EC Number   |
General Information |
Reference |
|---|
    2.6.1.11 | malfunction |
a yeast ACOAT mutant is complemented by TUP5 |
723477 |
| 2.6.1.11 | 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 |
703512 |
| 2.6.1.11 | malfunction |
two null alleles of TUP5 cause a reduced viability of gametes and embryo lethality, possibly caused by insufficient Arg supply from maternal tissue |
723477 |
| 2.6.1.11 | 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 |
759240 |
| 2.6.1.11 | 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 |
759919 |
| 2.6.1.11 | physiological function |
arginine synthesis |
703512 |
| 2.6.1.11 | 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 |
739103 |
| 2.6.1.11 | 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 |
759240 |
| 2.6.1.11 | 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 |
759240 |
| 2.6.1.11 | 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 |
-, 737502 |
