MCAL110307948(Nqo2)
MPAH110333764(Nqo2)
RNO291084(Nqo2)
MCOC116082571(Nqo2)
MUN110561377(Nqo2)
CGE100760827(Nqo2)
PLEU114701293(Nqo2)
NGI103741921
HGL101696975(Nqo2)
CPOC100715791(Nqo2)
CCAN109695454(Nqo2)
DORD105985892(Nqo2)
DSP122108437(Nqo2)
OCU100301550(NQO2)
OPI101518423(NQO2)
TUP102501485(NQO2)
CFA606932(NQO2)
VVP112907396(NQO2)
VLG121500053(NQO2)
AML100470883(NQO2)
UMR103664966(NQO2)
UAH113264395(NQO2)
UAR123801499(NQO2)
ELK111156722
LLV125103138
MPUF101684988(NQO2)
EJU114223916(NQO2)
ZCA113927119(NQO2)
MLX118027396(NQO2)
FCA101085630(NQO2)
PYU121020426(NQO2)
PBG122489294(NQO2)
PTG102964944(NQO2)
PPAD109249469(NQO2)
AJU106976161(NQO2)
HHV120241451(NQO2)
BTA508566(NQO2)
BOM102280064(NQO2)
BIU109577276(NQO2)
BBUB102389366(NQO2)
CHX102174178(NQO2)
OAS101122988(NQO2)
ODA120869996(NQO2)
CCAD122429864(NQO2)
SSC100739771(NQO2)
CFR102516140(NQO2)
CBAI105079770(NQO2)
CDK105087260(NQO2)
VPC102527353(NQO2)
BACU102998501(NQO2)
LVE103080201(NQO2)
OOR101275294(NQO2)
DLE111181306(NQO2)
PCAD102986827(NQO2)
PSIU116762852(NQO2)
ECB100057868(NQO2)
EPZ103548130(NQO2)
EAI106847885(NQO2)
MYB102244529(NQO2)
MYD102767115(NQO2)
MMYO118677072(NQO2)
MLF102425403(NQO2)
MNA107542940(NQO2)
PKL118724467(NQO2)
DRO112297552(NQO2) 112313165
AJM119042330
PDIC114496747(NQO2)
PHAS123820765(NQO2)
MMF118626549(NQO2)
RFQ117027727(NQO2)
PALE102885731(NQO2)
PGIG120607713(NQO2)
PVP105296779(NQO2)
RAY107521728(NQO2)
MJV108409763(NQO2)
TOD119251908(NQO2)
LAV100666204(NQO2)
TMU101353523
DNM101416911(NQO2)
MDO100028625(NQO2) 100028661
GAS123231865(NQO2)
SHR100914437 100934580
PCW110201160
OAA100079677(NQO2)
GGA420886(NQO2)
PCOC116226410(NQO2)
MGP100543456(NQO2)
CJO107309575(NQO2)
NMEL110393000(NQO2)
APLA101801396(NQO2)
ACYG106043848(NQO2)
AFUL116486849(NQO2)
TGU100190610(NQO2) 100220924(NQO2)
LSR110478235 110478241
SCAN103817683(NQO2)
PMOA120497252(NQO2)
OTC121340416 121340461
PRUF121354851 121357757(NQO2)
GFR102038242 102038415
FAB101805969 101806163
PHI102112623(NQO2)
PMAJ107199553(NQO2)
CCAE111923829 111923830
CCW104696786 120409664(NQO2)
ETL114062376(NQO2) 114072345 114072735
ZAB102066463(NQO2)
FPG101913611(NQO2)
FCH102058647(NQO2)
CLV102093500(NQO2)
EGZ104122836(NQO2)
NNI104021841(NQO2)
ACUN113476989(NQO2)
TALA104356076(NQO2)
PADL103919012(NQO2)
ACHC115353042(NQO2)
AAM106481991(NQO2)
AROW112968061(NQO2)
NPD112947640(NQO2)
DNE112992014(NQO2)
ASN102368685(NQO2)
AMJ102572705(NQO2)
CPOO109315071(NQO2)
GGN109301057(NQO2)
CMY122461324(NQO2)
CABI116835502(NQO2)
ACS100556008(nqo2)
PVT110077079(NQO2)
SUND121929357(NQO2)
PBI103061661(NQO2)
PMUR107287232(NQO2) 107289998 107300078
PGUT117672431(NQO2)
VKO123020618(NQO2)
GJA107112824(NQO2)
NPR108793407(NQO2)
RTEM120940659(NQO2)
BBUF121001071(NQO2)
BGAR122938929(NQO2)
SASA106586559
LCM102360651
HRJ124279219 124279221 124279222
LAK106178845
ATEN116308879
CPICpin_4986
 » show all
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 237:2981-7 (1962)
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 94:1669-74 (1997)
DOI:10.1073/pnas.94.5.1669
  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 347:221-8 (1997)
DOI:10.1006/abbi.1997.0344
  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 269:14502-8 (1994)
  Sequence
[hsa:4835]
Other DBs
ExplorEnz - The Enzyme Database: 1.10.5.1
IUBMB Enzyme Nomenclature: 1.10.5.1
ExPASy - ENZYME nomenclature database: 1.10.5.1
BRENDA, the Enzyme Database: 1.10.5.1
CAS: 667919-86-0
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