Information on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase

for references in articles please use BRENDA:EC1.2.1.19
Word Map on EC 1.2.1.19
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.2.1.19
-
RECOMMENDED NAME
GeneOntology No.
aminobutyraldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
putrescine degradation I
-
-
putrescine degradation IV
-
-
putrescine degradation V
-
-
alanine metabolism
-
-
Arginine and proline metabolism
-
-
beta-Alanine metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
4-aminobutanal:NAD+ 1-oxidoreductase
The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates [9]. The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54 gamma-guanidinobutyraldehyde dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme forms part of the arginine-catabolism pathway [8] and belongs in the aldehyde dehydrogenase superfamily [9].
CAS REGISTRY NUMBER
COMMENTARY hide
9028-98-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSM 1030, strictly anaerobic
-
-
Manually annotated by BRENDA team
putrescine grown cells
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
2 general aldehyde oxidases: A and B, both oxidize a range of aldehyde substrates, enzyme B is probably more specifically involved in putrescine degradation
-
-
Manually annotated by BRENDA team
strictly anaerobic
-
-
Manually annotated by BRENDA team
strictly anaerobic
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strictly anaerobic
-
-
Manually annotated by BRENDA team
strictly anaerobic
-
-
Manually annotated by BRENDA team
A.T.C.C. 13430
-
-
Manually annotated by BRENDA team
Wistar-strain
-
-
Manually annotated by BRENDA team
Wistar-strain
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
root growth of single loss-of-function mutants is more sensitive to salinity than wild-type plants, and this is accompanied by reduced GABA accumulation; root growth of single loss-of-function mutants is more sensitive to salinity than wild-type plants, and this is accompanied by reduced GABA accumulation
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,2-dimethyl-3-propionylaminopropanal + NAD+ + H2O
2,2-dimethyl-3-propionylaminopropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
2,2-dimethyl-4-aminobutanal + NAD+ + H2O
2,2-dimethyl-4-aminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
2,2-dimethyl-4-propionylaminobutanal + NAD+ + H2O
2,2-dimethyl-4-propionylaminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
2-methyl-3-butyrylaminopropanal + NAD+ + H2O
2-methyl-3-butyrylaminopropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
2-methyl-3-propionylaminopropanal + NAD+ + H2O
2-methyl-3-propionylaminopropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
2-methyl-4-aminobutanal + NAD+ + H2O
2-methyl-4-aminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
2-methyl-4-propionylaminobutanal + NAD+ + H2O
2-methyl-4-propionylaminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
3-acetaminopropanal + NAD+ + H2O
3-acetaminopropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
3-adipylaminopropanal + NAD+ + H2O
3-adipylaminopropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
3-aminobutanal + NAD+ + H2O
3-aminobutanoate + NADH + 2 H+
show the reaction diagram
best substrate
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
show the reaction diagram
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
show the reaction diagram
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH
show the reaction diagram
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH + H+
show the reaction diagram
100% activity
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + 2 H+
show the reaction diagram
best substrate
-
-
?
3-aminopropionaldehyde + NADP+ + H2O
3-aminopropanoate + NADPH
show the reaction diagram
-
-
-
-
?
3-butyrylaminopropanal + NAD+ + H2O
3-butyrylaminpropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
3-cyanopropionaldehyde + NAD+ + H2O
3-cyanopropanoate + NADH + H+
show the reaction diagram
3-guanidinopropionaldehyde + NAD+ + H2O
3-guanidinopropanoate + NADH + H+
show the reaction diagram
3-methyl-3-butyrylaminopropanal + NAD+ + H2O
3-methyl-3-butyrylaminopropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
3-methyl-4-aminobutanal + NAD+ + H2O
3-methyl-4-aminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
3-propionylaminopropanal + NAD+ + H2O
3-propionylaminopropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
3-pyridine carboxaldehyde + NAD+ + H2O
3-pyridine carboxylic acid + NADH + 2 H+
show the reaction diagram
-
-
-
?
3-valerylaminopropanal + NAD+ + H2O
3-valerylaminopropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
3aminopropanal+ NAD+ + H2O
3-aminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
4-acetaminobutanal + NAD+ + H2O
4-acetaminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
4-amino-2-hydroxybutyraldehyde + NAD+ + H2O
4-amino-2-hydroxybutanoate + NADH + H+
show the reaction diagram
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
show the reaction diagram
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH
show the reaction diagram
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + 2 H+
show the reaction diagram
-
-
-
?
4-aminobutyraldehyde + NADP+ + H2O
4-aminobutanoate + NADPH
show the reaction diagram
4-butyrylaminobutanal + NAD+ + H2O
4-butyrylaminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
4-guanidino-2-hydroxybutyraldehyde + NAD+ + H2O
4-guanidino-2-hydroxybutanoate + NADH + H+
show the reaction diagram
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH
show the reaction diagram
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH + 2 H+
show the reaction diagram
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH + H+
show the reaction diagram
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
show the reaction diagram
4-guanidinobutyraldehyde + NADP+ + H2O
4-guanidinobutanoate + NADPH
show the reaction diagram
-
-
-
-
?
4-propionylaminobutanal + NAD+ + H2O
4-propionylaminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
4-pyridine carboxaldehyde + NAD+ + H2O
4-pyridine carboxylic acid + NADH + 2 H+
show the reaction diagram
-
-
-
?
4-ureidobutyraldehyde + NAD+
4-ureidobutyrate + NADH + H+
show the reaction diagram
-
-
-
?
4-valerylaminobutanal + NAD+ + H2O
4-valerylaminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
5-aminovaleraldehyde + NAD+ + H2O
5-aminovalerate + NADH + H+
show the reaction diagram
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
aminoacetaldehyde + NAD+ + H2O
aminoacetate + NADH
show the reaction diagram
-
12% of activity with 3-aminopropionaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + 2 H+
show the reaction diagram
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
show the reaction diagram
capronaldehyde + NAD+ + H2O
capronate + NADH + H+
show the reaction diagram
isobutyraldehyde + NAD+ + H2O
isobutyrate + NADH + H+
show the reaction diagram
-
-
-
?
N,N,N-trimethyl-3-aminopropionaldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
show the reaction diagram
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+
show the reaction diagram
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + H+
show the reaction diagram
N,N-dimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N-dimethyl-4-aminobutanoate + NADH + H+
show the reaction diagram
N-(3-aminopropyl)-4-aminobutyraldehyde + NAD+ + H2O
N-(3-aminopropyl)-4-aminobutanoate + NADH
show the reaction diagram
-
11% of activity with 3-aminopropionaldehyde
-
-
?
N-acetyl-3-aminopropionaldehyde + NAD+ + H2O
N-acetyl-3-aminopropionate + NADH + H+
show the reaction diagram
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
succinate semialdehyde + NAD+
succinate + NADH + H+
show the reaction diagram
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-aminobutanal + NAD+ + H2O
3-aminobutanoate + NADH + 2 H+
show the reaction diagram
Q9S795, Q9STS1
best substrate
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
show the reaction diagram
3aminopropanal+ NAD+ + H2O
3-aminobutanoate + NADH + 2 H+
show the reaction diagram
C0P9J6, C6KEM4, G5DDC2
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
show the reaction diagram
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
no significant effect on the enzyme activity
