KEGG   ENZYME: 1.1.1.2Help
Entry
EC 1.1.1.2                  Enzyme                                 
Name
alcohol dehydrogenase (NADP+);
aldehyde reductase (NADPH2);
NADP-alcohol dehydrogenase;
NADP+-aldehyde reductase;
NADP+-dependent aldehyde reductase;
NADPH-aldehyde reductase;
NADPH-dependent aldehyde reductase;
nonspecific succinic semialdehyde reductase;
ALR 1;
low-Km aldehyde reductase;
high-Km aldehyde reductase;
alcohol dehydrogenase (NADP)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
alcohol:NADP+ oxidoreductase
Reaction(IUBMB)
an alcohol + NADP+ = an aldehyde + NADPH + H+ [RN:R07328]
Reaction(KEGG)
Substrate
alcohol [CPD:C00069];
NADP+ [CPD:C00006]
Product
aldehyde [CPD:C00071];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
A zinc protein. Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. May be identical with EC 1.1.1.19 (L-glucuronate reductase), EC 1.1.1.33 [mevaldate reductase (NADPH)] and EC 1.1.1.55 [lactaldehyde reductase (NADPH)]. A-specific with respect to NADPH.
Pathway
Glycolysis / Gluconeogenesis
Glycerolipid metabolism
Caprolactam degradation
Metabolic pathways
Biosynthesis of secondary metabolites
Microbial metabolism in diverse environments
Orthology
K00002  
alcohol dehydrogenase (NADP+)
Genes
HSA: 
10327(AKR1A1)
PTR: 
741418(AKR1A1)
PPS: 
100990701(AKR1A1)
GGO: 
101124639(AKR1A1)
PON: 
100173796(AKR1A1)
MCC: 
693380(AKR1A1)
MMU: 
58810(Akr1a1)
RNO: 
78959(Akr1a1)
CFA: 
610537(AKR1A1)
AML: 
FCA: 
101091464(AKR1A1)
BTA: 
618607(AKR1A1)
SSC: 
396924(AKR1A1)
ECB: 
100052360(AKR1A1)
MDO: 
100024617
SHR: 
100933920(AKR1A1)
OAA: 
100076515
GGA: 
424599(AKR1A1)
MGP: 
100547531
TGU: 
100220342(AKR1A1)
ACS: 
100553683
XLA: 
444488(akr1a1)
XTR: 
548891(akr1a1)
DRE: 
799805(akr1a1b)
TRU: 
101077149
OLA: 
101172969
SPU: 
587281
DME: 
Dmel_CG2767
NVE: 
NEMVE_v1g181888
TAD: 
TRIADDRAFT_29280
AQU: 
100632875
OSA: 
4338987
CME: 
CMM296C
SCE: 
YCR105W(ADH7) YMR318C(ADH6)
KLA: 
KLLA0E19889g
LTH: 
KLTH0B04972g KLTH0E07964g
PPA: 
PAS_chr1-1_0357 PAS_chr4_0576
VPO: 
Kpol_1057p24 Kpol_257p4 Kpol_526p18 Kpol_529p30
ZRO: 
ZYRO0G10318g
CGR: 
CAGL0H06853g CAGL0M14047g
DHA: 
DEHA2C04488g DEHA2C04510g DEHA2C17666g
PIC: 
PICST_29079(ADH4) PICST_31312(ADH5) PICST_45137(ADH7)
PGU: 
PGUG_05188 PGUG_05764
LEL: 
LELG_04799
CAL: 
CaO19.12963(ADH7) CaO19.5517(ADH7)
CTP: 
CTRG_02797
CDU: 
CD36_62710
COT: 
CORT_0F02920
CLU: 
CLUG_03198 CLUG_03199 CLUG_03797 CLUG_05090
NCR: 
NCU04823 NCU11179
