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Enzyme Nomenclature
Information on EC 2.6.1.11 - acetylornithine transaminase
for references in articles please use BRENDA:EC2.6.1.11
Word Map on EC 2.6.1.11
- 2.6.1.11
- acoat
- semialdehyde
- pyridoxal
-
arginine-inducible
- n-acetylglutamate
-
transamination
- aerogenes
- gabaculine
- syringae
-
n-succinyl-l,l-diaminopimelate
- biotechnology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.6.1.11
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RECOMMENDED NAME
GeneOntology No.
acetylornithine transaminase
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Escherichia coli W; 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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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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a yeast ACOAT mutant is complemented by TUP5; two null alleles of TUP5 cause a reduced viability of gametes and embryo lethality, possibly caused by insufficient Arg supply from maternal tissue
physiological function
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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
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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
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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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-
-
-
?
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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-
-
-
?
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
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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-
-
-
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
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-
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
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-
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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-
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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arginine degradation, arginine-inducible catabolic enzyme
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-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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arginine degradation, arginine-inducible catabolic enzyme
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-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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arginine degradation, arginine-inducible catabolic enzyme
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-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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arginine degradation, arginine-inducible catabolic enzyme
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-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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-
-
-
?
N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
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i.e. 2-ketoadipate
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-
?
N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
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i.e. 2-ketoadipate
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-
?
N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
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i.e. 2-ketoadipate
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?
N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinylglutamate semialdehyde + glutamate
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-
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?
N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinylglutamate semialdehyde + glutamate
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-
-
?
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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-
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Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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-
-
-
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Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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-
r
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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-
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r
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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additional information
?
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purified enzyme also has activity of EC 2.6.1.13
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additional information
?
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purified enzyme also has activity of EC 2.6.1.13
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additional information
?
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purified enzyme also has activity of EC 2.6.1.13
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
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-
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
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fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
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-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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arginine degradation, arginine-inducible catabolic enzyme
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-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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arginine degradation, arginine-inducible catabolic enzyme
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-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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arginine degradation, arginine-inducible catabolic enzyme
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-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
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arginine degradation, arginine-inducible catabolic enzyme
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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a pyridoxal phosphate protein; inactive unless pyridoxal 5-phosphate is supplied; Km: 0.0017 mM
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-amino-1,3-cyclohexadienylcarboxylic acid
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potent inhibitor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
N2-Acetyl-L-ornithine
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25°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
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25°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
37
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
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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
48000
by SDS-PAGE, based on the predicted size of the mature protein
105000
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thin-layer gel filtration, sucrose density gradient centrifugation
119000
119000
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gel filtration, arginine-repressible enzyme; sedimentation equilibrium studies
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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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
dimer
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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
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hanging drop vapour diffusion in the presence of 1 mM 5-amino-1,3-cyclohexadienylcarboxylic acid
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hanging drop vapour diffusion in the presence of 1 mM 5-amino-1,3-cyclohexadienylcarboxylic acid
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
arginine-inducible form, partial purification of arginine-repressible form
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Ni-NTA affinity column chromatography
Ni-NTA affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G424R
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
biotechnology
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the pCR2.1-argD complementation plasmid is stably maintained in the argD(1000)::Tn5 transposon mutant growing in host tissues without any antibiotic selection. The pCR2.1-argD complementation plasmid can be useful for the expression of genes, markers, and reporters in Erwinia amylovora growing in planta, without concern about losing the plasmid over time
biotechnology
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the pCR2.1-argD complementation plasmid is stably maintained in the argD(1000)::Tn5 transposon mutant growing in host tissues without any antibiotic selection. The pCR2.1-argD complementation plasmid can be useful for the expression of genes, markers, and reporters in Erwinia amylovora growing in planta, without concern about losing the plasmid over time
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