KEGG   ENZYME: 1.2.1.5Help
Entry
EC 1.2.1.5                  Enzyme                                 
Name
aldehyde dehydrogenase [NAD(P)+];
ALDH
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
aldehyde:NAD(P)+ oxidoreductase
Reaction(IUBMB)
an aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H + H+ [RN:R00538 R00634]
Reaction(KEGG)
Substrate
aldehyde [CPD:C00071];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Product
carboxylate [CPD:C00060];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Pathway
Glycolysis / Gluconeogenesis
Histidine metabolism
Tyrosine metabolism
Phenylalanine metabolism
beta-Alanine metabolism
Metabolism of xenobiotics by cytochrome P450
Drug metabolism - cytochrome P450
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K00129  
aldehyde dehydrogenase (NAD(P)+)
Genes
HSA: 
218(ALDH3A1) 220(ALDH1A3) 221(ALDH3B1) 222(ALDH3B2)
PTR: 
453686(ALDH1A3) 466685(ALDH3B1) 468186(ALDH3A1)
PPS: 
100967518(ALDH1A3) 100970713(ALDH3A1) 100992841 100993681(ALDH3B1)
GGO: 
101131216(ALDH3A1) 101135029(ALDH1A3) 101147407(ALDH3B1)
PON: 
100446485(ALDH3A1) 100450634(ALDH3B1) 100452276(ALDH1A3)
MCC: 
694231(ALDH1A3) 703870(ALDH3A1) 710746(ALDH3B1) 721683(ALDH3B2)
MMU: 
11670(Aldh3a1) 56847(Aldh1a3) 621603(Aldh3b2) 67689(Aldh3b1) 73458(1700055N04Rik)
RNO: 
25375(Aldh3a1) 266603(Aldh1a3) 309147(Aldh3b1) 688778
CFA: 
100856346 476003(ALDH3B1) 489526(ALDH3A1)
AML: 
FCA: 
101081050(ALDH1A3) 101093802 101094208(ALDH3B1) 101096364(ALDH3A1)
BTA: 
281617(ALDH3A1) 507093(ALDH1A3) 508879 511469(ALDH3B1)
SSC: 
100155494 100522421 100526075(ALDH3A1)
ECB: 
100053339(ALDH3B1) 100057072(ALDH1A3)
MDO: 
100010416 100020100 100020131(ALDH3A1) 100616732
SHR: 
100920413(ALDH1A3) 100934715(ALDH3A1)
OAA: 
100077088(ALDH3A1) 100083368
GGA: 
395389(ALDH1A3) 428812 428813(ALDH3B1)
MGP: 
100546607 100548954(ALDH3B1)
TGU: 
100231202(ALDH1A3) 100232483(ALDH3B1)
ACS: 
100555228 100558516 100559308 100559631
XLA: 
447062(aldh3b1) 733178(aldh1a3)
XTR: 
100145787(aldh3b1) 100485844(aldh1a3) 548883(aldh3b1)
DRE: 
282559(aldh3b1) 751785(aldh1a3)
TRU: 
100294697(raldh3)
OLA: 
101158531
DME: 
Dmel_CG11140(Aldh-III)
CEL: 
CELE_T08B1.3(alh-5)
SCE: 
YMR169C(ALD3) YMR170C(ALD2)
AGO: 
AGOS_AFL201W
ERC: 
Ecym_3381
KLA: 
KLLA0D09999g KLLA0D10021g
LTH: 
KLTH0F09658g KLTH0F09680g
PPA: 
PAS_chr2-1_0453
VPO: 
Kpol_534p18
ZRO: 
ZYRO0A07216g ZYRO0A07238g
CGR: 
CAGL0F07777g
NCS: 
NCAS_0D00880(NCAS0D00880)
NDI: 
NDAI_0H03250(NDAI0H03250)
TDL: 
TDEL_0G02690(TDEL0G02690)
KAF: 
KAFR_0B04820(KAFR0B04820)
DHA: 
DEHA2G22572g
PIC: 
PICST_63844(ALD2)
PGU: 
PGUG_00081
LEL: 
LELG_03249
CAL: 
CaO19.13683 CaO19.6306(ALD4)
CTP: 
CTRG_00532
CDU: 
CD36_00340 CD36_30260
COT: 
CORT_0D04080
YLI: 
YALI0D07942g YALI0F04444g
CLU: 
CLUG_03192
NCR: 
NCU00378
SMP: 
SMAC_06449
PAN: 
PODANSg4863
TTT: 
THITE_2119481
MTM: 
MYCTH_2304244
MGR: 
MGG_05008 MGG_07270
FGR: 
FG02160.1 FG02273.1
NHE: 
NECHADRAFT_72458 NECHADRAFT_98069
VAL: 
VDBG_05141 VDBG_08711
SSL: 
SS1G_00782
BFU: 
BC1G_02079
ANI: 
AN1689.2
NFI: 
NFIA_107580
AFM: 
AFUA_4G08600 AFUA_4G13500
AOR: 
AOR_1_1204144(AO090023000697)
ANG: 
ANI_1_1748184(An04g03400)
AFV: 
AFLA_111070
ACT: 
ACLA_047970
PCS: 
Pc18g02760 Pc22g17230
CIM: 
CIMG_08871
CPW: 
CPC735_056920 CPC735_063850
URE: 
UREG_02786
ABE: 
ARB_05929
TVE: 
TRV_00129
AJE: 
HCAG_06205
PNO: 
SNOG_00086
PTE: 
PTT_15834
ZTR: 
MYCGRDRAFT_39109(ALD2)
SPO: 
SPAC922.07c
LBC: 
LACBIDRAFT_392399
PTI: 
PHATRDRAFT_16540
PNA: 
Pnap_4188
ADE: 
Adeh_1143
RHA: 
RHA1_ro01724
AVA: 
Ava_3615
CCH: 
Cag_1754
CPH: 
Cpha266_2158
 » show all
Taxonomy
Reference
1  [PMID:14904038]
  Authors
BLACK S.
  Title
Yeast aldehyde dehydrogenase.
  Journal
Arch. Biochem. 34 (1951) 86-97.
  Organism
Saccharomyces cerevisiae [GN:sce]
Reference
2
  Authors
Jakoby, W.B.
  Title
Aldehyde dehydrogenases.
  Journal
In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
Reference
3  [PMID:13319337]
  Authors
KING TE, CHELDELIN VH.
  Title
Oxidation of acetaldehyde by Acetobacter suboxydans.
  Journal
J. Biol. Chem. 220 (1956) 177-91.
  Organism
Aerobacter suboxydans
Reference
4  [PMID:4293780]
  Authors
Steinman CR, Jakoby WB.
  Title
Yeast aldehyde dehydrogenase. I. Purification and crystallization.
  Journal
J. Biol. Chem. 242 (1967) 5019-23.
  Organism
Acetobacter peroxidans
Reference
5  [PMID:13363916]
  Authors
TANENBAUM SW.
  Title
The metabolism of Acetobacter peroxidans.  I.  Oxidative enzymes.
  Journal
Biochim. Biophys. Acta. 21 (1956) 335-42.
  Organism
Acetobacter peroxidans
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9028-88-0
DBGET integrated database retrieval system