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Information on EC 2.6.1.11 - acetylornithine transaminase
for references in articles please use BRENDA:EC2.6.1.11
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EC Tree 2 Transferases
2.6 Transferring nitrogenous groups
2.6.1 Transaminases
2.6.1.11 acetylornithine transaminase
IUBMB Comments
A pyridoxal-phosphate protein. Also acts on L-ornithine and N2-succinyl-L-ornithine.
The enzyme appears in viruses and cellular organisms
- 2.6.1.11
- acoat
- semialdehyde
- pyridoxal
-
transamination
- n-acetylglutamate
-
arginine-inducible
- aerogenes
-
n-succinyl-l,l-diaminopimelate
- gabaculine
- biotechnology
Reaction Schemes
showSynonyms
n-acetylornithine aminotransferase, acetylornithine aminotransferase, acetylornithine delta-transaminase, acetylornithine transaminase, dapatase, n2-acetylornithine 5-aminotransferase, acetylornithine 5-aminotransferase, succinylornithine aminotransferase, tumor prone5, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylornithine 5-aminotransferase
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acetylornithine aminotransferase
acetylornithine delta-transaminase
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-
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acetylornithine transaminase
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ACOAT
aminotransferase, acetylornithine
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-
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AOTA
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argD
DapATase
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EC 2.6.1.69
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formerly
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N-acetylornithine aminotransferase
N-acetylornithine-delta-transaminase
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N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
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N2-acetylornithine 5-aminotransferase
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N2-acetylornithine 5-transaminase
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slr1022
SOAT
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succinyldiaminopimelate transferase
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succinylornithine aminotransferase
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-
-
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additional information
acetylornithine aminotransferase
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ACOAT
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N-acetylornithine aminotransferase
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-
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N-acetylornithine aminotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N2-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-arginine biosynthesis II (acetyl cycle), L-arginine biosynthesis III (via N-acetyl-L-citrulline), L-ornithine biosynthesis I
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9030-40-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-ornithine + 2-oxoglutarate
L-glutamate-gamma-semialdehyde + L-glutamate
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Substrates: -
Products: -
Products: -
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N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
N-succinyl-2-amino-6-oxopimelate + L-glutamate
N2-succinyl-1,6-diaminopimelate + 2-oxoglutarate
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Substrates: -
Products: -
Products: -
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N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
Synechococcus sp. PCC 6803
Substrates: reaction of EC 2.6.1.19
Products: -
Products: -
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4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
Substrates: reaction of EC 2.6.1.19
Products: -
Products: -
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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Substrates: -
Products: -
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N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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Substrates: fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
Products: -
Products: -
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N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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Substrates: fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
Products: -
Products: -
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N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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Substrates: -
Products: -
Products: -
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N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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Substrates: -
Products: -
Products: -
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
Synechococcus sp. PCC 6803
Substrates: -
Products: -
Products: -
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N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
Substrates: -
Products: -
Products: -
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N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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Substrates: arginine degradation, arginine-inducible catabolic enzyme
Products: -
Products: -
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N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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Substrates: arginine degradation, arginine-inducible catabolic enzyme
Products: -
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N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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Substrates: arginine degradation, arginine-inducible catabolic enzyme
Products: -
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N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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Substrates: arginine degradation, arginine-inducible catabolic enzyme
Products: -
Products: -
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N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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Substrates: -
Products: -
Products: -
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N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
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Substrates: i.e. 2-ketoadipate
Products: -
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N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
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Substrates: i.e. 2-ketoadipate
Products: -
Products: -
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N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
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Substrates: i.e. 2-ketoadipate
Products: -
Products: -
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N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinylglutamate semialdehyde + glutamate
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Substrates: -
Products: -
Products: -
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N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinylglutamate semialdehyde + glutamate
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Substrates: -
Products: -
Products: -
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Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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Substrates: -
Products: -
Products: -
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Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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Substrates: -
Products: -
Products: -
r
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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Substrates: -
Products: -
Products: -
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Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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Substrates: -
Products: -
Products: -
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additional information
?
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Substrates: purified enzyme also has activity of EC 2.6.1.13
Products: -
Products: -
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additional information
?
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Substrates: purified enzyme also has activity of EC 2.6.1.13
Products: -
Products: -
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additional information
?
