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4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
L-ornithine + 2-oxoglutarate
?
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 5-semialdehyde + L-glutamate
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
N2-succinyl-L-ornithine + 2-oxoglutarate
N2-succinylglutamate semialdehyde + glutamate
Nalpha-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
additional information
?
-
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
reaction of EC 2.6.1.19
-
-
?
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
reaction of EC 2.6.1.19
-
-
?
L-ornithine + 2-oxoglutarate
?
-
-
-
-
?
L-ornithine + 2-oxoglutarate
?
-
-
-
-
?
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 5-semialdehyde + L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
?
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
?
-
-
not: putrescine
-
-
?
additional information
?
-
-
purified enzyme also has activity of EC 2.6.1.13
-
-
?
additional information
?
-
-
4-aminobutyrate
-
-
?
additional information
?
-
-
purified enzyme also has activity of EC 2.6.1.13
-
-
?
additional information
?
-
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase and GABA aminotransferase (EC 2.6.1.19) activities
-
-
-
additional information
?
-
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase and GABA aminotransferase (EC 2.6.1.19) activities
-
-
-
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4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
N-acetyl-L-glutamic gamma-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate-gamma-semialdehyde + L-glutamate
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
reaction of EC 2.6.1.19
-
-
?
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
reaction of EC 2.6.1.19
-
-
?
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 5-semialdehyde + L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
-
-
?
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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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
-
a yeast ACOAT mutant is complemented by TUP5
malfunction
-
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
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
-
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
arginine synthesis
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
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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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
Zhang, S.; Qian, X.; Chang, S.; Dismukes, G.C.; Bryant, D.A.
Natural and synthetic variants of the tricarboxylic acid cycle in cyanobacteria introduction of the GABA shunt into Synechococcus sp. PCC 7002
Front. Microbiol.
7
1972
2016
Synechococcus sp. PCC 7002 (B1XNF8), Synechococcus sp. PCC 6803 (P73133)
brenda
Joshi, V.; Joshi, M.; Silwal, D.; Noonan, K.; Rodriguez, S.; Penalosa, A.
Systematized biosynthesis and catabolism regulate citrulline accumulation in watermelon
Phytochemistry
162
129-140
2019
Citrullus lanatus
brenda