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Information on EC 1.2.1.99 - 4-(gamma-glutamylamino)butanal dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P23883

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IUBMB Comments
The enzyme, characterized from the bacterium Escherichia coli, is involved in a putrescine catabolic pathway. It has a broad substrate range, and can also catalyse the activities of EC 1.2.1.19, aminobutyraldehyde dehydrogenase, and EC 1.2.1.24, succinate-semialdehyde dehydrogenase (NAD+).
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This record set is specific for:
Escherichia coli
UNIPROT: P23883
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
ALDH, gamma-Glu-gamma-aminobutyraldehyde dehydrogenase, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase [NAD(P)+], NAD+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase, PuuC, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-Glu-gamma-aminobutyraldehyde dehydrogenase
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gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase [NAD(P)+]
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-
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
4-(gamma-L-glutamylamino)butanal:NAD(P)+ oxidoreductase
The enzyme, characterized from the bacterium Escherichia coli, is involved in a putrescine catabolic pathway. It has a broad substrate range, and can also catalyse the activities of EC 1.2.1.19, aminobutyraldehyde dehydrogenase, and EC 1.2.1.24, succinate-semialdehyde dehydrogenase (NAD+).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
show the reaction diagram
3-hydroxypropionaldehyde + NADP+ + H2O
3-hydroxypropanoate + NADPH + 2 H+
show the reaction diagram
activity is decreased by 73% when NAD+ is replaced with NADP+. The reduction of 3-hydroxypropionate to 3-hydroxypropionaldehyde is not catalyzed with NADPH as cofactor
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-
ir
4-(gamma-L-glutamylamino)butanal + NAD+ + H2O
4-(gamma-L-glutamylamino)butanoate + NADH + H+
show the reaction diagram
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
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-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + 2 H+
show the reaction diagram
-
-
-
?
gamma-glutamyl-gamma-aminobutyraldehyde + NAD+ + H2O
4-(glutamylamino) butanoate + NADH + 2 H+
show the reaction diagram
the enzyme is involved in degradation of putrescine
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-
?
isovaleraldehyde + NAD+ + H2O
3-methylbutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + 2 H+
show the reaction diagram
-
-
-
?
valeraldehyde + NAD+ + H2O
pentanoate + NADH + H+
show the reaction diagram
most preferred substrate
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-
?
additional information
?
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enzyme additionally displays the activity of EC 1.2.1.24, succinate-semialdehyde dehydrogenase (NAD+)
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?
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
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
gamma-glutamyl-gamma-aminobutyraldehyde + NAD+ + H2O
4-(glutamylamino) butanoate + NADH + 2 H+
show the reaction diagram
the enzyme is involved in degradation of putrescine
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
utilizes both NAD+ and NADP+ as cofactors, NAD+ is the preferred cofactor for all substrates except benzaldehyde and 2-furaldehyde. In case of 3-hydroxypropionaldehyde, the activity is decreased by 73% when NAD+ is replaced with NADP+
NADP+
utilizes both NAD+ and NADP+ as cofactors, NAD+ is the preferred cofactor for all substrates except benzaldehyde and 2-furaldehyde. In case of 3-hydroxypropionaldehyde, the activity is decreased by 73% when NAD+ is replaced with NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
1 mM, complete inhibition
Co2+
1 mM, 49.7% inhibition
Cu2+
1 mM, 97.1% inhibition
EDTA
1 mM, 14.7% inhibition
Fe2+
1 mM, 42.5% inhibition
Hg2+
1 mM, complete inhibition
Li+
1 mM, 97% inhibition
Mg2+
1 mM, 19.4% inhibition
Mn2+
1 mM, 15.2% inhibition
NaCl
1 mM, 16.4% inhibition
NH4Cl
1 mM, 21% inhibition
Ni2+
1 mM, 27.6% inhibition
Semicarbazide hydrochloride
1 mM, 13.3% inhibition
Sodium bisulfite
1 mM, 98% inhibition
Zn2+
1 mM, 93% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