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Substrates: purified enzyme also has activity of EC 2.6.1.13
Products: -
Products: -
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additional information
?
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Synechococcus sp. PCC 6803
Substrates: N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase and GABA aminotransferase (EC 2.6.1.19) activities
Products: -
Products: -
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additional information
?
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Substrates: N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase and GABA aminotransferase (EC 2.6.1.19) activities
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
Synechococcus sp. PCC 6803
Substrates: reaction of EC 2.6.1.19
Products: -
Products: -
?
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
Substrates: reaction of EC 2.6.1.19
Products: -
Products: -
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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Substrates: fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
Products: -
Products: -
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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Substrates: fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
Products: -
Products: -
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
Substrates: -
Products: -
Products: -
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
Synechococcus sp. PCC 6803
Substrates: -
Products: -
Products: -
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
Substrates: -
Products: -
Products: -
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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Substrates: arginine degradation, arginine-inducible catabolic enzyme
Products: -
Products: -
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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Substrates: arginine degradation, arginine-inducible catabolic enzyme
Products: -
Products: -
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
-
Substrates: arginine degradation, arginine-inducible catabolic enzyme
Products: -
Products: -
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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Substrates: arginine degradation, arginine-inducible catabolic enzyme
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-amino-1,3-cyclohexadienylcarboxylic acid
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potent inhibitor
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neoplasms
The Arabidopsis TUMOR PRONE5 Gene Encodes an Acetylornithine Aminotransferase Required for Arginine Biosynthesis and Root Meristem Maintenance in Blue Light.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
N2-Acetyl-L-ornithine
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25Ā°C, pH 9.5
1.1
N2-Acetyl-L-ornithine
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cosubstrate 2-oxoglutarate, arginine inducible and arginine repressible enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.55
N2-Acetyl-L-ornithine
-
25Ā°C, pH 9.5
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.1
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
7.1 - 9.1
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pH 7.1: about 70% of activity maximum, pH 9.1: about 15% of activity maximum
6.5 - 10
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pH 6.5: about 30% of activity maximum, pH 10.0: about 45% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
one arginine-inducible form and one arginine-repressible form
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-
brenda
ornithine delta transaminase activity (EC 2.6.1.13) in Escherichia coli is due to acetylornithine delta transaminase and not to a separate specific ornithine delta transaminase
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
amino acid profiling of various tissues of Citrullus lanatus cv. Charleston Gray during plant development confirms progressive accumulation of citrulline only in the fruit flesh and rind tissues. Citrulline content is positively correlated with precursor (ornithine) and by-product (arginine) amino acids during fruit ripening
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
in the green alga Chlamydomonas reinhardtii, the arg9-1 and arg9-2 mutations result in arginine auxotrophy because of a deficiency in N-acetyl ornithine aminotransferase activity
malfunction
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two null alleles of TUP5 cause a reduced viability of gametes and embryo lethality, possibly caused by insufficient Arg supply from maternal tissue
metabolism
in cyanobacteria 2-oxoglutarate dehydrogenase (2-OGDH) is missing. A bypass route via succinic semialdehyde (SSA), which utilizes 2-oxoglutarate decarboxylase (OgdA) and succinic semialdehyde dehydrogenase (SsaD) to convert 2-oxoglutarate (2-OG) into succinate, is identified, thus completing the TCA cycle in most cyanobacteria. In addition to the glyoxylate shunt that occurs in a few of cyanobacteria, the existence of a third variant of the TCA cycle connects these metabolites. The gamma-aminobutyric acid (GABA) shunt, is considered to be ambiguous because the GABA aminotransferase is missing in many cyanobacteria. N-acetylornithine aminotransferase (ArgD) can function as a GABA aminotransferase and, together with glutamate decarboxylase (GadA), it can complete a functional GABA shunt. Metabolite profiling of seven Synechococcus sp. PCC 7002 mutant strains related to these two routes to succinate proves the functional connectivity
