Information on EC 2.6.1.82 - putrescine aminotransferase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
2.6.1.82
-
RECOMMENDED NAME
GeneOntology No.
putrescine aminotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-aminobutanal = 1-pyrroline + H2O
show the reaction diagram
putrescine + 2-oxoglutarate = 1-pyrroline + L-glutamate + H2O
show the reaction diagram
overall reaction
-
-
-
putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NIL
-
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putrescine degradation IV
-
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spermine and spermidine degradation II
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Arginine and proline metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
butane-1,4-diamine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which is a 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].
CAS REGISTRY NUMBER
COMMENTARY hide
98982-73-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agmatine + 2-oxoglutarate
?
show the reaction diagram
2% activity
-
-
?
alpha-ketobutyric acid + putrescine
L-aspartate + 4-aminobutanal
show the reaction diagram
38% activity
-
-
?
cadaverine + 2-oxoglutarate
L-glutamate + 5-aminopentanal
show the reaction diagram
97% activity
-
-
?
L-ornithine + 2-oxoglutarate
?
show the reaction diagram
2% activity
-
-
?
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
show the reaction diagram
pyruvate + putrescine
L-alanine + 4-aminobutanal
show the reaction diagram
12% activity
-
-
?
spermidine + 2-oxoglutarate
?
show the reaction diagram
32% activity
-
-
?
additional information
?
-
-
only modified PATase is a ClpS-dependent ClpAP substrate
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-
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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
additional information
?
-
-
only modified PATase is a ClpS-dependent ClpAP substrate
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19
2-oxoglutaric acid
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0.0225 - 9.2
putrescine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000001
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wild type, growth with succinate as carbon source and NH3 as nitrogen source
0.000003
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gamma-aminobutyrate+ mutant, growth with gamma-aminobutyrate as carbon source and NH3 as nitrogen source
0.000006
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gamma-aminobutyrate+ mutant, growth with succinate as carbon source and NH3 as nitrogen source
0.000007
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gamma-aminobutyrate+ mutant, growth with gamma-aminobutyrate as carbon and nitrogen source
0.000064
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putrescine+ mutant, growth with putrescine as carbon source and NH3 as nitrogen source
0.000076
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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
11.68
purified enzyme with yield of 81%
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
in 0.1 mM phosphate buffer
9
in Tris-HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
SDS-PAGE, 49600 Da for ORF2 coding protein and 2100 Da for His6-tag leader peptide
100000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 50700, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the N-terminal modification of PATase is generated by a specificity of leucyl/phenylalanyltRNA-protein transferase, in which various combinations of primary destabilising residues (Leu and Phe) are attached to the N-terminal Met. This modification of PATase is essential not only for its recognition by ClpS, but also determines the stability of the protein in vivo
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, PEG 3350, pH 7.5
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, phosphate buffer, pH 7.4, 15% glycerol, until required
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
95% purified by immobilized-metal affinity chromatography
immobilized metal ion affinity chromatography (Ni2+), anion-exchange chromatography, gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli TG1 and BL21 (DE3)
His-tagged protein expressed in Escherichia coli B834 (DE3)
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