Information on EC 2.6.1.81 - succinylornithine transaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.81
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RECOMMENDED NAME
GeneOntology No.
succinylornithine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N2-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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L-arginine degradation II (AST pathway)
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Metabolic pathways
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arginine metabolism
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SYSTEMATIC NAME
IUBMB Comments
N2-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase
A pyridoxal-phosphate protein. Also acts on N2-acetyl-L-ornithine and L-ornithine, but more slowly [3]. In Pseudomonas aeruginosa, the arginine-inducible succinylornithine transaminase, acetylornithine transaminase (EC 2.6.1.11) and ornithine aminotransferase (EC 2.6.1.13) activities are catalysed by the same enzyme, but this is not the case in all species [5]. This is the third enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase) [3,6].
CAS REGISTRY NUMBER
COMMENTARY hide
99676-37-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NCTC 10743
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Manually annotated by BRENDA team
strain W3110
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Manually annotated by BRENDA team
strain PAO
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Manually annotated by BRENDA team
Pseudomonas formicans
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-
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Manually annotated by BRENDA team
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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
L-ornithine + 2-oxoglutarate
L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
N2-succinyl-L-ornithine + 2-oxoglutarate
N-succinyl-L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinyl-L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
additional information
?
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the bifunctional enzyme is also active with N2-acetyl-L-ornithine performing the reaction of the N2-acetylornithine transaminase, EC 2.6.1.11
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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
N2-succinyl-L-ornithine + 2-oxoglutarate
N-succinyl-L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinyl-L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aminooxoacetic acid
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.391
L-ornithine
pH 8.0, temperature not specified in the publication
0.338
N2-Acetyl-L-ornithine
pH 8.0, temperature not specified in the publication
0.284 - 1.25
N2-succinyl-L-ornithine
additional information
additional information
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specific activity in several aru mutant strains
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5
L-ornithine
Escherichia coli
A0A140N9B6
pH 8.0, temperature not specified in the publication
4.7
N2-Acetyl-L-ornithine
Escherichia coli
A0A140N9B6
pH 8.0, temperature not specified in the publication
3
N2-succinyl-L-ornithine
Escherichia coli
A0A140N9B6
pH 8.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
L-ornithine
Escherichia coli
A0A140N9B6
pH 8.0, temperature not specified in the publication
192
13.9
N2-Acetyl-L-ornithine
Escherichia coli
A0A140N9B6
pH 8.0, temperature not specified in the publication
2570
10.56
N2-succinyl-L-ornithine
Escherichia coli
A0A140N9B6
pH 8.0, temperature not specified in the publication
7255
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.025
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succinate/ammonium-grown cells, cell extract
0.027
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succinate/ammonium-grown cells, cell extract
0.03
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succinate/ammonium-grown cells, cell extract
0.038
Pseudomonas formicans
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glucose/ammonium-grown cells, cell extract
0.056
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glutamate-grown cells, cell extract
0.075
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ornithine-grown cells, induced enzyme, cell extract
0.083
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ornithine-grown cells, induced enzyme, cell extract
0.09
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citrulline-grown cells, induced enzyme, cell extract
0.112
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citrulline-grown cells, induced enzyme, cell extract
0.14
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glutamate-grown cells, cell extract
0.25
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ornithine-grown cells, induced enzyme, cell extract
0.3
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glutamate-grown cells, cell extract
0.33
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arginine-grown cells, induced enzyme, cell extract
0.36
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ornithine-grown cells, induced enzyme, cell extract
0.37
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arginine-grown cells, induced enzyme, cell extract
0.57
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citrulline-grown cells, induced enzyme, cell extract
0.58
Pseudomonas formicans
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ornithine-grown cells, induced enzyme, cell extract
0.69
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arginine-grown cells, induced enzyme, cell extract
0.77
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arginine-grown cells, induced enzyme, cell extract
0.9
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arginine-grown cells, induced enzyme, cell extract
0.97
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ornithine-grown cells, induced enzyme, cell extract
1.06
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arginine-grown cells, induced enzyme, cell extract
1.07
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arginine-grown cells, induced enzyme, cell extract
1.12
Pseudomonas formicans
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arginine-grown cells, induced enzyme, cell extract
1.38
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arginine-grown cells, induced enzyme, cell extract
1.77
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arginine-grown cells, induced enzyme, cell extract
2.33
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arginine-grown cells, induced enzyme, cell extract
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of apo and holo-Ast C and of the enzyme complexed with its physiological substrate, succinylornithine, to 2.2-2.75 A resolution. Docking studies support that AstC has a strong preference for acylated ornithine species over ornithine itself, and suggest that the increase in specificity associated with acylation is caused by steric and desolvation effects rather than specific interactions between the substrate and enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46
enzyme reconstituetd from apo-protein
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from strain W3110, by ammonium sulfate fractionation, ion exchange chromatography, gel filtration, and hydrophobic interaction chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene aruC, i.e. argD, is part of the aru gene cluster, DNA and amino acid sequence determination and analysis of the aru gene cluster, determination of the regulatory gene, expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the holo-enzyme can be reconstituted by the addition of pyridoxal 5'-phosphate to the apo-protein. The reconstituted enzyme is more heat stable than the apo-protein
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