metabolism
Synechococcus sp. PCC 6803
in cyanobacteria 2-oxoglutarate dehydrogenase (2-OGDH) is missing. A bypass route via succinic semialdehyde (SSA), which utilizes 2-oxoglutarate decarboxylase (OgdA) and succinic semialdehyde dehydrogenase (SsaD) to convert 2-oxoglutarate (2-OG) into succinate, is identified, thus completing the TCA cycle in most cyanobacteria. In addition to the glyoxylate shunt that occurs in a few of cyanobacteria, the existence of a third variant of the TCA cycle connects these metabolites. The gamma-aminobutyric acid (GABA) shunt, is considered to be ambiguous because the GABA aminotransferase is missing in many cyanobacteria. N-acetylornithine aminotransferase (ArgD) can function as a GABA aminotransferase and, together with glutamate decarboxylase (GadA), it can complete a functional GABA shunt. Metabolite profiling of seven Synechococcus sp. PCC 7002 mutant strains related to these two routes to succinate proves the functional connectivity
metabolism
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N-acetylornithine aminotransferase (N-AOA) catalyzes a step in ornithine and citrulline biosynthesis. Genetic variation in the partitioning of citrulline and related amino acids in the flesh and rind tissues is confirmed in a sub-set of watermelon cultivars. No correlation is established between morphological fruit traits (size and rind properties) and citrulline content. Expression of N-AOA involved in the production of N-acetylornithine and N-acetylornithine deacetylase (AOD-3) involved in ornithine synthesis coincide with increasing accumulation of citrulline in flesh and rind tissues during fruit development. Downregulation N-acetylornithine-glutamate acetyltransferase (N-AOGA) suggests the subordinate role of the non-cyclic pathway in citrulline synthesis. Eccentricity between citrulline accumulation and expression of carbamoyl phosphate synthases (CPS-1, CPS-2) during fruit development suggests that the localized synthesis of carbamoyl phosphates may not be required for citrulline synthesis. Regulation of the citrulline metabolism, overview
physiological function
-
in Escherichia coli, the enzymes with N-acetylornithine aminotransferase (ACOAT) activity in arginine synthesis are ArgD, AstC, GabT and PuuE. The major anaerobic ACOAT is ArgD. Loss of ArgD derepresses arginine biosynthetic enzymes, and could result in higher levels of pathway intermediates that allows an alternate enzyme to catalyze the ACOAT reaction. An ArgD/AstC double mutant has a slower doubling time than an ArgD mutant in glucose-containing minimal medium without arginine. The ArgD mutant is not polyamine deficient during anaerobic growth, and the growth defects of the argD mutant are more severe anaerobically
physiological function
-
the argD gene encodes a predicted N-acetylornithine aminotransferase enzyme. A mutant having the Tn5 transposon inserted after nucleotide 999 in the argD gene-coding region, is an arginine auxotroph that does not cause fire blight in apple and has reduced virulence in immature pear fruits. Even when mixed with virulent cells and inoculated onto immature apple fruit, the Tn5 mutant still fails to grow. The ArgD protein cannot be considered an Erwinia amylovora virulence factor because the argD(1000)::Tn5 mutant is auxotrophic and has a primary metabolism defect
physiological function
Synechococcus sp. PCC 6803
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase and GABA aminotransferase (EC 2.6.1.19) activities. N-acetylornithine aminotransferase (ArgD) can function as a GABA aminotransferase and, together with glutamate decarboxylase (GadA), it can complete a functional GABA shunt, metabolic profiling of glutamate decarboxylase expression strains
physiological function
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase and GABA aminotransferase (EC 2.6.1.19) activities. N-acetylornithine aminotransferase (ArgD) can function as a GABA aminotransferase and, together with glutamate decarboxylase (GadA, from Synechococcus sp. strain 6803) which is recombinantly expressed in strain Synechococcus sp. 7002, it can complete a functional GABA shunt, metabolic profiling of glutamate decarboxylase expression strains
physiological function
-
the argD gene encodes a predicted N-acetylornithine aminotransferase enzyme. A mutant having the Tn5 transposon inserted after nucleotide 999 in the argD gene-coding region, is an arginine auxotroph that does not cause fire blight in apple and has reduced virulence in immature pear fruits. Even when mixed with virulent cells and inoculated onto immature apple fruit, the Tn5 mutant still fails to grow. The ArgD protein cannot be considered an Erwinia amylovora virulence factor because the argD(1000)::Tn5 mutant is auxotrophic and has a primary metabolism defect
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PDB
SCOP
CATH
UNIPROT
ORGANISM