Mg2+
-
10% activation by 2 mM observed with 0.1 mM capronaldehyde as substrate
Mn2+
no significant effect on the enzyme activity
additional information
-
no requirement for bivalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2-dimethyl-4-propionylaminobutanal
causes substrate inhibition at high concentration
-
2-Carboxy-2'-hydroxy-5'-sulfoformazylbenzene
-
zincon
2-mercaptoethanol
66% inhibition at 1 mM
3-aminopropanal
substrate inhibition; substrate inhibition
3-methyl-3-butyrylaminopropanal
causes substrate inhibition at high concentration
-
3-methyl-4-butyrylaminobutanal
causes substrate inhibition at high concentration
-
3-propionylaminopropanal
causes substrate inhibition at high concentration
-
4-acetamidobutanal
causes substrate inhibition at high concentration
4-aminobutanal
substrate inhibition
4-guanidinobutyraldehyde
substrate inhibition; substrate inhibition
4-propionylaminobutanal
causes substrate inhibition at high concentration
-
acetaldehyde
-
strongly inhibits 4-aminobutyraldehyde oxidation
Ba2+
30% inhibition at 1 mM
Cationic buffers
-
-
-
Cu2+
complete inhibition at 1 mM
EGTA
7.5% inhibition at 1 mM
Hg2+
62% inhibition at 1 mM
iodoacetamide
-
-
ion-exchange resins
-
-
-
L-cysteine
59% inhibition at 1 mM
Mg2+
70% inhibition at 1 mM
monoiodoacetate
-
slowly
N,N,N-trimethyl-4-aminobutyraldehyde
substrate inhibition; substrate inhibition
N-ethylmaleimide
Ni2+
complete inhibition at 1 mM
p-chloromercuribenzoate
-
-
Pb2+
complete inhibition at 1 mM
Zn2+
92% inhibition at 1 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
4-8 mM, full reactivation after inactivation due to overnight dialysis against 50 mM phosphate pH 7
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.266 - 0.477
2,2-dimethyl-3-propionylaminopropanal
-
1.42
2,2-dimethyl-4-aminobutanal
isozyme PsAMADH 1, pH 9.0, 30C
-
0.506
2,2-dimethyl-4-propionylaminobutanal
isozyme PsAMADH 2, pH 9.0, 30C
-
0.366 - 0.638
2-methyl-3-butyrylaminopropanal
-
0.0935 - 0.183
2-methyl-3-propionylaminopropanal
-
0.189 - 0.525
2-methyl-4-propionylaminobutanal
-
0.109 - 0.268
3-acetaminopropanal
0.0392 - 0.431
3-adipylaminopropanal
-
0.00727 - 0.46
3-aminopropanal
0.0015 - 0.15
3-aminopropionaldehyde
0.226 - 0.227
3-butyrylaminopropanal
-
0.13 - 0.531
3-methyl-3-butyrylaminopropanal
-
0.0651 - 2
3-propionylaminopropanal
-
0.316
3-pyridine carboxaldehyde
pH 9.0, 37C
0.12 - 0.271
3-valerylaminopropanal
-
0.242 - 0.516
4-acetaminobutanal
-
0.0144 - 0.278
4-aminobutanal
0.002 - 0.83
4-Aminobutyraldehyde
0.264 - 0.738
4-butyrylaminobutanal
-
0.003 - 0.26
4-guanidinobutyraldehyde
0.0927 - 0.327
4-propionylaminobutanal
-
0.05
4-pyridine carboxaldehyde
pH 9.0, 37C
0.304 - 0.629
4-valerylaminobutanal
-
0.2
5-Aminovaleraldehyde
-
-
0.054 - 6.9
acetaldehyde
0.014 - 2.051
Betaine aldehyde
0.005 - 0.196
Butyraldehyde
0.003
Capronaldehyde
-
same value with benzaldehyde, constant substrate 1 mM NAD+
0.018 - 0.0313
DELTA1-pyrroline
0.016
Isobutyraldehyde
-
constant substrate 1 mM NAD+
0.006 - 0.141
N,N,N-trimethyl-4-aminobutyraldehyde
0.011 - 0.886
NAD+
0.013
propionaldehyde
-
constant substrate 1 mM NAD+
0.0225
putrescine
-
-
0.252 - 5.428
Succinic semialdehyde
0.004 - 0.013
Valeraldehyde
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.41 - 14.4
2,2-dimethyl-3-propionylaminopropanal
-
3.2
2,2-dimethyl-4-aminobutanal
isozyme PsAMADH 1, pH 9.0, 30C
-
5.8
2,2-dimethyl-4-propionylaminobutanal
isozyme PsAMADH 2, pH 9.0, 30C
-
1.2 - 12.1
2-methyl-3-butyrylaminopropanal
-
2.03 - 6.49
2-methyl-3-propionylaminopropanal
-
2.32 - 4.08
2-methyl-4-propionylaminobutanal
-
3.61 - 13.9
3-acetaminopropanal
1.03 - 8.78
3-adipylaminopropanal
-
3.65 - 11.8
3-aminopropanal
2.41 - 8.13
3-butyrylaminopropanal
-
1.22 - 9.54
