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Information on EC 2.6.1.11 - acetylornithine transaminase and Organism(s) Pseudomonas aeruginosa

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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.
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This record set is specific for:
Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
n-acetylornithine aminotransferase, acetylornithine aminotransferase, acetylornithine delta-transaminase, acetylornithine transaminase, dapatase, n2-acetylornithine 5-aminotransferase, acetylornithine 5-aminotransferase, succinylornithine aminotransferase, tumor prone5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylornithine 5-aminotransferase
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-
-
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acetylornithine aminotransferase
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-
-
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acetylornithine delta-transaminase
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-
-
-
acetylornithine transaminase
-
-
-
-
ACOAT
-
-
-
-
aminotransferase, acetylornithine
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-
-
-
AOTA
-
-
-
-
DapATase
-
-
-
-
N-acetylornithine aminotransferase
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-
-
-
N-acetylornithine-delta-transaminase
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-
-
-
N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase
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-
-
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N2-acetylornithine 5-aminotransferase
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-
-
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N2-acetylornithine 5-transaminase
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-
-
-
SOAT
-
-
-
-
succinyldiaminopimelate transferase
-
-
-
-
succinylornithine aminotransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-40-4
-
SUBSTRATE
PRODUCT                       
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
-
fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
show the reaction diagram
-
arginine degradation, arginine-inducible catabolic enzyme
-
-
?
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
show the reaction diagram
-
-
-
?
additional information
?
-
-
purified enzyme also has activity of EC 2.6.1.13
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
show the reaction diagram
-
arginine degradation, arginine-inducible catabolic enzyme
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
N2-acetyl-L-ornithine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
-
pH 6.5: about 30% of activity maximum, pH 10.0: about 45% of activity maximum
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G3SI40_PSEAI
406
0
43720
TrEMBL
-
A0A8F9K578_PSEAI
406
0
43747
TrEMBL
-
A0A0A8RND0_PSEAI
406
0
43820
TrEMBL
-
A0A080VLF2_PSEAI
393
0
41973
TrEMBL
-
A0A0C6ELF0_PSEAI
393
0
41943
TrEMBL
-
A0A485HF95_PSEAI
406
0
43691
TrEMBL
-
A0A8G4D2G1_PSEAI
406
0
43762
TrEMBL
-
A0A8G7IDS4_PSEAI
406
0
43718
TrEMBL
-
A0A8G2RBY4_PSEAI
406
0
43740
TrEMBL
-
A0A7M2ZMW7_PSEAI
406
0
43718
TrEMBL
-
A0A8G6NCX4_PSEAI
406
0
43738
TrEMBL
-
A0A8G5BWR4_PSEAI
406
0
43717
TrEMBL
-
A0A8G2X159_PSEAI
406
0
43734
TrEMBL
-
A0A8G2JQ33_PSEAI
406
0
43618
TrEMBL
-
A0A4U9LU92_PSEAI
406
0
43721
TrEMBL
-
A0A8G4NZE6_PSEAI
406
0
43788
TrEMBL
-
A0A0D6IE28_PSEAI
406
0
43748
TrEMBL
-
A0A2R3ILW3_PSEAI
406
0
43777
TrEMBL
-
A0A8G2QLM8_PSEAI
406
0
43776
TrEMBL
-
A0A3S0IX22_PSEAI
406
0
43749
TrEMBL
-
A0A8G2QUG8_PSEAI
406
0
43689
TrEMBL
-
A0A6A9JVL1_PSEAI
406
0
43676
TrEMBL
-
A0A077JU52_PSEAI
406
0
43690
TrEMBL
-
A0A8G5M2F7_PSEAI
406
0
43729
TrEMBL
-
A0A2R3J4I0_PSEAI
398
0
42206
TrEMBL
-
A0A8G2YMV2_PSEAI
406
0
43707
TrEMBL
-
A0A8G2WEJ7_PSEAI
406
0
43703
TrEMBL
-
A0A8G2KIA0_PSEAI
406
0
43718
TrEMBL
-
A0A8G4TJ27_PSEAI
406
0
43762
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
-
thin-layer gel filtration, sucrose density gradient centrifugation
55000
-
2 * 55000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 55000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, partially purified enzyme is stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of EC 2.6.1.11 and 2.6.1.13
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Voellmy, R.; Leisinger, T.
Dual role for N-2-acetylornithine 5-aminotransferase from Pseudomonas aeruginosa in arginine biosynthesis and arginine catabolism
J. Bacteriol.
122
799-809
1975
Pseudomonas aeruginosa
Manually annotated by BRENDA team