KEGG   ENZYME: 1.6.2.4Help
Entry
EC 1.6.2.4                  Enzyme                                 

Name
NADPH---hemoprotein reductase;
CPR;
FAD-cytochrome c reductase;
NADP---cytochrome c reductase;
NADP---cytochrome reductase;
NADPH-dependent cytochrome c reductase;
NADPH:P-450 reductase;
NADPH:ferrihemoprotein oxidoreductase;
NADPH---cytochrome P-450 oxidoreductase;
NADPH---cytochrome c oxidoreductase;
NADPH---cytochrome c reductase;
NADPH---cytochrome p-450 reductase;
NADPH---ferricytochrome c oxidoreductase;
NADPH---ferrihemoprotein reductase;
TPNH2 cytochrome c reductase;
TPNH-cytochrome c reductase;
aldehyde reductase (NADPH-dependent);
cytochrome P-450 reductase;
cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent);
dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase;
ferrihemoprotein P-450 reductase;
reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase;
reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate)
Class
Oxidoreductases;
Acting on NADH or NADPH;
With a heme protein as acceptor
BRITE hierarchy
Sysname
NADPH:hemoprotein oxidoreductase
Reaction(IUBMB)
NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
Reaction(KEGG)
Substrate
NADPH [CPD:C00005];
H+ [CPD:C00080];
oxidized hemoprotein
Product
NADP+ [CPD:C00006];
reduced hemoprotein
Comment
A flavoprotein (FMN, FAD) containing both FMN and FAD. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction. The enzyme catalyses the reduction of the heme-thiolate-dependent monooxygenases, such as EC 1.14.14.1, unspecific monooxygenase and reduction of EC 1.14.99.3, heme oxygenase (decyclizing). It is part of the microsomal hydroxylating system. It also reduces cytochrome b5 and cytochrome c.
History
EC 1.6.2.4 created 1972, modified 2003
Orthology
K00327  
NADPH-ferrihemoprotein reductase
K14338  
cytochrome P450 / NADPH-cytochrome P450 reductase
Genes
HSA: 
5447(POR)
PTR: 
463481(POR)
PPS: 
GGO: 
PON: 
NLE: 
MCC: 
715888(POR)
MCF: 
CJC: 
MMU: 
18984(Por)
RNO: 
29441(Por)
CGE: 
NGI: 
HGL: 
OCU: 
TUP: 
CFA: 
489816(POR)
AML: 
UMR: 
FCA: 
PTG: 
BTA: 
532512(POR)
BOM: 
PHD: 
CHX: 
OAS: 
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
MYB: 
MYD: 
PALE: 
MDO: 
SHR: 
GGA: 
417520(POR)
MGP: 
APLA: 
TGU: 
FAB: 
PHI: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XLA: 
379707(por)
XTR: 
DRE: 
568202(por)
TRU: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
724870(GB19444)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CBR: 
CBG03543(Cbr-emb-8)
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
AT4G24520(ATR1) AT4G30210(ATR2)
ALY: 
CRB: 
EUS: 
BRP: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
CSV: 
CMO: 
RCU: 
POP: 
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os04t0653400-01(Os04g0653400) Os08t0243500-01(Os08g0243500) Os09t0558900-01(Os09g0558900)
OBR: 
BDI: 
SBI: 
SORBI_02g032640(SORBIDRAFT_02g032640) SORBI_06g031110(SORBIDRAFT_06g031110) SORBI_07g007640(SORBIDRAFT_07g007640)
ZMA: 
SITA: 
PDA: 
MUS: 
ATR: 
s00019p00222550(AMTR_s00019p00222550)
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
OTA: 
BPG: 
MIS: 
MPP: 
CSL: 
CVR: 
SCE: 
YHR042W(NCP1)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0A01270(NCAS0A01270) NCAS_0F02460(NCAS0F02460)
NDI: 
NDAI_0C02110(NDAI0C02110) NDAI_0C03940(NDAI0C03940)
TPF: 
TPHA_0E02140(TPHA0E02140)
TBL: 
TBLA_0A10290(TBLA0A10290) TBLA_0C03210(TBLA0C03210)
TDL: 
TDEL_0E03350(TDEL0E03350)
KAF: 
KAFR_0E01430(KAFR0E01430) KAFR_0J00410(KAFR0J00410)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_1532054(AO090011000910) AOR_1_772164(AO090001000445) AOR_1_894144(AO090023000520)
ANG: 
ANI_1_1104074(An08g07840) ANI_1_2654014(An01g06820) ANI_1_384044(An05g00510) ANI_1_396144(An16g02820)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
TMS: 
PPL: 
DSQ: 
PCO: 
