EC Number   |
General Information |
Reference  |
|---|
    2.6.1.19 | evolution |
transaminases structure comparisons, overview |
-, 758736 |
| 2.6.1.19 | metabolism |
the enzyme takes part in the GABA shunt pathway and GABA uptake/assimilation pathway in Corynebacterium glutamicum |
-, 758736 |
| 2.6.1.19 | more |
active site structure analysis, the epsilon-amino group of Lys288, the catalytic residue of CgGABA-AT, may form an internal aldimine with the aldehydic carbon of PLP, which is required for catalysis |
-, 758736 |
| 2.6.1.19 | evolution |
EctB-type proteins are highly conserved |
-, 759234 |
| 2.6.1.19 | more |
structural homology modeling of (Pl)EctB usimg the crystal structure of the GABA transaminase from Arthrobacter aurescens (PDB ID 4ATP, EC 2.6.1.19) as template |
-, 759234 |
| 2.6.1.19 | 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 |
| 2.6.1.19 | physiological function |
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase 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 |
| 2.6.1.19 | physiological function |
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase 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 |
| 2.6.1.19 | malfunction |
inhibition of GABA aminotransferase (GABA-AT), the enzyme that degrades GABA, is a possible strategy for the treatment of substance abuse. The raised GABA levels that occur as a consequence of the inhibition antagonize the rapid release of dopamine in the ventral striatum (nucleus accumbens) that follows an acute challenge by an addictive substance. In addition, increased GABA levels are also known to elicit an anticonvulsant effect in patients with epilepsy |
759407 |
| 2.6.1.19 | physiological function |
gamma-aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the central nervous system. The enzyme GABA aminotransferase (GABA-AT) degrades GABA |
759407 |
