| Entry |
|
| Name |
6,7-dihydropteridine reductase;
6,7-dihydropteridine:NAD(P)H oxidoreductase;
DHPR;
NAD(P)H:6,7-dihydropteridine oxidoreductase;
NADH-dihydropteridine reductase;
NADPH-dihydropteridine reductase;
NADPH-specific dihydropteridine reductase;
dihydropteridine (reduced nicotinamide adenine dinucleotide)
reductase;
dihydropteridine reductase;
dihydropteridine reductase (NADH);
5,6,7,8-tetrahydropteridine:NAD(P)H+ oxidoreductase |
| Class |
Oxidoreductases;
Acting on the CH-NH group of donors;
With NAD+ or NADP+ as acceptor
 |
| Sysname |
5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase |
| Reaction(IUBMB) |
a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine +
NAD(P)H + H+ [RN:R07354 R07355] |
| Reaction(KEGG) |
R07354 > R01793;
R07355 > R01794
 |
| Substrate |
5,6,7,8-tetrahydropteridine [CPD:C05650];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006] |
| Product |
6,7-dihydropteridine [CPD:C05649];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080] |
| Comment |
The substrate is the quinonoid form of dihydropteridine. Not
identical with EC 1.5.1.3 dihydrofolate reductase. |
| Pathway |
PATH: ec00790 Folate biosynthesis
PATH: ec01100 Metabolic pathways |
| Orthology |
KO: K00357 dihydropteridine reductase
KO: K10679 nitroreductase / dihydropteridine reductase |
| Genes |
HSA: 5860(QDPR)
PTR: 745779(QDPR)
MCC: 714966
MMU: 110391(Qdpr)
RNO: 64192(Qdpr)
CFA: 479082(QDPR)
BTA: 618084(QDPR)
SSC: 397619(QDPR)
ECB: 100068697
MDO: 100015089
OAA: 100074628
GGA: 426335(QDPR)
TGU: 100220845
XTR: 496990(qdpr)
DRE: 791448(qdprb1)
CIN: 100175137
SPU: 575893
DME: Dmel_CG4665(Dhpr)
DPO: Dpse_GA18340
DAN: Dana_GF10857
DER: Dere_GG14376
DPE: Dper_GL15041
DSE: Dsec_GM25120
DSI: Dsim_GD14155
DYA: Dyak_GE20807
DGR: Dgri_GH15558
DMO: Dmoj_GI16833
AGA: AgaP_AGAP002534
AAG: AaeL_AAEL006836
CQU: CpipJ_CPIJ019137
AME: 409160
NVI: 100114241
API: 100166001
ISC: IscW_ISCW022552
CEL: T03F6.1(qdpr-1)
CBR: CBG07035
BMY: Bm1_25735
SMM: Smp_086210
NVE: NEMVE_v1g242045
HMG: 100211097
TAD: TRIADDRAFT_28401
DDI: DDB_0237752(qdpr)
TGO: TGME49_085750
TET: TTHERM_00220710
PTM: GSPATT00017447001
TCR: 510689.20
LMA: LmjF34.4330 LmjF34.4360 LmjF34.4390 LmjF34.4420 LmjF34.4450
LmjF34.4480 LmjF34.4510
LIF: LinJ34.4020
LBZ: LbrM20_V2.3970
PTI: PHATR_21181
ECO: b0578(nfsB)
ECJ: JW0567(nfnB)
ECD: ECDH10B_0536(nfnB)
EBW: BWG_0449(nfsB)
ECE: Z0717(nfnB)
ECS: ECs0616
ECF: ECH74115_0659(nfnB)
ETW: ECSP_0630(nfnB)
ECG: E2348C_0478(nfsB)
ECC: c0664(nfnB)
ECI: UTI89_C0578(nfnB)
ECP: ECP_0609
ECV: APECO1_1470(nfnB)
ECW: EcE24377A_0596(nfnB)
ECX: EcHS_A0625(nfnB)
ECM: EcSMS35_0596(nfnB)
ECY: ECSE_0642
ECL: EcolC_3068
ECK: EC55989_0569(nfnB)
ECQ: ECED1_0570(nfnB)
ECR: ECIAI1_0559(nfnB)
ECT: ECIAI39_0553(nfnB)
ECZ: ECS88_0615(nfnB)
EUM: ECUMN_0668(nfnB)
ELF: LF82_1483(nfsB)
EBL: B21_00528(nfnB)
EBD: ECBD_3084
EBR: ECB_00539(nfnB)
EOH: ECO103_0583(nfnB)
EOI: ECO111_0605(nfnB)
EOJ: ECO26_0650(nfnB)
EFE: EFER_2531(nfnB)
STY: STY0620(nfnB)
