Information on EC 2.6.1.11 - acetylornithine transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.6.1.11
-
RECOMMENDED NAME
GeneOntology No.
acetylornithine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N2-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine biosynthesis
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-arginine biosynthesis II (acetyl cycle)
-
-
L-arginine biosynthesis III (via N-acetyl-L-citrulline)
-
-
L-arginine biosynthesis IV (archaebacteria)
-
-
L-ornithine biosynthesis I
-
-
Metabolic pathways
-
-
arginine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
A pyridoxal-phosphate protein. Also acts on L-ornithine and N2-succinyl-L-ornithine.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-40-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NCTC 10743
-
-
Manually annotated by BRENDA team
one arginine-inducible form and one arginine-repressible form
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-ornithine + 2-oxoglutarate
?
show the reaction diagram
L-ornithine + 2-oxoglutarate
L-glutamate-gamma-semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
show the reaction diagram
N-succinyl-2-amino-6-oxopimelate + L-glutamate
N2-succinyl-1,6-diaminopimelate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
show the reaction diagram
N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
show the reaction diagram
N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinylglutamate semialdehyde + glutamate
show the reaction diagram
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
show the reaction diagram
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ni2+
-
stimulates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-amino-1,3-cyclohexadienylcarboxylic acid
L-ornithine
-
-
p-chloromercuribenzoate
-
-
additional information
-
not: EDTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 2.5
2-oxoglutarate
0.64 - 100
L-ornithine
0.037 - 6.3
N2-Acetyl-L-ornithine
1.25
N2-succinyl-L ornithine
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.82
L-ornithine
Salmonella enterica subsp. enterica serovar Typhimurium
-
25C, pH 9.5
1.55
N2-Acetyl-L-ornithine
Salmonella enterica subsp. enterica serovar Typhimurium
-
25C, pH 9.5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
gabaculine
Salmonella enterica subsp. enterica serovar Typhimurium
-
25C, pH 9.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
-
N2-acetyl-L-ornithine
8.5
-
N2-acetyl-L-ornithine
8.6
-
N2-succinyl-L-ornithine
8.7
-
catabolic enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
7 - 9
-
about 35% of activity maximum at pH 7.0 and 9.0
7.1 - 9.1
-
pH 7.1: about 70% of activity maximum, pH 9.1: about 15% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
2 * 27000, SDS-PAGE
31000
-
x * 31000, wild-type and arginine-inducible form are composed of 31000 MW subunits, which are products of 2 different structural genes, high-speed sedimentation equilibrium in 6 M guanidine-HCl, SDS-PAGE
41000
-
calculateed from cDNA
48000
by SDS-PAGE, based on the predicted size of the mature protein
48800
-
deduced from cDNA
55000
-
2 * 55000, SDS-PAGE
59000
-
arginine-inducible catabolic enzyme, gel filtration
61000
-
gel filtration, arginine-inducible enzyme
105000
-
thin-layer gel filtration, sucrose density gradient centrifugation
119000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 31000, wild-type and arginine-inducible form are composed of 31000 MW subunits, which are products of 2 different structural genes, high-speed sedimentation equilibrium in 6 M guanidine-HCl, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion in the presence of 1 mM 5-amino-1,3-cyclohexadienylcarboxylic acid
in unliganded form and in complex with gabaculine or L-gutamate, diffration to 1.9 A resolution. The structure of unliganded enzyme shows significant electron density for pyridoxal 5'-phosphate in subunits A which can be attributed to the ordering of the loop Lak-bm in subunit B
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, partially purified enzyme is stable for at least 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
arginine-inducible form, partial purification of arginine-repressible form
-
copurification of EC 2.6.1.11 and 2.6.1.13
-
Ni-NTA affinity column chromatography
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli and Corynebacterium crenatum
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
light-induced expression
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G424R
-
tup5-1 mutant is Arg deficient and shows a general deregulation of amino acid metabolism. Root growth is restored by supplementation with arginine and its metabolic precursors. Mutants show an unusual blue light-dependent root growth inhibition
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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