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Information on EC 2.6.1.11 - acetylornithine transaminase
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2.6.1.11 acetylornithine transaminaseIUBMB Comments
A pyridoxal-phosphate protein. Also acts on L-ornithine and N2-succinyl-L-ornithine.
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Word Map
- 2.6.1.11
- acoat
- semialdehyde
- pyridoxal
-
arginine-inducible
-
transamination
- n-acetylglutamate
- gabaculine
-
n-succinyl-l,l-diaminopimelate
- aerogenes
- biotechnology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
n-acetylornithine aminotransferase, acetylornithine aminotransferase, acetylornithine delta-transaminase, acetylornithine transaminase, dapatase, n2-acetylornithine 5-aminotransferase, acetylornithine 5-aminotransferase, succinylornithine aminotransferase, tumor prone5, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylornithine aminotransferase
ACOAT
argD
N-acetylornithine aminotransferase
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
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
-
fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
-
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
-
fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
-
?
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
-
arginine degradation, arginine-inducible catabolic enzyme
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
-
arginine degradation, arginine-inducible catabolic enzyme
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
-
arginine degradation, arginine-inducible catabolic enzyme
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
-
arginine degradation, arginine-inducible catabolic enzyme
-
?
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
-
i.e. 2-ketoadipate
-
?
N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
-
i.e. 2-ketoadipate
-
?
N2-acetyl-L-ornithine + 2-oxohexanedioic acid
N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid
-
i.e. 2-ketoadipate
-
?
N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinylglutamate semialdehyde + glutamate
-
-
-
?
N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinylglutamate semialdehyde + glutamate
-
-
-
?
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
?
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
?
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
r
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
?
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
?
additional information
?
-
-
purified enzyme also has activity of EC 2.6.1.13
-
?
additional information
?
-
-
purified enzyme also has activity of EC 2.6.1.13
-
?
additional information
?
-
-
purified enzyme also has activity of EC 2.6.1.13
-
?
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NATURAL SUBSTRATE
NATURAL 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
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
-
fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
-
-
?
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
-
fourth step in biosynthesis of arginine, arginine-repressible biosynthetic enzyme
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
-
arginine degradation, arginine-inducible catabolic enzyme
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
-
arginine degradation, arginine-inducible catabolic enzyme
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
-
arginine degradation, arginine-inducible catabolic enzyme
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
-
arginine degradation, arginine-inducible catabolic enzyme
-
-
?
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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
-
potent inhibitor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
N2-Acetyl-L-ornithine
-
25°C, pH 9.5
1.1
N2-Acetyl-L-ornithine
-
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
-
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
-
pH 7.1: about 70% of activity maximum, pH 9.1: about 15% of activity maximum
6.5 - 10
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
one arginine-inducible form and one arginine-repressible form
-
-
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
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
-
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
-
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
-
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
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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
105000
-
thin-layer gel filtration, sucrose density gradient centrifugation
119000
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
48000
by SDS-PAGE, based on the predicted size of the mature protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
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
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
-
hanging drop vapour diffusion in the presence of 1 mM 5-amino-1,3-cyclohexadienylcarboxylic acid
-
hanging drop vapour diffusion in the presence of 1 mM 5-amino-1,3-cyclohexadienylcarboxylic acid
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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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
-
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
biotechnology
-
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
-
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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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
brenda
Albrecht, A.M.; Vogel, H.J.
Acetylornithine delta-transaminase. Partial purification and repression behavior
J. Biol. Chem.
239
1872-1876
1964
Escherichia coli
brenda
Billheimer, J.T.; Carnevale, H.N.; Leisinger, T.; Eckardt, T.; Jones, E.E.
Ornithine delta-transaminase activity in Escherichia coli: its identity with acetylornithine delta-transaminase
J. Bacteriol.
127
1315-1323
1976
Escherichia coli
brenda
Billheimer, J.T.; Jones, E.E.
Inducible and repressible acetylornithine delta-transaminase in Escherichia coli: different proteins
Arch. Biochem. Biophys.
161
647-651
1974
Escherichia coli
brenda
Friedrich, B.; Friedrich, C.G.; Magasanik, B.
Catabolic N2-acetylornithine 5-aminotransferase of Klebsiella aerogenes: control of synthesis by induction, catabolite repression, and activation by glutamine synthetase
J. Bacteriol.
133
686-691
1978
Klebsiella aerogenes
brenda
Billheimer, J.T.; Shen, M.Y.; Carnevale, H.N.; Horton, H.R.; Jones, E.E.
Isolation and characterization of acetylornithine delta-transaminase of wild-type Escherichia coli W. Comparison with arginine-inducible acetylornithine delta-transaminase
Arch. Biochem. Biophys.
195
401-413
1979
Escherichia coli
brenda
Vander Wauven, C.; Stalon, V.
Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia
J. Bacteriol.
164
882-886
1985
Burkholderia cepacia
brenda
Rajaram, V.; Prasad, K.; Ratna Prasuna, P.; Ramachandra, N.; Bharath, S.R.; Savithri, H.S.; Murthy, M.R.
Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of the biosynthetic N-acetylornithine aminotransferases from Salmonella typhimurium and Escherichia coli
Acta Crystallogr. Sect. F
62
980-983
2006
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Rajaram, V.; Ratna Prasuna, P.; Savithri, H.S.; Murthy, M.R.
Structure of biosynthetic N-acetylornithine aminotransferase from Salmonella typhimurium: studies on substrate specificity and inhibitor binding
Proteins
70
429-441
2008
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Remacle, C.; Cline, S.; Boutaffala, L.; Gabilly, S.; Larosa, V.; Barbieri, M.R.; Coosemans, N.; Hamel, P.P.
The ARG9 gene encodes the plastid-resident N-acetyl ornithine aminotransferase in the green alga Chlamydomonas reinhardtii
Eukaryot. Cell
8
1460-1463
2009
Chlamydomonas reinhardtii (A8J933)
brenda
Xu, M.; Zhang, X.; Rao, Z.; Yang, J.; Dou, W.; Jin, J.; Xu, Z.
Cloning, expression and characterization of N-acetylornithine aminotransferase from Corynebacterium crenatum and its effects on L-arginine fermentation
Chin. J. Biotechnol.
27
1013-1023
2011
Corynebacterium crenatum
brenda
Fremont, N.; Riefler, M.; Stolz, A.; Schmuelling, T.
The Arabidopsis TUMOR PRONE5 (TUP5) gene encodes an acetylornithine aminotransferase required for arginine biosynthesis and root meristem maintenance in blue light
Plant Physiol.
161
1127-1140
2013
Arabidopsis thaliana
brenda
Ramos, L.S.; Lehman, B.L.; Peter, K.A.; McNellis, T.W.
Mutation of the Erwinia amylovora argD gene causes arginine auxotrophy, nonpathogenicity in apples, and reduced virulence in pears
Appl. Environ. Microbiol.
80
6739-6749
2014
Erwinia amylovora, Erwinia amylovora HKN06P1
brenda
Lal, P.B.; Schneider, B.L.; Vu, K.; Reitzer, L.
The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli
Mol. Microbiol.
94
843-856
2014
Escherichia coli
brenda
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