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 containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases (e.g. EC 1.14.14.1, unspecific monooxygenase) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. It also reduces cytochrome b5 and cytochrome c. 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.
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: 100990437(POR)
GGO: 101135912(POR)
PON: 100452085
NLE: 100587002(POR)
MCC: 715888(POR)
MCF: 102134028(POR)
CSAB: 103246654(POR)
RRO: 104681218(POR)
RBB: 108518920
CJC: 100406157(POR)
SBQ: 101035291(POR)
MMU: 18984(Por)
RNO: 29441(Por)
CGE: 100689241(Por) 107976996
NGI: 103733467(Por)
HGL: 101712555(Por)
CCAN: 109688432
OCU: 100301554(POR)
TUP: 102496445(POR)
CFA: 489816(POR)
AML: 100465011(POR)
UMR: 103670214(POR)
ORO: 101366006(POR)
FCA: 101085768
PTG: 102971734(POR)
AJU: 106980719(POR)
BTA: 532512(POR)
BOM: 102283470(POR)
BIU: 109578465
PHD: 102315534(POR)
CHX: 102181832(POR)
OAS: 101115252(POR)
SSC: 100170114(POR)
CFR: 102510441(POR)
CDK: 105089654(POR)
BACU: 103007702(POR)
LVE: 103083277(POR)
OOR: 101286608(POR)
ECB: 100059789(POR)
EPZ: 103560971(POR)
EAI: 106839273(POR)
MYB: 102246496(POR)
MYD: 102764298(POR)
HAI: 109385000
PALE: 102894416(POR)
LAV: 100658233
TMU: 101344901
MDO: 100619047(POR)
SHR: 100933747
GGA: 417520(POR)
MGP: 100548057(POR)
CJO: 107322571(POR)
APLA: 101804794(POR)
ACYG: 106041462(POR)
TGU: 100219500(POR)
GFR: 102036096(POR)
FAB: 101806381(POR)
PHI: 102107845(POR)
PMAJ: 107212723
CCW: 104691103
FPG: 101922201(POR)
FCH: 102057066(POR)
CLV: 102096906
EGZ: 104131908(POR)
AAM: 106497339(POR)
ASN: 102381176(POR)
AMJ: 102568888(POR)
PSS: 102444175(POR)
CMY: 102945437(POR)
CPIC: 101935324(POR)
ACS: 100565465(por)
PVT: 110085143
PBI: 103048009(POR)
GJA: 107107688(POR)
XLA: 108709620(por.S) 379707(por.L)
XTR: 100486781(por)
NPR: 108791088
DRE: 327556(porb) 568202(pora)
IPU: 108280677
TRU: 101077941(por)
LCO: 104924160(por) 109137665
NCC: 104940867(por)
MZE: 101479837
OLA: 101166486
XMA: 102220266
PRET: 103474460
NFU: 107380478
CSEM: 103378569
LCF: 108894792
HCQ: 109525476
BPEC: 110174320
LCM: 102350315(POR)
CIN: 100175298(por)
SPU: 594665
APLC: 110985397
SKO: 100370731
DME: Dmel_CG11567(Cpr)
DSI: Dsimw501_GD23403(Dsim_GD23403)
MDE: 101890161(CPR)
AAG: 5577930
AME: 724870
BIM: 100747022
BTER: 100652262
AEC: 105145812
ACEP: 105618981
