Any feedback?
Literature summary for 2.6.1.19 extracted from
- Natural and synthetic variants of the tricarboxylic acid cycle in cyanobacteria introduction of the GABA shunt into Synechococcus sp. PCC 7002 (2016), Front. Microbiol., 7, 1972 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene argD, functional recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain DH5alpha | Synechococcus sp. PCC 7002 |
| gene argD, functional recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain DH5alpha | Synechococcus sp. PCC 6803 |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-aminobutyrate + 2-oxoglutarate | Synechococcus sp. PCC 7002 | - |
succinic semialdehyde + L-glutamate | - |
? |  |
| 4-aminobutyrate + 2-oxoglutarate | Synechococcus sp. PCC 6803 | - |
succinic semialdehyde + L-glutamate | - |
? | |
| N2-acetyl-L-ornithine + 2-oxoglutarate | Synechococcus sp. PCC 7002 | reaction of EC 2.6.1.11 | N-acetyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
| N2-acetyl-L-ornithine + 2-oxoglutarate | Synechococcus sp. PCC 6803 | reaction of EC 2.6.1.19 | N-acetyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Synechococcus sp. PCC 6803 | P73133 | - |
- |
| Synechococcus sp. PCC 7002 | B1XNF8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally His10-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography and ultrafiltration | Synechococcus sp. PCC 7002 |
| recombinant N-terminally His10-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography and ultrafiltration | Synechococcus sp. PCC 6803 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-aminobutyrate + 2-oxoglutarate | - |
Synechococcus sp. PCC 7002 | succinic semialdehyde + L-glutamate | - |
? | |
| 4-aminobutyrate + 2-oxoglutarate | - |
Synechococcus sp. PCC 6803 | succinic semialdehyde + L-glutamate | - |
? | |
| additional information | N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase activities | Synechococcus sp. PCC 7002 | ? | - |
- |
|
| additional information | N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase activities | Synechococcus sp. PCC 6803 | ? | - |
- |
|
| N2-acetyl-L-ornithine + 2-oxoglutarate | reaction of EC 2.6.1.11 | Synechococcus sp. PCC 7002 | N-acetyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
| N2-acetyl-L-ornithine + 2-oxoglutarate | reaction of EC 2.6.1.11 | Synechococcus sp. PCC 6803 | N-acetyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
| N2-acetyl-L-ornithine + 2-oxoglutarate | reaction of EC 2.6.1.19 | Synechococcus sp. PCC 6803 | N-acetyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| argD | - |
Synechococcus sp. PCC 7002 |
| argD | - |
Synechococcus sp. PCC 6803 |
| argD6803 | - |
Synechococcus sp. PCC 6803 |
| argD7002 | - |
Synechococcus sp. PCC 7002 |
| GABA aminotransferase | - |
Synechococcus sp. PCC 7002 |
| GABA aminotransferase | - |
Synechococcus sp. PCC 6803 |
| More | see also EC 2.6.1.11 | Synechococcus sp. PCC 7002 |
| More | see also EC 2.6.1.11 | Synechococcus sp. PCC 6803 |
| slr1022 | - |
Synechococcus sp. PCC 7002 |
| slr1022 | - |
Synechococcus sp. PCC 6803 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Synechococcus sp. PCC 7002 |
| 22 | - |
assay at room temperature | Synechococcus sp. PCC 6803 |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
assay at | Synechococcus sp. PCC 7002 |
| 9 | - |
assay at | Synechococcus sp. PCC 6803 |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Synechococcus sp. PCC 7002 | |
| pyridoxal 5'-phosphate | - |
Synechococcus sp. PCC 6803 | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Synechococcus sp. PCC 7002 |
| 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 | Synechococcus sp. PCC 6803 |
| 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 | Synechococcus sp. PCC 6803 |
| 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 | Synechococcus sp. PCC 7002 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