3-methyl-3-butyrylaminopropanal
-
3.4 - 7.72
3-propionylaminopropanal
-
2.2
3-pyridine carboxaldehyde
pH 9.0, 37C
2.02 - 11
3-valerylaminopropanal
-
2.49 - 2.84
4-acetaminobutanal
-
1.2 - 5.2
4-aminobutanal
7.7
4-Aminobutyraldehyde
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25C
1.39 - 1.6
4-butyrylaminobutanal
-
1.6 - 5
4-guanidinobutyraldehyde
1.63 - 1.65
4-propionylaminobutanal
-
1.4
4-pyridine carboxaldehyde
pH 9.0, 37C
1.05 - 1.93
4-valerylaminobutanal
-
0.07 - 1
Betaine aldehyde
0.3
Butyraldehyde
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25C
2 - 10.8
N,N,N-trimethyl-4-aminobutyraldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20 - 1300
3-aminopropanal
6.9
3-pyridine carboxaldehyde
pH 9.0, 37C
19 - 1030
4-aminobutanal
53 - 520
4-guanidinobutyraldehyde
28
4-pyridine carboxaldehyde
pH 9.0, 37C
0.46 - 45
Betaine aldehyde
14 - 840
N,N,N-trimethyl-4-aminobutyraldehyde
40 - 260
NAD+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.111 - 0.914
3-aminopropanal
0.858
4-aminobutanal
pH 9.0, 37C
0.211 - 0.581
4-guanidinobutyraldehyde
0.09 - 1.56
N,N,N-trimethyl-4-aminobutyraldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.005
-
wild type strain, succinate used as C-source and NH3 used as N-source
0.009
-
cells grown on succinate and NH3
0.01
-
histidine used as N-source
0.015
-
L-glutamate used as growth substrate
0.017
-
4-aminobutyrate used as N-source
0.024
-
putrescine used as N-source
0.029
-
L-arginine used as growth substrate
0.038
-
D-arginine used as growth substrate
0.045
-
4-guanidinobutyrate used as growth substrate
0.047
-
4-aminobutyrate positive mutant, 4-aminobutyrate used as C-source and NH3 used as N-source
0.056
-
4-aminobutyrate positive mutant, succinate used as C-source and NH3 used as N-source
0.062
-
cells grown on L-glutamate
0.064
-
cells grown on 4-aminobutyric acid
0.073
-
4-aminobutyrate positive mutant, 4-aminobutyrate used as C-source and as N-source
0.086
-
2-ketoarginine used as growth substrate
0.092
-
putrescine used as growth substrate
0.12
-
CS101B pyrrolidine negative strain
0.122
-
agmatine used as growth substrate
0.148
-
cells grown on 4-guanidinobutyraldehyde
0.15
-
M20 strain
0.156
-
cells grown on 4-guanidinobutyric acid
0.211
-
putrescine positive mutant, putrescine used as C-source and as N-source
0.24
-
putrescine positive mutant, putrescine used as C-source and NH3 used as N-source
0.33
-
cells grown on L-arginine
0.96
-
CS101A strain
0.975
-
CS101B strain
11.6
-
purified enzyme
13.71
purified native enzyme, substrate 4-aminobutanal, pH 8.0, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
in the presence of sodium citrate buffer
7.3 - 8.4
-
-
8.5 - 9.5
-
optimum toward 4-guanidinobutyraldehyde and 5-aminovaleraldehyde
9
assay at; assay at
9 - 10
-
4-aminobutanal
9.4 - 9.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
AMADH activity increases with a pH ranging from pH 3.0 to pH 8.0, but it decreases drastically when pH continuously rises from pH 8.0 to pH 10.0. At pH 9.0, the activity decreases by 75% compared to pH 8.0
4 - 7
-
at pH 4.0 and pH 7.0: about 60% of activity maximum
6.5 - 11
the enzyme retains approximately 20% of its maximal substrate-limited, 3-aminopropanal-dependent activity at pH 7.5 and is inactive at pH 6.5; the enzyme retains approximately 20% of its maximal substrate-limited, 3-aminopropanal-dependent activity at pH 7.5 and is inactive at pH 6.5
6.5 - 9
-
4-aminobutyraldehyde, at pH 6.5: about 30% of activity maximum, at pH 9.0: about 70% of activity maximum
6.9 - 8.5
-
at pH 6.9: about 30% of activity maximum, at pH 8.5: about 65% of activity maximum
7 - 8.3
-
highly active between
7 - 10
7.5 - 11
activity range, profile overview
7.5 - 11.5
activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature; assay at room temperature
30
assay at; assay at
75
-
increase in dehydrogenase capacity from 25C to 75C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
activity range, profile overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.16
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
germinated
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
AtALDH10A8 is cytosolic, although the N-terminal 140 amino acid sequence of AtALDH10A8 localizes to the plastid and to the leucoplast
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
2 * 52000, SDS-PAGE
55000
-
gel filtration
57000
-
4 * 57000, SDS-PAGE
64000
-
x * 64000
75000
-
3 * 75000, SDS-PAGE
83000
-
gel filtration
95000
-
2 * 95000, SDS-PAGE
112000
-
gel filtration
115000
-
gel filtration
117000
gel filtration
120000
gel filtration
195000
-
gel filtration
202000
native protein, gel-filtration
228000
-
gel filtration, PAGE
240000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 55000, SDS-PAGE
tetramer
trimer
-
3 * 75000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isozyme AMADH1 in complex with NAD+, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 13% (w/v) PEG 6000 and 5% (v/v) 2-methyl-2,4-pentanediol, at 20C; isozyme AMADH2 in complex with NAD+, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 18% (w/v) PEG 4000, 10% (v/v) isopropanol and 0.5% (w/v) n-octyl beta-D-glucopyranoside, at 20C
wild-type SlAMADH1 with 5 mM NAD+is crystallized over a reservoir containing 23% PEG 1000, 0.1 M HEPES, pH 7.5, mutant E260A of SlAMADH1 with 5 mM NAD+ is crystallized over a reservoir containing 15% PEG 1500, 0.1 M imidazole, pH 7.0, and 10% glycerol, sitting drop vapor diffusion method, cryoprotectant solution consits of mother liquor supplemented with 25% PEG 400 for SlAMADH1 or 20% glycerol for the E260A mutant, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model
wild-type ZnAMADH1a with 5 mM NAD+ is crystallized over a reservoir containing 16% PEG 4000, 0.1 M HEPES, pH 7.5, and 10% isopropyl alcohol, sitting drop vapor diffusion method, cryoprotection by 20% glycerol in mother liquor, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
most stable at neutral pH
288069
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20
-
stable over several months
-15
-
retains 70% of activity when stored for 2 weeks
0 - 35
-
up to 5 min, stable
2
-
80% loss of activity after overnight storage
28
-
temperature higher than 28C promotes slow activation
30
-
30 min, pH 5.0-8.0, stable; for 30 min, in 100 mM K-phosphate buffer, pH 7, allmost all activity retained; for 30 min, in 100 mM Na-acetate buffer, pH 5, allmost all activity retained; for 30 min, in 100 mM Na-bicine buffer, pH 8, allmost all activity retained
35
-
unstable above
40
-
64% loss of activity after 10 min
50 - 60
purified enzyme, pH 8.0, rapid inactivation above 50C, loss of almost 50% activity at 60C
70
-
for 5 min, 3% activity recovered; for 5 min, NAD+ present during heating, 16% activity recovered
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol and NAD+, no stabilization
-
2-mercaptoethanol and NAD+, stabilization
-
NAD+ and sulfhydryl compounds are necessary for stabilization
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glycerol
-
stable in 30% with 5 mM mercaptoethanol + 5 mM EDTA
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 25% glycerol, retaines almost full activity, one year
-
-20C, several months
-
2C, overnight, purified enzyme, 20% loss of activity
-
4C, 250 mM phosphate, pH 6.8, in the presence of 4 mM dithiothreitol, activity decreases by 20-30% after 7 days, freezing resultes in complete inactivation
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE Sephacel, hydroxyapatite, 5'-AMP Sepharose 4B, Mono Q, TSK-GEL