SHS: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT113910(AGABI1DRAFT_113910)
ABV: 
AGABI2DRAFT193746(AGABI2DRAFT_193746)
CPUT: 
SLA: 
UMA: 
PFP: 
MGL: 
PGR: 
MLR: 
WSE: 
MBR: 
DDI: 
DPP: 
DFA: 
DFA_11137(redB)
ACAN: 
PFA: 
PFD: 
PFH: 
PYO: 
PCB: 
PBE: 
PKN: 
PVX: 
PCY: 
TAN: 
TPV: 
BBO: 
BBOV_I002330(19.m02062)
BEQ: 
CPV: 
CHO: 
TGO: 
TET: 
PTM: 
PTI: 
TPS: 
PIF: 
EHX: 
GTT: 
TBR: 
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
GLA: 
PCT: 
RPI: 
RPF: 
REH: 
CNC: 
RME: 
BUR: 
BCED: 
VAP: 
VPE: 
VPD: 
HOH: 
BJA: 
BJU: 
BRS: 
RPB: 
RPD: 
AZC: 
ELI: 
BSU: 
BSU07250(yetO) BSU27160(cypB)
BSR: 
BSL: 
BSH: 
BSY: 
BSUT: 
BSUL: 
BSS: 
BST: 
BSO: 
BSN: 
BSQ: 
BSX: 
C663_0751(cypD) C663_2550(cypE)
BSP: 
BLI: 
BL02398(cypE)
BLD: 
BLi02848(yrhJ)
BLH: 
BAO: 
BAMF_0695(yetO) BAMF_2522(cypB)
BAY: 
BAQ: 
BYA: 
BAMP: 
BAML: 
BAMA: 
RBAU_0722(cypD) RBAU_2563(cypB)
BAMN: 
BASU_0699(cypD) BASU_2369(cypB)
BAMB: 
BAMT: 
BAZ: 
BQL: 
LL3_00745(yetO) LL3_02800(yrhJ)
BXH: 
BQY: 
MUS_0726(yetO) MUS_2901(yrhJ)
BAMI: 
BAMC: 
BAMF: 
BAMY: 
BAE: 
BAN: 
BA_3221(cypD)
BAR: 
GBAA_3221(cypD)
BAT: 
BAH: 
BAI: 
BAA_3269(cypD)
BAX: 
BANT: 
BANR: 
BANS: 
BANH: 
BAL: 
BCE: 
BCA: 
BCE_3239(cypD)
BCZ: 
BCR: 
BCB: 
BCU: 
BCG: 
BCQ: 
BCQ_3034(cypD)
BCX: 
BCA_3251(cypD)
BNC: 
BCF: 
BCER: 
BCEF: 
BTK: 
BTL: 
BTB: 
BTT: 
BTHR: 
BTC: 
BTF: 
BTM: 
BTG: 
BTI: 
BTN: 
BTHT: 
BTHU: 
BWE: 
BTY: 
BMYC: 
DJ92_5480(cyp102A1)
BPU: 
BPUM_1680(yrhJ)
BPUM: 
BMQ: 
BMD: 
BMH: 
BJS: 
BMP: 
HHD: 
GYM: 
PPM: 
PPO: 
PPM_3514(M1_3883)
PPOL: 
PPQ: 
PMS: 
PMW: 
MRH: 
MNE: 
CUV: 
RPY: 
SMA: 
SAV_575(cyp2)
SCB: 
SCT: 
SCAT_4838(CYP102A)
SCY: 
SHY: 
SHO: 
SDV: 
SALU: 
SRO: 
NML: 
SEN: 
SACE_4205(cypD)
PDX: 
KAL: 
SACI: 
SGN: 
HAU: 
DGO: 
 » show all
Taxonomy
Reference
1
  Authors
Haas, E., Horecker, B.L. and Hogness, T.R.
  Title
The enzymatic reduction of cytochrome c, cytochrome c reductase.
  Journal
J. Biol. Chem. 136 (1940) 747-774.
Reference
2
  Authors
Horecker, B.L.
  Title
Triphosphopyridine nucleotide-cytochrome c reductase in liver.
  Journal
J. Biol. Chem. 183 (1950) 593-605.
Reference
3  [PMID:4389465]
  Authors
Lu AY, Junk KW, Coon MJ.
  Title
Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components.
  Journal
J. Biol. Chem. 244 (1969) 3714-21.
Reference
4  [PMID:14275154]
  Authors
GIBSON QH, PALMER G, WHARTON DC.
  Title
STUDIES ON THE MECHANISM OF MICROSOMAL TRIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME C REDUCTASE.
  Journal
J. Biol. Chem. 240 (1965) 921-31.
Reference
5  [PMID:14007123]
  Authors
WILLIAMS CH Jr, KAMIN H.
  Title
Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver.
  Journal
J. Biol. Chem. 237 (1962) 587-95.
Reference
6  [PMID:4378860]
  Authors
Masters BS, Bilimoria MH, Kamin H, Gibson QH.
  Title
The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase.
  Journal
J. Biol. Chem. 240 (1965) 4081-8.
Reference
7  [PMID:8589067]
  Authors
Sevrioukova IF, Peterson JA.
  Title
NADPH-P-450 reductase: structural and functional comparisons of the eukaryotic and prokaryotic isoforms.
  Journal
Biochimie. 77 (1995) 562-72.
Reference
8  [PMID:9237990]
  Authors
Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ.
  Title
Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 8411-6.
  Sequence
[rno:29441]
Reference
9  [PMID:11329262]
  Authors
Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK.
  Title
Determination of the redox properties of human NADPH-cytochrome P450 reductase.
  Journal
Biochemistry. 40 (2001) 1956-63.
Reference
10 [PMID:12773143]
  Authors
Gutierrez A, Grunau A, Paine M, Munro AW, Wolf CR, Roberts GC, Scrutton NS.
  Title
Electron transfer in human cytochrome P450 reductase.
  Journal
Biochem. Soc. Trans. 31 (2003) 497-501.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9023-03-4

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