1 mM, activity increases by 27%
dithiothreitol
1 mM, activity increases by 75%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 0.49
3-hydroxypropionaldehyde
0.12
3-hydroxypropionate
pH 8.0, 37°C, cofactor: NADH
1
acetaldehyde
pH 8.0, 37°C, cofactor: NAD+
5.37
benzaldehyde
pH 8.0, 37°C, cofactor: NAD+
0.97
Butyraldehyde
pH 8.0, 37°C, cofactor: NAD+
0.68
Isovaleraldehyde
pH 8.0, 37°C, cofactor: NAD+
1.21
propionaldehyde
pH 8.0, 37°C, cofactor: NAD+
0.24
Valeraldehyde
pH 8.0, 37°C, cofactor: NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.91 - 28.54
3-hydroxypropionaldehyde
0.26
3-hydroxypropionate
pH 8.0, 37°C, cofactor: NADH
11.03
acetaldehyde
pH 8.0, 37°C, cofactor: NAD+
17.37
benzaldehyde
pH 8.0, 37°C, cofactor: NAD+
26.95
Butyraldehyde
pH 8.0, 37°C, cofactor: NAD+
27.31
Isovaleraldehyde
pH 8.0, 37°C, cofactor: NAD+
24.35
propionaldehyde
pH 8.0, 37°C, cofactor: NAD+
26.24
Valeraldehyde
pH 8.0, 37°C, cofactor: NAD+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.92 - 58.57
3-hydroxypropionaldehyde
2.2
3-hydroxypropionate
pH 8.0, 37°C, cofactor: NADH
11.03
acetaldehyde
pH 8.0, 37°C, cofactor: NAD+
3.23
benzaldehyde
pH 8.0, 37°C, cofactor: NAD+
27.79
Butyraldehyde
pH 8.0, 37°C, cofactor: NAD+
40.16
Isovaleraldehyde
pH 8.0, 37°C, cofactor: NAD+
20.12
propionaldehyde
pH 8.0, 37°C, cofactor: NAD+
109
Valeraldehyde
pH 8.0, 37°C, cofactor: NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.3
Vmax: 3-hydroxypropionate, pH 8.0, 37°C, cofactor: NADH
12.39
Vmax: acetaldehyde, pH 8.0, 37°C, cofactor: NAD+
19.51
Vmax: benzaldehyde, pH 8.0, 37°C, cofactor: NAD+
27.35
Vmax: propionaldehyde, pH 8.0, 37°C, cofactor: NAD+
29.47
Vmax: valeraldehyde, pH 8.0, 37°C, cofactor: NAD+
30.07
Vmax: butyraldehyde, pH 8.0, 37°C, cofactor: NAD+
30.67
Vmax: isovaleraldehyde, pH 8.0, 37°C, cofactor: NAD+
32.1
Vmax: 3-hydroxypropionaldehyde, pH 8.0, 37°C, cofactor: NAD+
5.5
Vmax: 3-hydroxypropionaldehyde, pH 8.0, 37°C, cofactor: NADP+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
pH 7.0: about 25% of maximal activity, pH 9.0: about 20% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
20°C: about 35% of maximal activity, 50°C: about 65% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
PuuC is a nonspecific aldehyde dehydrogenase that oxidizes all the aldehydes in putrescine catabolism. Strains lacking PuuC activity have a doubling time 50% greater than the wild type with putrescine as the sole nitrogen source. Strains with deletions of putrescine aminotransferase PatA and any of PuuA, PuuB, or PuuC do not grow with putrescine as the nitrogen source
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into Escherichia coli BL21 under the T5 promoter using the pQE-80L vector
the recombinant strain SH254 producing 3-hydroxypropionate from glycerol is developed by cloning of dhaB and aldH genes in Escherichia coli BL21 under different regulatory promoters
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
3-hydroxypropionic acid is an important compound from which several commodity and specialty chemicals can be generated. The recombinant strain SH254 producing 3-hydroxypropionate from glycerol is developed by cloning of dhaB and aldH genes in Escherichia coli BL21 under different regulatory promoters. The recombinant SH254 can accumulate 3-hydroxypropionic acid from glycerol at 6.5 mmol/l in 30 h
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kurihara, S.; Oda, S.; Kato, K.; Kim, H.G.; Koyanagi, T.; Kumagai, H.; Suzuki, H.
A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12
J. Biol. Chem.
280
4602-4608
2005
Escherichia coli (P23883)
Manually annotated by BRENDA team
Jo, J.E.; Mohan Raj, S.; Rathnasingh, C.; Selvakumar, E.; Jung, W.C.; Park, S.
Cloning, expression, and characterization of an aldehyde dehydrogenase from Escherichia coli K-12 that utilizes 3-hydroxypropionaldehyde as a substrate
Appl. Microbiol. Biotechnol.
81
51-60
2008
Escherichia coli (P23883)
Manually annotated by BRENDA team
Raj, S.M.; Rathnasingh, C.; Jo, J.-E.; Park, S.
Production of 3-hydroxypropionic acid from glycerol by a novel recombinant Escherichia coli BL21 strain
Proc. Biochem.
32
1440-1446
2008
Escherichia coli (P23883)
-
Manually annotated by BRENDA team
Schneider, B.L.; Reitzer, L.
Pathway and enzyme redundancy in putrescine catabolism in Escherichia coli
J. Bacteriol.
194
4080-4088
2012
Escherichia coli (P23883)
Manually annotated by BRENDA team