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Information on EC 2.6.1.82 - putrescine-2-oxoglutarate transaminase and Organism(s) Escherichia coli and UniProt Accession P42588
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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
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corynebacterium
- 5-aminovalerate
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pyrroline
- putida
- adaptor
- aminotransferases
-
synchrotron
- l-arginine
- clpap
-
n-degron
-
catabolite
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klebsiella
- l-ornithine
- polyamide
- semialdehyde
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diamines
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY
98982-73-1
-
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
alpha-ketobutyric acid + putrescine
L-aspartate + 4-aminobutanal
38% activity
-
-
?
cadaverine + 2-oxoglutarate
L-glutamate + 5-aminopentanal
97% activity
-
-
?
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
putrescine best amino group donor for the enzyme, 100% activity
-
-
?
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
-
coupling action of Escherichia coli YgjG putrescine transaminase and YdcW dehydrogenase
-
-
?
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
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
SDS-PAGE, 49600 Da for ORF2 coding protein and 2100 Da for His6-tag leader peptide
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
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
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), anion-exchange chromatography, gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
a route for the production of GABA via putrescine in Corynebacterium glutamicum. A putrescine-producing recombinant Corynebacterium glutamicum strain is converted into a GABA producing strain by heterologous expression of putrescine transaminase PatA and gamma-aminobutyraldehyde dehydrogenase PatD genes from Escherichia coli. The resultant strain produces 5.3 g per l of GABA. GABA production is improved further by adjusting the concentration of nitrogen in the culture medium, by avoiding the formation of the by-product N-acetylputrescine and by deletion of the genes for GABA catabolism and GABA re-uptake. GABA accumulation by this strain is increased by 5% to 8.0 g per l, and the volumetric productivity is increased to 0.31 g per l and h
synthesis
enzyme prefers diaminoalkanes as substrates and thereby generates cyclic imines from the omega-amino aldehyde intermediates. The addition of a mild chemical reducing agent rapidly reduces the imine intermediate in situ to furnish a range of N-heterocycle products
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Prieto-Santos, M.I.; Martin-Checa, J.; Balane-Fouce, R.; Garrido-Pertierra, A.
A pathway for putrescine catabolism in Escherichia coli
Biochim. Biophys. Acta
880
242-244
1986
Escherichia coli
Samsonova, N.N.; Smirnov, S.V.; Altman, I.B.; Ptitsyn, L.R.
Molecular cloning and characterization of Escherichia coli K12 ygjG gene
BMC Microbiol.
3
2
2003
Escherichia coli (P42588)
Samsonova, N.N.; Smirnov, S.V.; Novikova, A.E.; Ptitsyn, L.R.
Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase
FEBS Lett.
579
4107-4112
2005
Escherichia coli
Ninnis, R.L.; Spall, S.K.; Talbo, G.H.; Truscott, K.N.; Dougan, D.A.
Modification of PATase by L/F-transferase generates a ClpS-dependent N-end rule substrate in Escherichia coli
EMBO J.
28
1732-1744
2009
Escherichia coli
Yeo, S.J.; Jeong, J.H.; Yu, S.N.; Kim, Y.G.
Crystallization and preliminary X-ray crystallographic analysis of YgjG from Escherichia coli
Acta Crystallogr. Sect. F
68
1070-1072
2012
Escherichia coli (P42588), Escherichia coli
Jorge, J.M.; Leggewie, C.; Wendisch, V.F.
A new metabolic route for the production of gamma-aminobutyric acid by Corynebacterium glutamicum from glucose
Amino Acids
48
2519-253
2016
Escherichia coli (P42588), Escherichia coli
Kim, Y.S.; Shin, H.C.; Lee, J.H.
Two mechanisms for putrescine-dependent transcriptional expression of the putrescine aminotransferase gene, ygjG, in Escherichia coli
Arch. Microbiol.
196
611-618
2014
Escherichia coli
Slabu, I.; Galman, J.; Weise, N.; Lloyd, R.; Turner, N.
Putrescine transaminases for the synthesis of saturated nitrogen heterocycles from polyamines
ChemCatChem
8
1038-1042
2016
Priestia megaterium, Bacillus mycoides (A0A0B5S7N0), Escherichia coli (P42588), Priestia megaterium WSH-002
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