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Information on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P77674

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IUBMB Comments
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 . 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 and belongs in the aldehyde dehydrogenase superfamily .
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Escherichia coli
UNIPROT: P77674
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
betaine aldehyde dehydrogenase, amadh, aminoaldehyde dehydrogenase, aldh10a8, 4-aminobutyraldehyde dehydrogenase, aldh10a9, gamma-aminobutyraldehyde dehydrogenase, slamadh1, abaldh, 4-aminobutanal dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-aminobutyraldehyde dehydrogenase
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4-aminobutanal dehydrogenase
-
-
-
-
4-aminobutyraldehyde dehydrogenase
-
-
-
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ABAL dehydrogenase
-
-
-
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dehydrogenase, aminobutyraldehyde
-
-
-
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gamma-aminobutyraldehyde dehydroganase
-
-
-
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gamma-aminobutyraldehyde dehydrogenase
gamma-guanidinobutyraldehyde dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH
show the reaction diagram
-
-
-
?
4-aminobutyraldehyde + NADP+ + H2O
4-aminobutanoate + NADPH
show the reaction diagram
-
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + 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
DELTA1-pyrroline + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
-
r
putrescine + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
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 + 2 H+
show the reaction diagram
-
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement for bivalent cations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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competitive inhibitor with respect to NAD+
additional information
-
addition of 4-aminobutyric acid, GABA, to the growth medium hardly affects growth of Corynebacterium glutamicum, since a half-inhibitory concentration of 1.1 M GABA is determined
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041
4-Aminobutyraldehyde
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25°C
0.196
Butyraldehyde
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25°C
0.018 - 0.0313
DELTA1-pyrroline
0.037 - 0.0538
NAD+
0.0225
putrescine
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.7
4-Aminobutyraldehyde
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25°C
0.3
Butyraldehyde
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25°C
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
0.047
-
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
0.073
-
4-aminobutyrate positive mutant, 4-aminobutyrate used as C-source and as N-source
0.12
-
CS101B pyrrolidine negative strain
0.15
-
M20 strain
0.211
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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
0.96
-
CS101A strain
0.975
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CS101B strain
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
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in the presence of sodium citrate buffer
9.5
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assay at
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
75
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increase in dehydrogenase capacity from 25°C to 75°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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as alternative to GABA production by glutamate decarboxylation, another route for the production of GABA via putrescine is established in Corynebacterium glutamicum
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
202000
native protein, gel-filtration
51000
single subunit, SDS-PAGE
195000
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gel filtration
95000
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2 * 95000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 51000
dimer
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2 * 95000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
a putrescine-producing recombinant Corynebacterium glutamicum strain is converted into a 4-aminobutyric acid, GABA, producing strain by heterologous expression of putrescine transaminase (PatA) and gamma-aminobutyraldehyde dehydrogenase (PatD) genes from Escherichia coli. The resultant strain produces 5.3 g/l of GABA. GABA production is improved further by adjusting the concentration of nitrogen in the culture medium, by avoiding the formation of the by-product N-acetylputrescine and by deletion of the genes for GABA catabolism and GABA re-uptake
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 35
-
up to 5 min, stable
35
-
unstable above
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity by ammonium sulfate precipitation, anion-exchange chromatography and hydrophobic interaction 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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene patD, recombinant expression in Corynebacterium glutamicum strain ATCC 13032 with deleted gabTDP operon and cgmA gene
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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the enzyme is useful for GABA production in an engineered strain of Corynebacterium glutamicum produces 5.3 g/l of GABA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shaibe, E.; Metzer, E.; Halpern, Y.S.
Metabolic pathway for the utilization of L-arginine, L-ornithine, agmatine, and putrescine as nitrogen sources in Escherichia coli K-12
J. Bacteriol.
163
933-937
1985
Escherichia coli
Manually annotated by BRENDA team
Jakoby, W.B.
Enzymes of gamma-aminobutyrate metabolism (bacterial)
Methods Enzymol.
5
765-778
1962
Escherichia coli, Pseudomonas fluorescens
-
Manually annotated by BRENDA team
Prieto, M.I.; Martin, J.; Balana-Fouce, R.; Garrido-Pertierra, A.
Properties of gamma-aminobutyraldehyde dehydrogenase from Escherichia coli
Biochimie
69
1161-1168
1987
Escherichia coli
Manually annotated by BRENDA team
Prieto-Santos, M.I.; Martin-Checa, J.; Balane-Fouce, R.; Garrido-Pertierra, A.
A pathway for putrescine catabolism in Escherichia coli
Biochim. Biophys. Acta
880
242-244
1986
Escherichia coli
Manually annotated by BRENDA team
Shaibe, E.; Metzer, E.; Halpern, Y.S.
Control of utilization of L-arginine, L-ornithine, agmatine, and putrescine as nitrogen sources in Escherichia coli K-12
J. Bacteriol.
163
938-942
1985
Escherichia coli
Manually annotated by BRENDA team
Samsonova, N.N.; Smirnov, S.V.; Novikova, A.E.; Ptitsyn, L.R.
Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase
FEBS Lett.
579
4107-4112
2005
Escherichia coli (P77674), Escherichia coli, Escherichia coli K12 MG1655 (P77674)
Manually annotated by BRENDA team
Jorge, J.M.; Leggewie, C.; Wendisch, V.F.
A new metabolic route for the production of gamma-aminobutyric acid by Corynebacterium glutamicum from glucose
Amino Acids
48
2519-2531
2016
Escherichia coli
Manually annotated by BRENDA team