1.2.1.5: aldehyde dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about aldehyde dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.2.1.5
-
1.2.1.5
-
aldhs
-
retinoic
-
disulfiram
-
alcohol-induced
-
benzaldehyde
-
nadp+-dependent
-
retinaldehyde
-
cyanamide
-
meta-cleavage
-
aldh2*2
-
phosphotransacetylase
-
1.2.1.3
-
hangover
-
alcohol-related
-
medicine
-
energy production
-
synthesis
-
analysis
-
degradation
- 1.2.1.5
-
aldhs
-
retinoic
- disulfiram
-
alcohol-induced
- benzaldehyde
-
nadp+-dependent
- retinaldehyde
- cyanamide
-
meta-cleavage
-
aldh2*2
- phosphotransacetylase
-
1.2.1.3
-
hangover
-
alcohol-related
- medicine
- energy production
- synthesis
- analysis
- degradation
Reaction
Synonyms
acetaldehyde dehydrogenase, ALD4, aldehyde dehydrogenase, aldehyde dehydrogenase 1A3, aldehyde dehydrogenase 2, aldehyde dehydrogenase 3A1, aldehyde: NAD(P)+ oxidoreductase, ALDH, ALDH1, ALDH13, ALDH17, ALDH1a, ALDH1A1, Aldh1a3, ALDH1b, ALDH2, ALDH2a, ALDH2b, ALDH3, ALDH3A1, Aldh3b1, ALDH3F1, ALDH3H1, ALDH3I1, ALDH7B7, ALDH9, ALDHC, ALDHIII, BcALDH, BCP54, chromosomally encoded box pathway ALDH, class 3 aldehyde dehydrogenase, Corneal 15.8 kDa protein, Corneal protein 54, dehydrogenase, aldehyde (nicotinamide adenine dinucleotide (phosphate)), HTC-ALDH, K-ACDH, MI dehydrogenase, More, myo-inositol dehydrogenase, NAD(P)(+)-dependent aldehyde dehydrogenase, NAD(P)+-dependent aldehyde dehydrogenase, NAD+-dependent Ald4, nicotinprotein aldehyde dehydrogenase, OsALDH2-1, OsALDH2-2, OsALDH2-3, OsALDH2-4, OsALDH2-5, OsALDH22, OsALDH3-1, OsALDH3-2, OsALDH3-3, OsALDH3-4, OsALDH3-5, OsALDH5, OsALDH7, PEG-ALDH, PuuC, ST0064, succinic semialdehyde dehydrogenase, Transparentin, Tumor-associated aldehyde dehydrogenase, ybcD
ECTree
1.2.1.5 aldehyde dehydrogenase [NAD(P)+]Advanced search results
results (
results (Substrates Products
Substrates Products on EC 1.2.1.5 - aldehyde dehydrogenase [NAD(P)+]
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3-dihydroxyacetone + NAD+ + H2O
? + NADH + H+
53.93% of the activity compared to acetaldehyde
-
-
?
1-formyl-6-methylpyrene + NADP+ + H2O
6-methylpyrene-1-carboxylic acid + NADPH + H+
-
-
-
?
1-formyl-8-methylpyrene + NADP+ + H2O
8-methylpyrene-1-carboxylic acid + NADPH + H+
-
-
-
?
1-formylpyrene + NADP+ + H2O
pyrene-1-carboxylic acid + NADPH + H+
-
-
-
?
2,5-dihydroxybenzaldehyde + NADP+ + H2O
2,5-dihydroxybenzoate + NADPH + H+
-
-
-
-
?
2-formylpyrene + NADP+ + H2O
pyrene-2-carboxylic acid + NADPH + H+
-
-
-
?
3,4-dihydroxymandelaldehyde + NAD+ + H2O
3,4-dihydroxyphenylmandelate + NADH + H+
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+
3,4-dihydroxyphenylacetate + NADH
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
?
3,4-dihydroxyphenylglycolaldehyde + NAD+ + H2O
3,4-dihydroxyphenylglycolate + NADH + H+
-
-
-
?