PBAR: 105430980
HST: 105180558
CFO: 105252547
LHU: 105677070
PGC: 109862557
NVI: 100121805(Cpr)
TCA: 659809
DPA: 109539561
NVL: 108558177
BMOR: 100127056(Cpr)
PMAC: 106720355
PRAP: 110992755
ZNE: 110829356
FCD: 110851145
TUT: 107366505
CEL: CELE_K10D2.6(emb-8)
CBR: CBG03543(Cbr-emb-8)
BMY: Bm1_41510
TSP: Tsp_02446
CRG: 105327991
MYI: 110463152
OBI: 106869693
LAK: 106154571
SHX: MS3_08027
EPA: 110252358
HMG: 100208539
ATH: AT4G24520(ATR1) AT4G30210(ATR2)
LJA: Lj0g3v0139899.1(Lj0g3v0139899.1) Lj0g3v0353589.1(Lj0g3v0353589.1) Lj1g3v1548790.1(Lj1g3v1548790.1) Lj4g3v2107210.1(Lj4g3v2107210.1) Lj4g3v2107220.1(Lj4g3v2107220.1) Lj4g3v2107220.2(Lj4g3v2107220.2)
PXB: 103964936
SOT: 102604882
CANN: 107857074 107867353(cpr1) 107877895(cpr2)
DOSA: Os04t0653400-01(Os04g0653400) Os08t0243500-01(Os08g0243500) Os09t0558900-01(Os09g0558900)
ATS: 109755228(LOC109755228) 109772248(LOC109772248)
ATR: 18435533
APRO: F751_4650
SCE: YHR042W(NCP1)
ERC: Ecym_4744
KMX: KLMA_20725(NCP1)
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)
CAL: CAALFM_C403180WA(NCP1)
CDU: CD36_43030(NCP1)
CAUR: QG37_03739
SLB: AWJ20_472(NCP1)
NTE: NEUTE1DRAFT116342(NEUTE1DRAFT_116342) NEUTE1DRAFT145879(NEUTE1DRAFT_145879)
ANG: ANI_1_1104074(An08g07840) ANI_1_2654014(An01g06820) ANI_1_384044(An05g00510) ANI_1_396144(An16g02820) ANI_1_622054(An06g02530)
PBL: PAAG_11783(PAAG_03974)
PBN: PADG_11605(PADG_03462)
SPO: SPBC29A10.01(ccr1)
CNE: CND01320
CNB: CNBD4990
ABP: AGABI1DRAFT113910(AGABI1DRAFT_113910)
ABV: AGABI2DRAFT193746(AGABI2DRAFT_193746)
MGL: MGL_1677
DDI: DDB_G0269912(redB)
DFA: DFA_11137(redB)
PYO: PY17X_0827400(PY05179)
PCB: PCHAS_082440(PC300648.00.0)
TAN: TA04090
TPV: TP03_0092
BBO: BBOV_I002330(19.m02062)
CPV: cgd4_2700
SMIN: v1.2.022851.t1(symbB.v1.2.022851.t1) v1.2.034545.t1(symbB.v1.2.034545.t1) v1.2.041829.t1(symbB.v1.2.041829.t1)
TCR: 506585.70
PCT: PC1_0268
RPI: Rpic_4258
REH: H16_B1009(h16_B1009)
CNC: CNE_2c09660(cypE)
RME: Rmet_3467
BCEO: I35_5939
BCED: DM42_5902
BCON: NL30_31780
BPSL: WS57_03680
HOH: Hoch_2584
SAME: SAMCFNEI73_pB0314(cypD)
BJA: blr2882
BRS: S23_51340
BRAD: BF49_1812
RPB: RPB_3645
RPD: RPD_1820
VGO: GJW-30_1_03917(cypE)
AZC: AZC_3520
ELI: ELI_00100
BSU: BSU07250(yetO) BSU27160(cypB)
BSH: BSU6051_07250(yetO) BSU6051_27160(cypB)
BSUT: BSUB_00799(yetO) BSUB_02898(cypB)
BSUL: BSUA_00799(yetO) BSUA_02898(cypB)
