Information on EC 1.2.1.99 - 4-(gamma-glutamylamino)butanal dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.99
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RECOMMENDED NAME
GeneOntology No.
4-(gamma-glutamylamino)butanal dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-(gamma-L-glutamylamino)butanal + NAD(P)+ + H2O = 4-(gamma-L-glutamylamino)butanoate + NAD(P)H + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
putrescine degradation II
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Arginine and proline metabolism
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Metabolic 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+).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-furaldehyde + NAD+ + H2O
furan-2-carboxylate + NADH + 2 H+
show the reaction diagram
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22% of the activity with 3-hydroxypropionaldehyde
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?
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
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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
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?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
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
additional information
?
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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-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
P23883
the enzyme is involved in degradation of putrescine
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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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+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mn2+
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1 mM, 15.2% inhibition
NH4Cl
Semicarbazide hydrochloride
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1 mM, 13.3% inhibition
Sodium bisulfite
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1 mM, 98% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
dithiothreitol
Semicarbazide hydrochloride
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1 mM, activity increases by 19%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 0.49
3-hydroxypropionaldehyde
0.12
3-hydroxypropionate
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pH 8.0, 37°C, cofactor: NADH
1
acetaldehyde
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pH 8.0, 37°C, cofactor: NAD+
5.37
benzaldehyde
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pH 8.0, 37°C, cofactor: NAD+
0.26 - 0.97
Butyraldehyde
0.21 - 0.68
Isovaleraldehyde
1.21
propionaldehyde
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pH 8.0, 37°C, cofactor: NAD+
0.14 - 0.24
Valeraldehyde
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.91 - 28.54
3-hydroxypropionaldehyde
0.26
3-hydroxypropionate
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pH 8.0, 37°C, cofactor: NADH
11.03
acetaldehyde
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pH 8.0, 37°C, cofactor: NAD+
17.37
benzaldehyde
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pH 8.0, 37°C, cofactor: NAD+
26.95 - 30.34
Butyraldehyde
25.47 - 27.31
Isovaleraldehyde
24.35
propionaldehyde
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pH 8.0, 37°C, cofactor: NAD+
26.24 - 29.61
Valeraldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.92 - 58.57
3-hydroxypropionaldehyde
2.2
3-hydroxypropionate
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pH 8.0, 37°C, cofactor: NADH
11.03
acetaldehyde
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pH 8.0, 37°C, cofactor: NAD+
3.23
benzaldehyde
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pH 8.0, 37°C, cofactor: NAD+
27.79 - 117.2
Butyraldehyde
40.16 - 121.9
Isovaleraldehyde
20.12
propionaldehyde
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pH 8.0, 37°C, cofactor: NAD+
109 - 207.1
Valeraldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.3
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Vmax: 3-hydroxypropionate, pH 8.0, 37°C, cofactor: NADH
1.5
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recombinant KpBC_DELTA_dhaT_DELTA_yqhD strain, pH 8.0, 45°C
2.5
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recombinant KpC_DELTA_dhaT_DELTA_yqhD strain, pH 8.0, 45°C
5.5
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Vmax: 3-hydroxypropionaldehyde, pH 8.0, 37°C, cofactor: NADP+
12.39
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Vmax: acetaldehyde, pH 8.0, 37°C, cofactor: NAD+
19.51
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Vmax: benzaldehyde, pH 8.0, 37°C, cofactor: NAD+
22.25
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Vmax: 3-hydroxypropionaldehyde, pH 8.0, 45°C
27.35
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Vmax: propionaldehyde, pH 8.0, 37°C, cofactor: NAD+
28.61
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Vmax: isovaleraldehyde, pH 8.0, 45°C
29.47
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Vmax: valeraldehyde, pH 8.0, 37°C, cofactor: NAD+
30.07
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Vmax: butyraldehyde, pH 8.0, 37°C, cofactor: NAD+
30.67
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Vmax: isovaleraldehyde, pH 8.0, 37°C, cofactor: NAD+
32.1
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Vmax: 3-hydroxypropionaldehyde, pH 8.0, 37°C, cofactor: NAD+
33.26
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Vmax: valeraldehyde, pH 8.0, 45°C
34.08
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Vmax: butyraldehyde, pH 8.0, 45°C
additional information
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activity varies depending on the type of strain and culture conditions, e.g. aeration conditions and working volume
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
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20°C: about 35% of maximal activity, 50°C: about 65% of maximal activity
20 - 60
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20°C: about 30% of maximal activity, 60°C: about 35% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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PuuC protein in recombinant Klebsiella pneumoniae, SDS–PAGE
53800
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x * 53800, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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becomes unstable at 60°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into Escherichia coli BL21 under the T5 promoter using the pQE-80L vector
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expressed in Escherichia coli
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PuuC of Klebsiella pneumoniae alone or with coenzyme B12-dependent glycerol dehydratase, DhaB overexpressed homologously, and two major oxidoreductases, DhaT and YqhD, disrupted resulting in KpC_DELTA_dhaT_DELTA_yqhD strain and KpBC_DELTA_dhaT_DELTA_yqhD strain, overexpressing the glycerol dehydratase DhaB, too
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis