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Information on EC 2.6.1.82 - putrescine-2-oxoglutarate transaminase
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EC Tree
2.6.1.82 putrescine-2-oxoglutarate transaminaseIUBMB Comments
A pyridoxal 5'-phosphate protein . The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which may be the actual substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates . Forms part of the arginine-catabolism pathway . cf. EC 2.6.1.113, putrescine---pyruvate transaminase.
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Word Map
- 2.6.1.82
- cadaverine
- synthesis
- l-lysine
-
gamma-aminobutyric
- gamma-aminobutyraldehyde
- agmatine
-
transamination
- glutamicum
-
volumetric
-
corynebacterium
- 5-aminovalerate
-
pyrroline
- putida
- adaptor
- aminotransferases
-
synchrotron
- l-arginine
- clpap
-
n-degron
-
catabolite
-
klebsiella
- l-ornithine
- polyamide
- semialdehyde
-
diamines
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
putrescine aminotransferase, putrescine transaminase, patase, kes24511, putrescine:2-oxoglutarate aminotransferase, putrescine-alpha-ketoglutarate transaminase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FG99_07980
KES24511
PATase
Pp-SpuC
putrescine aminotransferase
putrescine transaminase
SpuC
YgjG
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-aminobutanal = 1-pyrroline + H2O
-
-
-
-
putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
overall reaction
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
putrescine:2-oxoglutarate aminotransferase
A pyridoxal 5'-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which may be the actual substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates [3]. Forms part of the arginine-catabolism pathway [2]. cf. EC 2.6.1.113, putrescine---pyruvate transaminase.
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CAS REGISTRY NUMBER
COMMENTARY
98982-73-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1H-indole-2-carbaldehyde + isopropylamine
1-(1H-indol-2-yl)methanamine + acetone + H2O
-
-
-
?
2,3-dimethoxybenzaldehyde + cadaverine
3,5-dimethoxybenzylamine + piperideine + H2O
-
-
-
?
2,3-dimethoxybenzaldehyde + isopropylamine
2,3-dimethoxybenzylamine + acetone + H2O
-
-
-
?
2,4-dimethoxybenzaldehyde + cadaverine
2,4-dimethoxybenzylamine + piperideine + H2O
-
-
-
?
2,4-dimethoxybenzaldehyde + isopropylamine
2,4-dimethoxybenzylamine + acetone + H2O
-
-
-
?
2-(trifluoromethyl)benzaldehyde + cadaverine
2-(trifluoromethyl)benzylamine + piperideine + H2O
-
-
-
?
2-(trifluoromethyl)benzaldehyde + isopropylamine
2-(trifluoromethyl)benzylamine + acetone + H2O
-
-
-
?
2-formylbenzoic acid + cadaverine
2-(aminomethyl)benzoic acid + piperideine + H2O
-
-
-
?
2-formylbenzoic acid + isopropylamine
2-(aminomethyl)benzoic acid + acetone + H2O
-
-
-
?
2-formylbenzonitrile + cadaverine
2-(aminomethyl)benzonitrile + piperideine + H2O
-
-
-
?
2-formylbenzonitrile + isopropylamine
2-(aminomethyl)benzonitrile + acetone + H2O
-
-
-
?
2-methoxybenzaldehyde + cadaverine
2-methoxybenzylamine + piperideine + H2O
-
-
-
?
2-methoxybenzaldehyde + isopropylamine
2-methoxybenzylamine + acetone + H2O
-
-
-
?
2-methoxypyridine-3-carbaldehyde + cadaverine
1-(2-methoxypyridin-3-yl)methanamine + piperideine + H2O
-
-
-
?
2-methoxypyridine-3-carbaldehyde + isopropylamine
1-(2-methoxypyridin-3-yl)methanamine + acetone + H2O
-
-
-
?
2H-1,3-benzodioxole-4-carbaldehyde + cadaverine
1-(2H-1,3-benzodioxol-4-yl)methanamine + piperideine + H2O
-
-
-
?
2H-1,3-benzodioxole-4-carbaldehyde + isopropylamine
1-(2H-1,3-benzodioxol-4-yl)methanamine + acetone + H2O
-
-
-
?
3,4-difluorobenzaldehyde + cadaverine
3,4-difluorobenzylamine + piperideine + H2O
-
-
-
?
3,4-difluorobenzaldehyde + isopropylamine
3,4-difluorobenzylamine + acetone + H2O
-
-
-
?
3,5-dibromobenzaldehyde + cadaverine
3,5-dibromobenzylamine + piperideine + H2O
-
-
-
?
3,5-dibromobenzaldehyde + isopropylamine
3,5-dibromobenzylamine + acetone + H2O
-
-
-
?
3,5-dimethoxybenzaldehyde + isopropylamine
3,5-dimethoxybenzylamine + acetone + H2O
-
-
-
?
3-acetylbenzoic acid + cadaverine
3-(1-aminoethyl)benzoic acid + piperideine + H2O
-
-
-
?
3-acetylbenzoic acid + isopropylamine
3-(1-aminoethyl)benzoic acid + acetone + H2O
-
-
-
?
3-chlorobenzaldehyde + cadaverine
3-chlorobenzylamine + piperideine + H2O
-
-
-
?
3-chlorobenzaldehyde + isopropylamine
3-chlorobenzylamine + acetone + H2O
-
-
-
?
3-fluorobenzaldehyde + cadaverine
3-fluorobenzylamine + piperideine + H2O
-
-
-
?
3-fluorobenzaldehyde + isopropylamine
3-fluorobenzylamine + acetone + H2O
-
-
-
?
3-formylbenzonitrile + cadaverine
3-(aminomethyl)benzonitrile + piperideine + H2O
-
-
-
?
3-formylbenzonitrile + isopropylamine
3-(aminomethyl)benzonitrile + acetone + H2O
-
-
-
?
3-methoxybenzaldehyde + cadaverine
3-methoxybenzylamine + piperideine + H2O
-
-
-
?
3-methoxybenzaldehyde + isopropylamine
3-methoxybenzylamine + acetone + H2O
-
-
-
?
3-nitrobenzaldehyde + cadaverine
3-nitrobenzylamine + piperideine + H2O
-
-
-
?
3-nitrobenzaldehyde + isopropylamine
3-nitrobenzylamine + acetone + H2O
-
-
-
?
4-acetylbenzoic acid + cadaverine
4-(1-aminoethyl)benzoic acid + piperideine + H2O
-
-
-
?
4-acetylbenzoic acid + isopropylamine
4-(1-aminoethyl)benzoic acid + acetone + H2O
-
-
-
?
4-chlorobenzaldehyde + cadaverine
4-chlorobenzylamine + piperideine + H2O
-
-
-
?
4-chlorobenzaldehyde + isopropylamine
4-chlorobenzylamine + acetone + H2O
-
-
-
?
4-fluorobenzaldehyde + cadaverine
4-fluorobenzylamine + piperideine + H2O
-
-
-
?
4-fluorobenzaldehyde + isopropylamine
4-fluorobenzylamine + acetone + H2O
-
-
-
?
4-formylbenzoic acid + cadaverine
4-(aminomethyl)benzoic acid + piperideine + H2O
-
-
-
?
4-formylbenzoic acid + isopropylamine
4-(aminomethyl)benzoic acid + acetone + H2O
-
-
-
?
4-formylbenzonitrile + cadaverine
4-(aminomethyl)benzonitrile + piperideine + H2O
-
-
-
?
4-formylbenzonitrile + isopropylamine
4-(aminomethyl)benzonitrile + acetone + H2O
-
-
-
?
4-nitrobenzaldehyde + cadaverine
4-nitrobenzylamine + piperideine + H2O
-
-
-
?
4-nitrobenzaldehyde + isopropylamine
4-nitrobenzylamine + acetone + H2O
-
-
-
?
5-chlorothiophene-2-carbaldehyde + cadaverine
1-(5-chlorothiophen-2-yl)methanamine + piperideine + H2O
-
-
-
?
5-chlorothiophene-2-carbaldehyde + isopropylamine
1-(5-chlorothiophen-2-yl)methanamine + acetone + H2O
-
-
-
?
5-formylthiophene-2-carboxylic acid + cadaverine
5-(aminomethyl)thiophene-2-carboxylic acid + piperideine + H2O
-
-
-
?
5-formylthiophene-2-carboxylic acid + isopropylamine
5-(aminomethyl)thiophene-2-carboxylic acid + acetone + H2O
-
-
-
?
5-methylfuran-2-carbaldehyde + cadaverine
1-(5-methylfuran-2-yl)methanamine + piperideine + H2O
-
-
-
?
5-methylfuran-2-carbaldehyde + isopropylamine
1-(5-methylfuran-2-yl)methanamine + acetone + H2O
-
-
-
?
6-acetylpyridine-2-carboxylic acid + cadaverine
6-(1-aminoethyl)pyridine-2-carboxylic acid + piperideine + H2O
-
-
-
?
6-acetylpyridine-2-carboxylic acid + isopropylamine
6-(1-aminoethyl)pyridine-2-carboxylic acid + acetone + H2O
-
-
-
?
6-methoxypyridine-3-carbaldehyde + cadaverine
1-(6-methoxypyridin-3-yl)methanamine + piperideine + H2O
-
-
-
?
6-methoxypyridine-3-carbaldehyde + isopropylamine
1-(6-methoxypyridin-3-yl)methanamine + acetone + H2O
-
-
-
?
alpha-ketobutyric acid + putrescine
L-aspartate + 4-aminobutanal
38% activity
-
-
?
cadaverine + 2-oxoglutarate
L-glutamate + 5-aminopentanal
97% activity
-
-
?
cadaverine + 2-oxoglutarate
piperideine + L-glutamate + H2O
-
-
-
?
isopropylamine + 2-oxoglutarate
acetone + L-glutamate + H2O
-
-
-
?
quinoline-3-carbaldehyde + cadaverine
1-(quinolin-3-yl)methanamine + piperideine + H2O
-
-
-
?
quinoline-3-carbaldehyde + isopropylamine
1-(quinolin-3-yl)methanamine + acetone + H2O
-
-
-
?
1H-indole-2-carbaldehyde + cadaverine
1-(1H-indol-2-yl)methanamine + piperideine + H2O
-
-
-
?
1H-indole-2-carbaldehyde + cadaverine
1-(1H-indol-2-yl)methanamine + piperideine + H2O
Pseudomonas putida NBRC 14161
-
-
-
?
3,5-dimethoxybenzaldehyde + cadaverine
3,5-dimethoxybenzylamine + piperideine + H2O
-
-
-
?
3,5-dimethoxybenzaldehyde + cadaverine
3,5-dimethoxybenzylamine + piperideine + H2O
Pseudomonas putida NBRC 14161
-
-
-
?
putrescine + 2-oxoglutarate
1-pyrroline + L-glutamate + H2O
-
-
-
?
putrescine + 2-oxoglutarate
1-pyrroline + L-glutamate + H2O
overall reaction
-
-
?
putrescine + 2-oxoglutarate
1-pyrroline + L-glutamate + H2O
Pseudomonas putida NBRC 14161
overall reaction
-
-
?
putrescine + 2-oxoglutarate
1-pyrroline + L-glutamate + H2O
-
overall reaction
-
-
?
putrescine + 2-oxoglutarate
1-pyrroline + L-glutamate + H2O
-
overall reaction
-
-
?
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
-
coupling action of Escherichia coli YgjG putrescine transaminase and YdcW dehydrogenase
-
-
?
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
putrescine best amino group donor for the enzyme, 100% activity
-
-
?
additional information
?
-
enzyme prefers diaminoalkanes as substrates and thereby generates cyclic imines from the omega-amino aldehyde intermediates
-
-
?
additional information
?
-
-
only modified PATase is a ClpS-dependent ClpAP substrate
-
-
?
additional information
?
-
enzyme prefers diaminoalkanes as substrates and thereby generates cyclic imines from the omega-amino aldehyde intermediates
-
-
?
additional information
?
-
-
enzyme prefers diaminoalkanes as substrates and thereby generates cyclic imines from the omega-amino aldehyde intermediates
-
-
?
additional information
?
-
-
enzyme prefers diaminoalkanes as substrates and thereby generates cyclic imines from the omega-amino aldehyde intermediates
-
-
?
additional information
?
-
the enzyme shows dual substrate recognition for biogenic diamines (i.e. cadaverine) and readily available monoamines (i.e. isopropylamine) for the synthesis of benzylamine derivatives with excellent product conversions and extremely broad substrate tolerance. Biocatalytic synthesis of a range of substituted benzylamines mediated by Pp-SpuC in a coupled assay approach with cadaverine or isopropylamine as co-substrate at 50 mM Tris-HCl, pH 9.0, 30°C, 1 mM PLP, and 1% v/v DMSO, overview
-
-
-
additional information
?
-
-
the enzyme shows dual substrate recognition for biogenic diamines (i.e. cadaverine) and readily available monoamines (i.e. isopropylamine) for the synthesis of benzylamine derivatives with excellent product conversions and extremely broad substrate tolerance. Biocatalytic synthesis of a range of substituted benzylamines mediated by Pp-SpuC in a coupled assay approach with cadaverine or isopropylamine as co-substrate at 50 mM Tris-HCl, pH 9.0, 30°C, 1 mM PLP, and 1% v/v DMSO, overview
-
-
-
additional information
?
-
Pseudomonas putida NBRC 14161
the enzyme shows dual substrate recognition for biogenic diamines (i.e. cadaverine) and readily available monoamines (i.e. isopropylamine) for the synthesis of benzylamine derivatives with excellent product conversions and extremely broad substrate tolerance. Biocatalytic synthesis of a range of substituted benzylamines mediated by Pp-SpuC in a coupled assay approach with cadaverine or isopropylamine as co-substrate at 50 mM Tris-HCl, pH 9.0, 30°C, 1 mM PLP, and 1% v/v DMSO, overview
-
-
-
additional information
?
-
-
the activity of KES24511 is determined using an alanine dehydrogenase enzyme-coupled assay, the purified protein exhibited activity with two substrates, putrescine and 12-aminododecanoic acid, with pyruvate as the co-substrate for transamination. The transaminase reaction co-product (L-alanine) is converted in situ by the dehydrogenase in an NAD+-dependent oxidation, and nicotinamide conversion is spectrophotometrically monitored by the change in UV absorbance at 340 nm
-
-
-
additional information
?
-
-
the activity of KES24511 is determined using an alanine dehydrogenase enzyme-coupled assay, the purified protein exhibited activity with two substrates, putrescine and 12-aminododecanoic acid, with pyruvate as the co-substrate for transamination. The transaminase reaction co-product (L-alanine) is converted in situ by the dehydrogenase in an NAD+-dependent oxidation, and nicotinamide conversion is spectrophotometrically monitored by the change in UV absorbance at 340 nm
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
only modified PATase is a ClpS-dependent ClpAP substrate
-
-
?
putrescine + 2-oxoglutarate
1-pyrroline + L-glutamate + H2O
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
PLP, the the PLP cofactor is typically covalently bound in the active site to a lysine residue in an internal aldimine conformation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000001
-
wild type, growth with succinate as carbon source and NH3 as nitrogen source
0.000003
-
gamma-aminobutyrate+ mutant, growth with gamma-aminobutyrate as carbon source and NH3 as nitrogen source
0.000006
-
gamma-aminobutyrate+ mutant, growth with succinate as carbon source and NH3 as nitrogen source
0.000007
-
gamma-aminobutyrate+ mutant, growth with gamma-aminobutyrate as carbon and nitrogen source
0.000064
-
putrescine+ mutant, growth with putrescine as carbon source and NH3 as nitrogen source
0.000076
-
putrescine+ mutant, growth with putrescine as carbon and nitrogen source
0.047
highest activity in cell extracts grown under nitrogen limitation
2.16
essential level of glutamate formation activity in crude cells of BL21(DE3) harboring pET-Ht-ORF2
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 90
activity range, profile overview. The activity of the enzyme significantly improves as the temperature increased to its suboptimum activity at 50°C, and reaches 100% optimum relative activity at 60°C. At higher temperature, it shows gradual denaturation but maintaining significant residual activity (77%) up to 70°C. Over 50% of maximal activity at 45-75°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
-
a knockout mutation in alternative sigma factor, rpoS, abolishes putrescine-dependent ygjG-lacZ expression. RpoS overexpression induces ygjG-lacZ expression with putrescine supplementation but not without supplementation. The loss of putrescine-dependent ygjG-lacZ expression induced by rpoS is completely restored under nitrogen-starvation conditions. The putrescine-dependent expression of ygjG-lacZ under this condition is clearly dependent on alternative sigma factor, rpoN, and its cognate activator ntrC
additional information
evolution
the enzyme forms a dimer that adopts a class I transaminase fold comparable to other class III transaminases
evolution
Pseudomonas putida NBRC 14161
-
the enzyme forms a dimer that adopts a class I transaminase fold comparable to other class III transaminases
-
metabolism
promiscuous role of Pseudomonas putida Pp-SpuC in metabolism
metabolism
-
the enzyme KES24511 is involved in the amino alkanoate catabolism of the 12-aminododecanoic acid-metabolizing Pseudomonas sp. strain AAC
metabolism
-
the enzyme KES24511 is involved in the amino alkanoate catabolism of the 12-aminododecanoic acid-metabolizing Pseudomonas sp. strain AAC
-
metabolism
Pseudomonas putida NBRC 14161
-
promiscuous role of Pseudomonas putida Pp-SpuC in metabolism
-
additional information
schematic representation of the amino acid residues forming the small and large binding pockets of Pp-SpuC around the external aldimine intermediate (PLP-substrate adduct). The model is based on the multiple sequence alignment analysis and on the active site structure of Vf-omega transaminase (PDB ID 4E3Q)
additional information
-
schematic representation of the amino acid residues forming the small and large binding pockets of Pp-SpuC around the external aldimine intermediate (PLP-substrate adduct). The model is based on the multiple sequence alignment analysis and on the active site structure of Vf-omega transaminase (PDB ID 4E3Q)
additional information
Pseudomonas putida NBRC 14161
-
schematic representation of the amino acid residues forming the small and large binding pockets of Pp-SpuC around the external aldimine intermediate (PLP-substrate adduct). The model is based on the multiple sequence alignment analysis and on the active site structure of Vf-omega transaminase (PDB ID 4E3Q)
-
Show AA Sequence and Transmembrane Helices (2098 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
SDS-PAGE, 49600 Da for ORF2 coding protein and 2100 Da for His6-tag leader peptide
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
the enzyme forms a dimer that adopts a class I transaminase fold comparable to other class III transaminases
dimer
Pseudomonas putida NBRC 14161
-
the enzyme forms a dimer that adopts a class I transaminase fold comparable to other class III transaminases
-