BSS: BSUW23_03690(cypD) BSUW23_13125(cypB)
BSQ: B657_07250(cypD) B657_27160(cypB)
BSX: C663_0751(cypD) C663_2550(cypE)
BLI: BL02398(cypE)
BLD: BLi02848(yrhJ)
BLH: BaLi_c29470(cypB)
BAY: RBAM_007390(yetO) RBAM_024260(yrhJ)
BAQ: BACAU_0708(yetO) BACAU_2438(yrhJ)
BYA: BANAU_0661(yetO) BANAU_2583(yrhJ)
BAML: BAM5036_0659(cypD) BAM5036_2365(cypB)
BAMA: RBAU_0722(cypD) RBAU_2563(cypB)
BAMN: BASU_0699(cypD) BASU_2369(cypB)
BAMB: BAPNAU_0670(YetO) BAPNAU_1137(yrhJ)
BAMY: V529_06850(yetO) V529_27090(yrhJ)
BAO: BAMF_0695(yetO) BAMF_2522(cypB)
BAZ: BAMTA208_03280(yetO) BAMTA208_13325(cypB)
BQL: LL3_00745(yetO) LL3_02800(yrhJ)
BXH: BAXH7_00690(yetO) BAXH7_02724(yrhJ)
BQY: MUS_0726(yetO) MUS_2901(yrhJ)
BAN: BA_3221(cypD)
BAR: GBAA_3221(cypD)
BAT: BAS2993
BAH: BAMEG_1392(cypD)
BAI: BAA_3269(cypD)
BANT: A16_32460
BANR: A16R_32890
BANS: BAPAT_3089
BANV: DJ46_1971(cyp102A1)
BCE: BC3211
BCA: BCE_3239(cypD)
BCR: BCAH187_A3250(cypD)
BCB: BCB4264_A3231(cypD)
BCU: BCAH820_3229(cypD)
BCG: BCG9842_B2016(cypD)
BCQ: BCQ_3034(cypD)
BCX: BCA_3251(cypD)
BNC: BCN_3047
BCF: bcf_15685
BCER: BCK_18985
BTL: BALH_2868
BTB: BMB171_C2898(cypD)
BTT: HD73_2783
BTHI: BTK_13800
BTC: CT43_CH3164(cypD)
BTM: MC28_2359
BTG: BTB_c32980(cypD)
BTI: BTG_03315
BTW: BF38_4372(cyp102A1)
BWW: bwei_1841(cypD)
BMYC: DJ92_5480(cyp102A1)
BPU: BPUM_1680
BPUM: BW16_09260
BPUS: UP12_08650
BMQ: BMQ_3237
BMD: BMD_3248
BMH: BMWSH_1945(cypD)
BMEG: BG04_163(cYP102a1)
BACW: QR42_08590
BACL: BS34A_08250(yetO) BS34A_29630(cypB)
BEO: BEH_16435
BGY: BGLY_3163
PPO: PPM_3514(M1_3883)
PPOL: X809_33460
PPQ: PPSQR21_035110(cysJ)
PPOY: RE92_19680
PMS: KNP414_03453(cypD)
PMW: B2K_06870
PSWU: SY83_13600
ASOC: CB4_02158(cypE)
MCHE: BB28_22565
MSTE: MSTE_04573
SMA: SAVERM_575(cyp2)
SCB: SCAB_5931
SCT: SCAT_4838(CYP102A)
SHY: SHJG_8055
SDV: BN159_1745(cypD)
SALU: DC74_6871
SALL: SAZ_35695
STRE: GZL_01897
SLD: T261_1104
STRM: M444_30060
SLE: sle_05650(sle_05650)
SALJ: SMD11_0205(cypD_E)
SRO: Sros_6421
SEN: SACE_4205(cypD)
PDX: Psed_5892
PSEE: FRP1_10540
KAL: KALB_657
HAU: Haur_2522
DGO: DGo_PB0521(cypD)
SACI: Sinac_6636
PBOR: BSF38_00176(cypB)
SGN: SGRA_1002
 » 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: 1.6.2.4
IUBMB Enzyme Nomenclature: 1.6.2.4
ExPASy - ENZYME nomenclature database: 1.6.2.4
BRENDA, the Enzyme Database: 1.6.2.4
CAS: 9023-03-4

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