3-hydroxybenzaldehyde + NADP+ + H2O
3-hydroxybenzoate + NADPH + H+
-
-
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
32.98% of the activity compared to acetaldehyde
-
-
?
4-carboxybenzaldehyde + NADP+ + H2O
4-carboxybenzoate + NADPH + H+
-
-
-
-
?
4-chlorobenzaldehyde + NADP+ + H2O
4-chlorobenzoate + NADPH + H+
-
-
-
-
?
4-formylpyrene + NADP+ + H2O
pyrene-4-carboxylic acid + NADPH + H+
-
-
-
?
4-hydroxy-2-nonenal + NADP+ + H2O
4-hydroxy-2-nonenoic acid + NADPH + H+
-
-
-
-
r
4-pyridinecarboxaldehyde + NAD+ + H2O
4-pyridinecarboxylate + NADH + H+
-
-
-
-
?
5-hydroxyindole-3-acetyldehyde + NAD+ + H2O
5-hydroxyindole-3-acetate + NADH + H+
-
-
-
-
?
6-methoxy-2-naphthaldehyde + NADH + H+
(6-methoxynaphthalen-2-yl)methanol + NAD+
-
-
-
?
acetaldehyde + 3-pyridine aldehyde adenine dinucleotide phosphate
acetate + ?
-
-
-
-
?
aldophosphamide + NAD+
N,N-bis-(2-chloroethyl)-diaminophosphoric-(2-carboxyethylester) + ?
-
-
-
-
?
all-trans-retinol + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
-
-
-
?
all-trans-retinol + NADP+ + H2O
all-trans-retinoic acid + NADPH + H+
-
-
-
?
D-glyceraldehyde + NAD+ + H2O
D-glycerate + NADH + H+
50.25% of the activity compared to acetaldehyde. kcat/KM for NAD+ with D-glyceraldehyde as cosubstrate is 3.8fold higher compared to NADP+
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH
50.25% of the activity compared to acetaldehyde
-
-
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
D-glycerate 3-phosphate + NADH + H+
52.7% of the activity compared to acetaldehyde
-
-
?
DL-glyceraldehyde + NAD(P)+ + H2O
glycerate + NAD(P)H + H+
-
14% of activity with benzaldehyde
-
-
ir
glycolaldehyde + NAD+ + H2O
glycolate + NADH + H+
75.43% of the activity compared to acetaldehyde
-
-
?
heptanal + NADP+ + H2O
heptanoate + NADPH + H+
-
-
-
?
isovaleraldehyde + NADP+ + H2O
isovalerate + NADPH + H+
-
-
-
?
n-tetradecanal + NADP+ + H2O
n-tetradecanoate + NADPH + H+
-
-
-
-
?
p-hydroxybenzaldehyde + NADP+ + H2O
p-hydroxybenzoic acid + NADPH + H+
-
-
-
?
polyethylene glycol 4000-aldehyde + NADP+
? + NADPH
-
highest activtiy compared to other polyethylene glycolaldehydes
-
-
?
propanal + 1,N6-ethenoadenine dinucleotide
propionate + ?
-
isoenzyme E1 and E2
-
-
?
propanal + 3-acetylpyridine adenine dinucleotide
propionate + ?
-
isoenzyme E1 and E2
-
-
?
propanal + 3-pyridine adenine dinucleotide
propionate + ?
-
isoenzyme E1 and E2
-
-
?
propanal + beta-NADP+ + H2O
propionate + beta-NADPH + H+
-
isoenzyme E1 and E2
-
-
?
propanal + oxidized nicotinamide hypoxanthine dinucleotide + H2O
propionate + reduced nicotinamide hypoxanthine dinucleotide
-
isoenzyme E1 and E2
-
-
?
propionaldehyde + 3-pyridinealdehyde adenine dinucleotide + H2O
propionate + reduced 3-pyridinealdehyde adenine dinucleotide + H+
-
-
-
-
r
propionaldehyde + N-1,N6-ethenoadenine dinucleotide + H2O
propionate + reduced N-1,N6-ethenoadenine dinucleotide + H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoic acid + NADH + H+
preferred substrate of isozyme ALDH1A3
-
-
?
valeraldehyde + NADP+ + H2O
valerate + NADPH + H+
-
-
-
?
