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]
History
EC 1.2.1.5 created 1961
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)
MCF: 
102115665(ALDH1A3) 102120140(ALDH3B1) 102122172 102140050(ALDH3A1)
MMU: 
11670(Aldh3a1) 56847(Aldh1a3) 621603(Aldh3b2) 67689(Aldh3b1) 73458(1700055N04Rik)
RNO: 
25375(Aldh3a1) 266603(Aldh1a3) 309147(Aldh3b1) 688778
CGE: 
100755596 100756470 100757371(Aldh3a1) 100763332(Aldh3b2) 100768227(Aldh1a3)
HGL: 
101699453(Aldh3a1) 101700669(Aldh1a3) 101722793(Aldh3b1) 101724442(Aldh3b2)
TUP: 
102470787 102474716(ALDH3B1) 102475132 102490907(ALDH3A1) 102491549(ALDH1A3)
CFA: 
100856346(ALDH1A3) 476003(ALDH3B1) 489526(ALDH3A1)
AML: 
FCA: 
101081050(ALDH1A3) 101093802 101094208(ALDH3B1) 101096364(ALDH3A1)
PTG: 
102952022(ALDH1A3) 102953099(ALDH3A1) 102969525(ALDH3B1)
BTA: 
281617(ALDH3A1) 507093(ALDH1A3) 508879 511469(ALDH3B1)
BOM: 
102267436 102267473(ALDH3B1) 102269123(ALDH3A1) 102273352 102284286(ALDH1A3)
PHD: 
102331077(ALDH3A1) 102332149(ALDH3B1) 102337504 102344693(ALDH1A3)
CHX: 
102179701(ALDH3A1) 102179885(ALDH1A3) 102185156 102185988(ALDH3B1)
OAS: 
101108502(ALDH3A1) 101109831(ALDH1A3) 101111922 101112687(ALDH3B1)
SSC: 
100155494 100526075(ALDH3A1) 100739347(ALDH3B1)
CFR: 
102504927(ALDH1A3) 102508421 102512509(ALDH3A1) 102521023(ALDH3B1)
BACU: 
103000712(ALDH3A1) 103004940(ALDH3B1) 103013550(ALDH1A3)
LVE: 
103068962(ALDH3B1) 103078726(ALDH3B2) 103082981(ALDH1A3) 103083340(ALDH3A1)
ECB: 
100053339(ALDH3B1) 100057072(ALDH1A3) 100073157(ALDH3A1)
MYB: 
102241863(ALDH1A3) 102255064 102255772(ALDH3B1) 102260012(ALDH3A1)
MYD: 
102758582(ALDH1A3) 102761807(ALDH3B1) 102762385 102774766(ALDH3A1)
PALE: 
102888323 102889864(ALDH1A3) 102889891(ALDH3A1) 102895234(ALDH3B1)
MDO: 
100010416(ALDH3B1) 100020100 100020131(ALDH3A1) 100616732(ALDH1A3)
SHR: 
OAA: 
100077088(ALDH3A1) 100083368(ALDH1A3)
GGA: 
395389(ALDH1A3) 428812 428813(ALDH3B1)
MGP: 
TGU: 
100231202(ALDH1A3) 100232483(ALDH3B1)
FAB: 
101809399 101809598(ALDH3B1) 101816772(ALDH1A3)
PHI: 
102103263 102103447(ALDH3B1) 102105549(ALDH1A3)
APLA: 
FPG: 
101915870(ALDH1A3) 101919850(ALDH3B1) 101920028
FCH: 
102050613(ALDH1A3) 102058662(ALDH3B1) 102058835
CLV: 
102089147(ALDH1A3) 102096341(ALDH3B1)
ASN: 
AMJ: 
PSS: 
102450892(ALDH1A3)
CMY: 
102931111 102936985(ALDH3B1) 102939103(ALDH1A3)
ACS: 
PBI: 
XLA: 
447062(aldh3b1) 733178(aldh1a3)
XTR: 
100145787(aldh3b1) 100485844(aldh1a3) 548883(aldh3b1)
DRE: 
282559(aldh3b1) 557008 751785(aldh1a3)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
DME: 
Dmel_CG11140(Aldh-III)
CEL: 
CCP: 
SCE: 
YMR169C(ALD3) YMR170C(ALD2)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0D00880(NCAS0D00880)
NDI: 
NDAI_0H03250(NDAI0H03250)
TDL: 
TDEL_0G02690(TDEL0G02690)
KAF: 
KAFR_0B04820(KAFR0B04820)
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_1204144(AO090023000697) AOR_1_1330014(AO090026000741)
ANG: 
ANI_1_1748184(An04g03400)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
SPO: 
TMS: 
LBC: 
DPP: 
PTI: 
PNA: 
ADE: 
RHA: 
AVA: 
CCH: 
CPH: 
 » show all
Taxonomy
Reference
1  [PMID:14904038]
  Authors
BLACK S.
  Title
Yeast aldehyde dehydrogenase.
  Journal
Arch. Biochem. 34 (1951) 86-97.
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.
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.
Reference
5  [PMID:13363916]
  Authors
TANENBAUM SW.
  Title
The metabolism of Acetobacter peroxidans.  I.  Oxidative enzymes.
  Journal
Biochim. Biophys. Acta. 21 (1956) 335-42.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9028-88-0

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