Information on EC 6.3.1.11 - glutamate-putrescine ligase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
6.3.1.11
-
RECOMMENDED NAME
GeneOntology No.
glutamate-putrescine ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + putrescine = ADP + phosphate + gamma-L-glutamylputrescine
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid amide formation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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Metabolic pathways
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putrescine degradation II
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polyamine pathway
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:putrescine ligase (ADP-forming)
Forms part of a novel bacterial putrescine utilization pathway in Escherichia coli.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K-12
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-
Manually annotated by BRENDA team
gene puuA
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + glutamate + putrescine
ADP + phosphate + gamma-L-glutamylputrescine
show the reaction diagram
-
the enzyme is involved in a putrescine utilization pathway
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-
?
ATP + L-glutamate + putrescine
ADP + phosphate + gamma-L-glutamylputrescine
show the reaction diagram
additional information
?
-
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
ATP + glutamate + putrescine
ADP + phosphate + gamma-L-glutamylputrescine
show the reaction diagram
-
the enzyme is involved in a putrescine utilization pathway
-
-
?
ATP + L-glutamate + putrescine
ADP + phosphate + gamma-L-glutamylputrescine
show the reaction diagram
-
the enzyme catalyzes the gamma-glutamylation of putrescine, the first step in a different putrescine utilization pathway involving gamma-glutamylated intermediates, the Puu pathway, in Escherichia coli, overview. The intracellular concentration of putrescine is probably optimized by PuuA transcriptionally and posttranslationally and excess putrescine is converted to a nutrient source by the Puu pathway, regulation, overview
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-
?
additional information
?
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intracellular polyamine profile of various strains relevant to puuA, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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can substitute Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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The transcription of puuA is induced by putrescine, deletion of gene puuR leads to overexpression of puuA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.35
ATP
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pH 8.0 37C, recombinant enzyme
2.07
L-glutamate
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pH 8.0 37C, recombinant enzyme
44.6
putrescine
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pH 8.0 37C, recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.94
putrescine
Escherichia coli K-12
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pH 8.0 37C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12.7
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purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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12 * 53000, recombinant enzyme, SDS-PAGE
630000
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recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
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12 * 53000, recombinant enzyme, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant untagged enzyme by ammonium sulfate fractionation and adsorption chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene puuA, expression analysis, expression of untagged enzyme
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H269N
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site-directed mutagenesis, the mutant shows 3% activity compared to the wild-type enzyme, the mutant also shows increased susceptibility to proteolytic degradation
H269N/R344Q
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site-directed mutagenesis, the mutant shows 0.1% activity compared to the wild-type enzyme, the mutant also shows increased susceptibility to proteolytic degradation
H282N
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site-directed mutagenesis, the mutant shows 9% activity compared to the wild-type enzyme
H282N/R357Q
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site-directed mutagenesis, the mutant shows 0.05% activity compared to the wild-type enzyme
R357Q
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site-directed mutagenesis, the mutant shows 3% activity compared to the wild-type enzyme
additional information
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deletion of the puu gene cluster, puuA deletion mutants cannot grow on minimal medium with putrescine as the sole source of nitrogen, phenotypes, overview
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