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Literature summary for 2.6.1.11 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 | reaction of EC 2.6.1.19 | succinic semialdehyde + L-glutamate | - |
? |  |
| 4-aminobutyrate + 2-oxoglutarate | Synechococcus sp. PCC 6803 | reaction of EC 2.6.1.19 | succinic semialdehyde + L-glutamate | - |
? | |
| N2-acetyl-L-ornithine + 2-oxoglutarate | Synechococcus sp. PCC 7002 | - |
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
| N2-acetyl-L-ornithine + 2-oxoglutarate | Synechococcus sp. PCC 6803 | - |
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 | reaction of EC 2.6.1.19 | Synechococcus sp. PCC 7002 | succinic semialdehyde + L-glutamate | - |
? | |
| 4-aminobutyrate + 2-oxoglutarate | reaction of EC 2.6.1.19 | Synechococcus sp. PCC 6803 | succinic semialdehyde + L-glutamate | - |
? | |
| additional information | N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase and GABA aminotransferase (EC 2.6.1.19) activities | Synechococcus sp. PCC 7002 | ? | - |
- |
|
| additional information | N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase and GABA aminotransferase (EC 2.6.1.19) activities | Synechococcus sp. PCC 6803 | ? | - |
- |
|
| N2-acetyl-L-ornithine + 2-oxoglutarate | - |
Synechococcus sp. PCC 7002 | N-acetyl-L-glutamate 5-semialdehyde + L-glutamate | - |
? | |
| N2-acetyl-L-ornithine + 2-oxoglutarate | - |
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 |
| More | see also EC 2.6.1.19 | Synechococcus sp. PCC 7002 |
| More | see also EC 2.6.1.19 | Synechococcus sp. PCC 6803 |
| N-acetylornithine aminotransferase | - |
Synechococcus sp. PCC 7002 |
| N-acetylornithine aminotransferase | - |
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 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 | Synechococcus sp. PCC 6803 |
| 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 | Synechococcus sp. PCC 7002 |
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