Information on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase

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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
-
-
-
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redox reaction
-
-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alanine metabolism
-
-
Arginine and proline metabolism
-
-
beta-Alanine metabolism
-
-
Metabolic pathways
-
-
putrescine degradation I
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putrescine degradation IV
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putrescine degradation V
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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
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-
Manually annotated by BRENDA team
putrescine grown cells
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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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
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-
Manually annotated by BRENDA team
strain Marburg, strictly anaerobic
-
-
Manually annotated by BRENDA team
strain Marburg, strictly anaerobic
-
-
Manually annotated by BRENDA team
Escherichia coli K12 MG1655
strain K12 MG1655
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain M1h, strictly anaerobic
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-
Manually annotated by BRENDA team
strain M1h, strictly anaerobic
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-
Manually annotated by BRENDA team
A.T.C.C. 13430
-
-
Manually annotated by BRENDA team
Wistar-strain
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar-strain
Wistar-strain
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
AMADH participates in carnitine biosynthesis in plants; AMADH participates in carnitine biosynthesis in plants
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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 + NADP+ + H2O
3-aminopropanoate + NADPH
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
4-amino-2-hydroxybutyraldehyde + NAD+ + H2O
4-amino-2-hydroxybutanoate + NADH + 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 + NADP+ + H2O
4-aminobutanoate + NADPH
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 + 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-ureidobutyraldehyde + NAD+
4-ureidobutyrate + NADH + 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 + 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 + 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
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
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
10% activation by 2 mM observed with 0.1 mM capronaldehyde as substrate
additional information
-
no requirement for bivalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Carboxy-2'-hydroxy-5'-sulfoformazylbenzene
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zincon
acetaldehyde
-
strongly inhibits 4-aminobutyraldehyde oxidation
Cationic buffers
-
-
-
iodoacetamide
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-
ion-exchange resins
-
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-
monoiodoacetate
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slowly
N-ethylmaleimide
p-chloromercuribenzoate
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-
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
0.0015 - 0.15
3-aminopropionaldehyde
0.015
4-aminobutanal
-
-
0.002 - 0.83
4-Aminobutyraldehyde
0.007 - 0.26
4-Guanidinobutyraldehyde
0.2
5-Aminovaleraldehyde
-
-
0.054 - 6.9
acetaldehyde
0.285
Betaine aldehyde
-
250 mM phosphate preparation, constant substrate 1 mM NAD+
0.005 - 0.196
Butyraldehyde
0.003
Capronaldehyde
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same value with benzaldehyde, constant substrate 1 mM NAD+
0.018 - 0.0313
DELTA1-pyrroline
0.016
Isobutyraldehyde
-
constant substrate 1 mM NAD+
0.01 - 0.021
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.7
4-Aminobutyraldehyde
Escherichia coli
P77674
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25C
0.3
Butyraldehyde
Escherichia coli
P77674
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25C
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
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4-aminobutyrate positive mutant, succinate used as C-source and NH3 used as N-source
0.062
-
cells grown on L-glutamate
0.064
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cells grown on 4-aminobutyric acid
0.073
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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
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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
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CS101B strain
11.6
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purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
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in the presence of sodium citrate buffer
7.3 - 8.4
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-
8.5 - 9.5
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optimum toward 4-guanidinobutyraldehyde and 5-aminovaleraldehyde
9 - 10
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4-aminobutanal
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
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at pH 4.0 and pH 7.0: about 60% of activity maximum
6.5 - 9
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4-aminobutyraldehyde, at pH 6.5: about 30% of activity maximum, at pH 9.0: about 70% of activity maximum
6.9 - 8.5
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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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
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increase in dehydrogenase capacity from 25C to 75C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
in etiolated seedlings, AMADH activity in extracts from root tips is higher than those determined for stem segments
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
single subunit, SDS-PAGE
55000
-
gel filtration
83000
-
gel filtration
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
?
-
x * 64000
monomer
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1 * 55000, SDS-PAGE
tetramer
trimer
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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
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
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
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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
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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
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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
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using CM-trisacryl, DEAE-Sephacel, 5'-AMP-Sepharose affinity chromatography, and fast protein liquid chromatography on a mono-Q column
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using column chromatography on DEAE-cellulose
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using column chromatography on DEAE-cellulose, DEAE-Toyopearl, Toyopearl HW-55 and Affi-Gel Blue
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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