-
cobalt- or nickel-charged IDA-Sepharose column chromatography and Resource Q column chromatography; cobalt- or nickel-charged IDA-Sepharose column chromatography and Resource Q column chromatography
from putrescine-grown cells, using ammonium sulfate fractionation and column chromatography on Sephacryl S-300, DEAE-Sephacel and Blue-Sepharose CL6B
-
from putrescine-grown cells, using column chromatography on DEAE-cellulose, DEAE-Sephadex A-50, Sephadex G-200, Hydroxylapatite and Sephadex G-200 in 150 mM NaCl
-
native enzyme 27.22fold from germinated seeds by ammonium sulfate fractionation, desalting gel filtration, and anion exchange chromatography
recombinant His-tagged enzyme from in Escherichia coli by affinity chromatography; recombinant His-tagged enzyme from in Escherichia coli by affinity chromatography
to homogeneity by ammonium sulfate precipitation, anion-exchange chromatography and hydrophobic interaction chromatography
using ammonium sulfate fractionation and column chromatography on DEAE-cellulose, AMP-Sepharose, Sephadex G-200 and NAD+-Sepharose
-
using CM-trisacryl, DEAE-Sephacel, 5'-AMP-Sepharose affinity chromatography, and fast protein liquid chromatography on a mono-Q column
-
using column chromatography on DEAE-cellulose
-
using column chromatography on DEAE-cellulose, DEAE-Toyopearl, Toyopearl HW-55 and Affi-Gel Blue
-
using column chromatography on DEAE-cellulose, hydroxylapatite, Sephacryl S-300 and Phenyl-Superose and isoelectrofocusing
-
using column chromatography on hydroxylapatite, precipitation with ammonium sulfate, column chromatography on Sephacryl S-300, Phenyl-superose, 5'-AMP-Sepharose and hydroxylapatite
-
using protamine, ammonium sulfate, acetone and column chromatography on DEAE-cellulose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons
gene AMADH1, sequence comparisons and phylogenetic analysis, recombinant expression of GFP-tagged isozyme PsAMADH1 in Arabidopsis thaliana Col-0 protoplasts; gene AMADH2, sequence comparisons and phylogenetic analysis, recombinant expression of GFP-tagged isozyme PsAMADH2 in Arabidopsis thaliana Col-0 protoplasts
gene ataldh10A8, recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana protoplast, recombinant expression of His-tagged enzyme in in Escherichia coli; gene ataldh10A9, recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana protoplast, recombinant expression of His-tagged enzyme in in Escherichia coli
gene patD, recombinant expression in Corynebacterium glutamicum strain ATCC 13032 with deleted gabTDP operon and cgmA gene
-
isozyme SlAMADH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; isozyme SlAMADH2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
isozyme ZmAMADH1a, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; isozyme ZmAMADH1b, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; isozyme ZmAMADH2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AtALDH109 gene is expressed constitutively in Arabidopsis thaliana, although it has been reported to be weakly induced by salinity and dehydration; AtALDH10A8 gene is expressed constitutively in Arabidopsis thaliana, although it has been reported to be weakly induced by salinity and dehydration
changes in O2 availability and cellular redox balance due to stress may directly influence the activity of 4-aminobutyraldehyde dehydrogenase, thereby restricting 4-aminobutyrate formation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
the enzyme is useful for GABA production in an engineered strain of Corynebacterium glutamicum produces 5.3 g/l of GABA
additional information
Show AA Sequence (1994 entries)
Please use the Sequence Search for a specific query.