2-bromobenzaldehyde + NAD+ + H2O
2-bromobenzoate + NADH + H+
-
-
-
-
?
2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + H+
-
-
-
-
?
2-fluorobenzaldehyde + NAD+ + H2O
2-fluorobenzoate + NADH + H+
-
-
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
-
-
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
-
-
-
-
?
acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
-
51% of activity with benzaldehyde
-
-
ir
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
activity with the enzyme from stomach mucosa, no activity with the enzyme from breast adenocarcinoma cell line
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
kcat/KM for NAD+ with acetaldehyde as cosubstrate is 2.5fold higher compared to NADP+
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
kcat/KM for NAD+ with acetaldehyde as cosubstrate is 2.5fold higher compared to NADP+
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
-
-
-
?
all-trans-retinal + NADP+ + H2O
all-trans-retinol + NADPH + H+
-
-
-
?
all-trans-retinal + NADP+ + H2O
all-trans-retinol + NADPH + H+
-
-
-
?
an aldehyde + NAD+ + H2O
a carboxylate + NADH + H+
-
-
-
?
an aldehyde + NADP+ + H2O
a carboxylate + NADPH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
ALDH2 is very active, low activity with ALDH1 and ALDH5
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
35.5% of the activity compared to acetaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
35.5% of the activity compared to acetaldehyde
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
25% of activity with NAD+
-
-
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
-
-
?
butyraldehyde + NAD(P)+ + H2O
butanoate + NAD(P)H + H+
-
23% of activity with benzaldehyde
-
-
ir
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
48.15% of the activity compared to acetaldehyde
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
48.15% of the activity compared to acetaldehyde
-
-
?
formaldehyde + NAD(P)+ + H2O
formate + NAD(P)H + H+
-
52% of activity with benzaldehyde
-
-
ir
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
-
-
?
furfuryl aldehyde + NAD+ + H2O
2-furancarboxylate + NADH + H+
-
4% of the activity with acetaldehyde
-
-
?
furfuryl aldehyde + NAD+ + H2O
2-furancarboxylate + NADH + H+
-
4% of the activity with acetaldehyde
-
-
?
heptylaldehyde + NAD(P)+ + H2O
heptanoate + NAD(P)H + H+
-
12% of activity with benzaldehyde
-
-
ir
hexylaldehyde + NAD(P)+ + H2O
hexanoate + NAD(P)H + H+
-
22% of activity with benzaldehyde
-
-
ir
isobutyraldehyde + NAD(P)+ + H2O
isobutanoate + NAD(P)H + H+
-
-
-
?, ir
isobutyraldehyde + NAD(P)+ + H2O
isobutanoate + NAD(P)H + H+
-
188% of activity with benzaldehyde
-
-
ir
isovaleraldehyde + NAD(P)+ + H2O
isovalerate + NAD(P)H
-
83% of activity with benzaldehyde
-
-
ir
isovaleraldehyde + NADP+
isovalerate + NADPH + H+
-
-
-
-
?
m-bromobenzaldehyde + NAD(P)+ + H2O
m-bromobenzoate + NAD(P)H + H+
-
-
-
ir
m-bromobenzaldehyde + NAD(P)+ + H2O
m-bromobenzoate + NAD(P)H + H+
-
28% of activity with benzaldehyde
-
-
ir
m-chlorobenzaldehyde + NAD(P)+ + H2O
m-chlorobenzoate + NAD(P)H + H+
-
-
-
ir
m-chlorobenzaldehyde + NAD(P)+ + H2O
m-chlorobenzoate + NAD(P)H + H+
-
35% of activity with benzaldehyde
-
-
ir
m-fluorobenzaldehyde + NAD(P)+ + H2O
m-fluorobenzoate + NAD(P)H + H+
-
-
-
ir
m-fluorobenzaldehyde + NAD(P)+ + H2O
m-fluorobenzoate + NAD(P)H + H+
-
41% of activity with benzaldehyde
-
-
ir
n-butanal + NAD+ + H2O
butanoate + NADH + H+
-
62% of the activity with acetaldehyde
-
-
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
-
55% of the activity with acetaldehyde
-
-
?