STT: t2290(nfnB)
SPT: SPA2156(nfnB)
SEK: SSPA2005
SPQ: SPAB_02986
SEI: SPC_0590(nfnB)
SEC: SC0609(nfnB)
SEH: SeHA_C0690
SEE: SNSL254_A0631
SEA: SeAg_B0617
SED: SeD_A0674
SEG: SG0582(nfnB)
SET: SEN0548(nfnB)
SES: SARI_02359
STM: STM0578(nfnB)
SFX: S0493(nfnB)
SFV: SFV_0518(nfnB)
SSN: SSON_0529(nfnB)
SBO: SBO_0439(nfnB)
SBC: SbBS512_E0472(nfnB)
SDY: SDY_0491(nfnB)
ENT: Ent638_1074
ESA: ESA_01874
CTU: Ctu_21120(nfnB)
KPN: KPN_00553(nfnB)
KPE: KPK_4032(nfnB)
KPU: KP1_1487(nfnB)
CKO: CKO_02596
EIC: NT01EI_0993
ETR: ETAE_0916(nfnB)
VCH: VCA0637
VCO: VC0395_0581
VCM: VCM66_A0595
VCJ: VCD_000685
VVU: VV2_0966
VVY: VVA1455
VPA: VPA1591
VEX: VEA_000360 VEA_001134
VFI: VF_A0691(nfsB)
VFM: VFMJ11_A0778
PPU: PP_2432
PPF: Pput_3263
PPG: PputGB1_2077
PPW: PputW619_3066
PEN: PSEEN2307(nfsB)
PMY: Pmen_2015
AVN: Avin_24750
ACI: ACIAD1923(nfnB)
ACB: A1S_2111
ABY: ABAYE1451(nfnB)
ABC: ACICU_02308
ABN: AB57_2444
ABB: ABBFA_001355
SON: SO_3715
SDN: Sden_2794
SFR: Sfri_1409
SAZ: Sama_2932
SBL: Sbal_3396
SBM: Shew185_0943
SBN: Sbal195_0977
SBP: Sbal223_0966
SLO: Shew_0688
SPC: Sputcn32_3034
SSE: Ssed_3785
SPL: Spea_2510
SHE: Shewmr4_3061
SHM: Shewmr7_0911
SHN: Shewana3_0876
SHW: Sputw3181_0911
SHL: Shal_1742
SWD: Swoo_2454
SWP: swp_1100
CPS: CPS_4747
PHA: PSHAa1234
FTU: FTT_0304c(nfnB)
FTF: FTF0304c(nfnB)
FTW: FTW_1781(nfnB)
FTL: FTL_0215
FTH: FTH_0210(nfnB)
FTA: FTA_0231
FTM: FTM_1548(nfnB)
FTN: FTN_0218(nfnB)
FPH: Fphi_0606
TCX: Tcr_1024
MMW: Mmwyl1_3894
CVI: CV_2244(nfnB)
RME: Rmet_3717
BCJ: BCAS0700
BXE: Bxe_A2684
DAR: Daro_1868
DDE: Dde_0086
DSA: Desal_1315
DPS: DP0728
HBA: Hbal_1083
APT: APA01_08130
MAB: MAB_3310c
FJO: Fjoh_0114
COC: Coch_0484
AMU: Amuc_2137
 |
| Structures |
PDB: 1YKI 1YLR 1YLU 3BM1 3BM2 |
Reference Authors Title
Journal
|
1
Harano, T.
New diaphorases from Bombyx silkworm eggs. NADH/NADPH cytochrome c
reductase activity mediated with 6,7-dimethyltetrahydropterin.
Insect Biochem. 2 (1972) 385-399. |
Reference Authors Title
Journal Organism
|
2 [PMID:191436]
Hasegawa H.
Dihydropteridine reductase from bovine liver. Purification,
crystallization, and isolation of a binary complex with NADH.
J. Biochem. (Tokyo). 81 (1977) 169-77.
Bos taurus [GN:bta] |
Reference Authors Title Journal
|
3
Kaufman, S.
Phenylalanine hydroxylase.
Methods Enzymol. 5 (1962) 809-816. |
Reference Authors Title
Journal Organism
|
4 [PMID:4402916]
Lind KE.
Dihydropteridine reductase. Investigation of the specificity for
quinoid dihydropteridine and the inhibition by
2,4-diaminopteridines.
Eur. J. Biochem. 25 (1972) 560-2.
Rattus norvegicus [GN:rno] |
Reference Authors Title Journal Organism
|
5 [PMID:16875]
Nakanishi N, Hasegawa H, Watabe S.
A new enzyme, NADPH-dihydropteridine reductase in bovine liver.
J. Biochem. (Tokyo). 81 (1977) 681-5.
Bos taurus [GN:bta] |
| Other DBs |
ExplorEnz - The Enzyme Database: 1.5.1.34
IUBMB Enzyme Nomenclature: 1.5.1.34
ExPASy - ENZYME nomenclature database: 1.5.1.34
BRENDA, the Enzyme Database: 1.5.1.34
CAS: 9074-11-7 |