Information on EC 2.6.1.82 - putrescine aminotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.82
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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
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-
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putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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Metabolic pathways
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NIL
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putrescine degradation IV
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spermine and spermidine degradation II
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
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
alpha-ketobutyric acid + putrescine
L-aspartate + 4-aminobutanal
show the reaction diagram
cadaverine + 2-oxoglutarate
L-glutamate + 5-aminopentanal
show the reaction diagram
L-ornithine + 2-oxoglutarate
?
show the reaction diagram
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
show the reaction diagram
pyruvate + putrescine
L-alanine + 4-aminobutanal
show the reaction diagram
12% activity
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-
?
spermidine + 2-oxoglutarate
?
show the reaction diagram
32% activity
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-
?
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
additional information
?
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-
only modified PATase is a ClpS-dependent ClpAP substrate
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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
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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
50700
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2 * 50700, gel filtration
52000
SDS-PAGE, 49600 Da for ORF2 coding protein and 2100 Da for His6-tag leader peptide
100000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 50700, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
crystal structures of YgjG at 2.3 and 2.1 A resolutions for the free and putrescine-bound enzymes, respectively. YgjG forms a dimer that adopts a class III pyridoxal 5'-phosphate-dependent aminotransferase fold. Structures of YgjG and other class III aminotransferases are similar. YgjG has an additional N-terminal helical structure that partially contributes to a dimeric interaction with the other subunit via a helix-helix interaction. The YgjG substrate-binding site entrance size and charge distribution are smaller and more hydrophobic than other class III aminotransferases
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hanging-drop vapour-diffusion method, PEG 3350, pH 7.5
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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
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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (806 entries)
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