o-fluorobenzaldehyde + NAD(P)+ + H2O
o-fluorobenzoate + NAD(P)H + H+
-
-
-
ir
o-fluorobenzaldehyde + NAD(P)+ + H2O
o-fluorobenzoate + NAD(P)H + H+
-
100% of activity with benzaldehyde
-
-
ir
o-methoxybenzaldehyde + NAD(P)+ + H2O
o-methoxybenzoate + NAD(P)H + H+
-
-
-
ir
o-methoxybenzaldehyde + NAD(P)+ + H2O
o-methoxybenzoate + NAD(P)H + H+
-
18% of activity with benzaldehyde
-
-
ir
octylaldehyde + NAD(P)+ + H2O
octanoate + NAD(P)H + H+
-
10% of activity with benzaldehyde
-
-
ir
p-bromobenzaldehyde + NAD(P)+ + H2O
p-bromobenzoate + NAD(P)H + H+
-
-
-
ir
p-bromobenzaldehyde + NAD(P)+ + H2O
p-bromobenzoate + NAD(P)H + H+
-
14% of activity with benzaldehyde
-
-
ir
p-chlorobenzaldehyde + NAD(P)+ + H2O
p-chlorobenzoate + NAD(P)H + H+
-
-
-
ir
p-chlorobenzaldehyde + NAD(P)+ + H2O
p-chlorobenzoate + NAD(P)H + H+
-
35% of activity with benzaldehyde
-
-
ir
p-fluorobenzaldehyde + NAD(P)+ + H2O
p-fluorobenzoate + NAD(P)H + H+
-
-
-
ir
p-fluorobenzaldehyde + NAD(P)+ + H2O
p-fluorobenzoate + NAD(P)H + H+
-
75% of activity with benzaldehyde
-
-
ir
p-isopropylbenzaldehyde + NAD(P)+ + H2O
p-isopropylbenzoate + NAD(P)H + H+
-
-
-
ir
p-isopropylbenzaldehyde + NAD(P)+ + H2O
p-isopropylbenzoate + NAD(P)H + H+
-
15% of activity with benzaldehyde
-
-
ir
propanal + 3-thionicotinamide adenine dinucleotide
propionate + ?
-
isoenzyme E1
-
-
?
propanal + 3-thionicotinamide adenine dinucleotide
propionate + ?
-
no reaction with isoenzyme E2
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
88% of the activity with acetaldehyde
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
88% of the activity with acetaldehyde
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD(P)+ + H2O
propionate + NAD(P)H
-
75% of activity with benzaldehyde
-
-
ir
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
best substrate combination
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
best substrate combination
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
r
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
56.22% of the activity compared to acetaldehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
56.22% of the activity compared to acetaldehyde
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
-
-
?
valeraldehyde + NAD(P)+ + H2O
valerate + NAD(P)H + H+
-
16.3% of activity with benzaldehyde
-
-
ir
additional information
?
-
no activity with 9-cis-retinal and 13-cis-retinal
-
-
?
additional information
?
-
-
no activity with 9-cis-retinal and 13-cis-retinal
-
-
?
additional information
?
-
in the first acylation step, the activated catalytic Cys, Cys300 in BcALDH, attacks the substrate aldehyde group to form a thio-hemiacetal intermediate. The oxidized NAD(P)+ cofactor takes up a hydride ion from the thio-hemiacetal intermediate, which transforms it to a thioester intermediate. This intermediate is then deacylated by a water molecule, in which the additional catalytic residue Glu, Glu266 in BcALDH, activates the hydrolytic water molecule by abstracting a proton. Finally, the reduced NAD(P)H is released. Plausible mechanism for the minor reducing activity of BcALDH with all-trans-retinal, overview. The beta-ionone ring of the superimposed retinoic acid (REA) is bound at the mouth of the channel and exposed to the solvent. The substrate binding pocket-bound REA shows a bent conformation in the carbon positions from 9 to 11. Molecular docking of retinoic acid into the enzyme structure. BcALDH has a strict substrate preference for oxidation of all-trans-retinal, with no activity detected against 9-cis-retinal and 13-cis-retinal. BcALDH also has 14 and 30fold lower Km values for all-trans-retinal compared to the small aldehydes acetaldehyde and benzaldehyde, respectively
-
-
-
additional information
?