PAN: 
PODANSg2904 PODANSg4584
MGR: 
MGG_00220 MGG_06489 MGG_11818
FGR: 
FG06619.1 FG08980.1
SSL: 
SS1G_00401 SS1G_07135
BFU: 
BC1G_00717 BC1G_10210
ANI: 
AN2860.2
NFI: 
NFIA_065400
AFM: 
AFUA_1G09750 AFUA_3G11900 AFUA_6G10260
AOR: 
AOR_1_1328154(AO090003000751) AOR_1_780144(AO090023000460)
AFV: 
AFLA_030660
ACT: 
ACLA_039770
PCS: 
Pc18g00530
CPW: 
CPC735_041920
URE: 
UREG_02137
TVE: 
TRV_03693
PNO: 
SNOG_15556
CNE: 
CNC05140 CNK02370
CNB: 
CNBC2030
PPL: 
POSPLDRAFT_106595 POSPLDRAFT_88715
UMA: 
UM01861.1
MBR: 
MONBRDRAFT_32881
EHI: 
EHI_023110(81.t00034) EHI_039190(73.t00013) EHI_198760(34.t00053)
EDI: 
EDI_247390 EDI_307670
TET: 
TTHERM_00274500
TCR: 
504339.19 504425.60 508677.80 509331.210
LMA: 
LMJF_23_0360
TVA: 
TVAG_344880
PTI: 
PHATRDRAFT_41470
TPS: 
THAPSDRAFT_40021
XFA: 
XF1136 XF1727 XF1734
XFT: 
PD0423(adhP)
PST: 
PSPTO_2182
PSB: 
Psyr_1992
PSP: 
PSPPH_1961
CBD: 
CBUD_1937
CBG: 
CbuG_1847
ABO: 
ABO_2414(AKR1A1)
RSO: 
RSc0632
HPJ: 
jhp1429
ABU: 
Abu_0783
DPR: 
Despr_0031
ATU: 
Atu2022(adh)
CCE: 
Ccel_1009
CGL: 
NCgl0324(Cgl0331)
CGB: 
cg0400(adhC)
CGT: 
cgR_0413
CEF: 
CE0338
CJK: 
jk2055(adhA)
KRH: 
KRH_19860(adhC)
PAC: 
PPA1072
SEN: 
SACE_2652
LIC: 
LIC10949(dkgA)
PPN: 
Palpr_2608
SRU: 
SRU_1267
SRM: 
SRM_01456
CMR: 
Cycma_3529
MTT: 
Ftrac_3685
GFO: 
GFO_1874
ZPR: 
ZPR_1868
CAT: 
CA2559_11288
SYN: 
slr0942
SYG: 
sync_0822
CYT: 
cce_0782
MAC: 
MA0403
MBA: 
Mbar_A0771
MST: 
Msp_0967(adh)
HMA: 
pNG7101(adh8)
HWA: 
HQ1729A(adh)
 » show all
Taxonomy
Reference
1  [PMID:4402936]
  Authors
Bosron WF, Prairie RL.
  Title
Triphosphopyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex.
  Journal
J. Biol. Chem. 247 (1972) 4480-5.
  Organism
Sus scrofa [GN:ssc]
Reference
2
  Authors
DeMoss, R.
  Title
Triphosphopyridine nucleotide-specific ethanol dehydrogenase from Leuconostoc mesenteroides.
  Journal
Bacteriol. Proc. (1953) 81.
Reference
3
  Authors
Reeves, R.E., Montalvo, F.E. and Lushbaugh, T.S.
  Title
Nicotinamide-adenine dinucleotide phosphate-dependent alcohol dehydrogenase. Enzyme from Entamoeba histolytica and some enzyme inhibitors.
  Journal
Int. J. Biochem. 2 (1971) 55-64.
Reference
4  [PMID:4393513]
  Authors
Tabakoff B, Erwin VG.
  Title
Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain.
  Journal
J. Biol. Chem. 245 (1970) 3263-8.
  Organism
Bos taurus [GN:bta]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9028-12-0
DBGET integrated database retrieval system