-
-
in the first acylation step, the activated catalytic Cys, Cys300 in BcALDH, attacks the substrate aldehyde group to form a thio-hemiacetal intermediate. The oxidized NAD(P)+ cofactor takes up a hydride ion from the thio-hemiacetal intermediate, which transforms it to a thioester intermediate. This intermediate is then deacylated by a water molecule, in which the additional catalytic residue Glu, Glu266 in BcALDH, activates the hydrolytic water molecule by abstracting a proton. Finally, the reduced NAD(P)H is released. Plausible mechanism for the minor reducing activity of BcALDH with all-trans-retinal, overview. The beta-ionone ring of the superimposed retinoic acid (REA) is bound at the mouth of the channel and exposed to the solvent. The substrate binding pocket-bound REA shows a bent conformation in the carbon positions from 9 to 11. Molecular docking of retinoic acid into the enzyme structure. BcALDH has a strict substrate preference for oxidation of all-trans-retinal, with no activity detected against 9-cis-retinal and 13-cis-retinal. BcALDH also has 14 and 30fold lower Km values for all-trans-retinal compared to the small aldehydes acetaldehyde and benzaldehyde, respectively
-
-
-
additional information
?
-
no activity with 9-cis-retinal and 13-cis-retinal
-
-
?
additional information
?
-
-
no activity with formaldehyde and benzaldehyde
-
-
?
additional information
?
-
-
no activity with formaldehyde and benzaldehyde
-
-
?
additional information
?
-
-
the membrane bound enzyme may act as barrier when the aldehyde concentration in cytosol is high
-
-
?
additional information
?
-
-
enzyme is induced during growth on tetrahydrofurfuryl alcohol
-
-
?
additional information
?
-
-
enzyme is induced during growth on tetrahydrofurfuryl alcohol
-
-
?
additional information
?
-
-
isoenzyme f1 may be the primary enzyme for oxidizing the acetaldehyde produced during ethanol oxidation in vivo
-
-
?
additional information
?
-
-
enzyme plays a dual role in the absorption of UVR and in the oxidation of peroxidic aldehydes in the mammalian cornea
-
-
?
additional information
?
-
enzyme follows a sequential mode of reaction mechanism
-
-
?
additional information
?
-
ALDH1A1 can also use glutathione (GSH) and dihydrolipoic acid (DHLA) as electron donors to reduce NAD+ to NADH, product identification by thin layer chromatography (TLC)
-
-
-
additional information
?
-
-
iol operon is involved in myo-inositol catabolism
-
-
?
additional information
?
-
-
enzyme prefers aldehyde products of lipid peroxidation as substrates
-
-
?
additional information
?
-
-
dual role for the corneal enzyme in providing the eye with protection against UV-B light: by oxidizing aldehydes generated through light-induced lipid peroxidation and by direct absorption of UV-B light by the enzyme
-
-
?
additional information
?
-
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
ALDHC is preferentially active towards linear medium-chain to long-chain aldehydes as compared to branched-chain, short-chain or aromatic aldehydes. Reorientation of an extended loop (Asn478-Pro490) is responsible for the constricted structure of the substrate tunnel, with the side chain of Asn478 imposing steric restrictions on branched-chain and aromatic aldehydes. A key glycine (Gly104) positioned at the mouth of the tunnel allows for maximum tunnel depth required to bind the linear medium to long aliphatic chain of the native substrate
-
-
?
additional information
?
-
-
the enzyme plays a role in oxidation of a variety of aldehydes generated by lipid metabolism
-
-
?
additional information
?
-
no activity with methanol or ethanol
-
-
?
additional information
?
-
no activity with methanol or ethanol
-
-
?
