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Literature summary extracted from

  • 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 (2016), Front. Microbiol., 7, 1972 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.11 gene argD, functional recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain DH5alpha Synechococcus sp. PCC 7002
2.6.1.11 gene argD, functional recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain DH5alpha Synechococcus sp. PCC 6803
2.6.1.19 gene argD, functional recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain DH5alpha Synechococcus sp. PCC 7002
2.6.1.19 gene argD, functional recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain DH5alpha Synechococcus sp. PCC 6803

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.11 4-aminobutyrate + 2-oxoglutarate Synechococcus sp. PCC 7002 reaction of EC 2.6.1.19 succinic semialdehyde + L-glutamate
-
 ?
2.6.1.11 4-aminobutyrate + 2-oxoglutarate Synechococcus sp. PCC 6803 reaction of EC 2.6.1.19 succinic semialdehyde + L-glutamate
-
 ?
2.6.1.11 N2-acetyl-L-ornithine + 2-oxoglutarate Synechococcus sp. PCC 7002
-
 N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
 ?
2.6.1.11 N2-acetyl-L-ornithine + 2-oxoglutarate Synechococcus sp. PCC 6803
-
 N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
 ?
2.6.1.19 4-aminobutyrate + 2-oxoglutarate Synechococcus sp. PCC 7002
-
 succinic semialdehyde + L-glutamate
-
 ?
2.6.1.19 4-aminobutyrate + 2-oxoglutarate Synechococcus sp. PCC 6803
-
 succinic semialdehyde + L-glutamate
-
 ?
2.6.1.19 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
-
 ?
2.6.1.19 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

EC Number Organism UniProt Comment Textmining
2.6.1.11 Synechococcus sp. PCC 6803 P73133
-
-
2.6.1.11 Synechococcus sp. PCC 7002 B1XNF8
-
-
2.6.1.19 Synechococcus sp. PCC 6803 P73133
-
-
2.6.1.19 Synechococcus sp. PCC 7002 B1XNF8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.11 recombinant N-terminally His10-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography and ultrafiltration Synechococcus sp. PCC 7002
2.6.1.11 recombinant N-terminally His10-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography and ultrafiltration Synechococcus sp. PCC 6803
2.6.1.19 recombinant N-terminally His10-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinity chromatography and ultrafiltration Synechococcus sp. PCC 7002
2.6.1.19 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.11 4-aminobutyrate + 2-oxoglutarate reaction of EC 2.6.1.19 Synechococcus sp. PCC 7002 succinic semialdehyde + L-glutamate
-
 ?
2.6.1.11 4-aminobutyrate + 2-oxoglutarate reaction of EC 2.6.1.19 Synechococcus sp. PCC 6803 succinic semialdehyde + L-glutamate
-
 ?
2.6.1.11 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 ?
-
-
2.6.1.11 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 ?
-
-
2.6.1.11 N2-acetyl-L-ornithine + 2-oxoglutarate
-
 Synechococcus sp. PCC 7002 N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
 ?
2.6.1.11 N2-acetyl-L-ornithine + 2-oxoglutarate
-
 Synechococcus sp. PCC 6803 N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
 ?
2.6.1.19 4-aminobutyrate + 2-oxoglutarate
-
 Synechococcus sp. PCC 7002 succinic semialdehyde + L-glutamate
-
 ?
2.6.1.19 4-aminobutyrate + 2-oxoglutarate
-
 Synechococcus sp. PCC 6803 succinic semialdehyde + L-glutamate
-
 ?
2.6.1.19 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 ?
-
-
2.6.1.19 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 ?
-
-
2.6.1.19 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
-
 ?
2.6.1.19 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
-
 ?
2.6.1.19 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

EC Number Synonyms Comment Organism
2.6.1.11 argD
-
 Synechococcus sp. PCC 7002
2.6.1.11 argD
-
 Synechococcus sp. PCC 6803
2.6.1.11 argD6803
-
 Synechococcus sp. PCC 6803
2.6.1.11 argD7002
-
 Synechococcus sp. PCC 7002
2.6.1.11 More see also EC 2.6.1.19 Synechococcus sp. PCC 7002
2.6.1.11 More see also EC 2.6.1.19 Synechococcus sp. PCC 6803
2.6.1.11 N-acetylornithine aminotransferase
-
 Synechococcus sp. PCC 7002
2.6.1.11 N-acetylornithine aminotransferase
-
 Synechococcus sp. PCC 6803
2.6.1.11 slr1022
-
 Synechococcus sp. PCC 7002
2.6.1.11 slr1022
-
 Synechococcus sp. PCC 6803
2.6.1.19 argD
-
 Synechococcus sp. PCC 7002
2.6.1.19 argD
-
 Synechococcus sp. PCC 6803
2.6.1.19 argD6803
-
 Synechococcus sp. PCC 6803
2.6.1.19 argD7002
-
 Synechococcus sp. PCC 7002
2.6.1.19 GABA aminotransferase
-
 Synechococcus sp. PCC 7002
2.6.1.19 GABA aminotransferase
-
 Synechococcus sp. PCC 6803
2.6.1.19 More see also EC 2.6.1.11 Synechococcus sp. PCC 7002
2.6.1.19 More see also EC 2.6.1.11 Synechococcus sp. PCC 6803
2.6.1.19 slr1022
-
 Synechococcus sp. PCC 7002
2.6.1.19 slr1022
-
 Synechococcus sp. PCC 6803

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.11 22
-
 assay at room temperature Synechococcus sp. PCC 7002
2.6.1.11 22
-
 assay at room temperature Synechococcus sp. PCC 6803
2.6.1.19 22
-
 assay at room temperature Synechococcus sp. PCC 7002
2.6.1.19 22
-
 assay at room temperature Synechococcus sp. PCC 6803

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.11 9
-
 assay at Synechococcus sp. PCC 7002
2.6.1.11 9
-
 assay at Synechococcus sp. PCC 6803
2.6.1.19 9
-
 assay at Synechococcus sp. PCC 7002
2.6.1.19 9
-
 assay at Synechococcus sp. PCC 6803

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.11 pyridoxal 5'-phosphate
-
 Synechococcus sp. PCC 7002
2.6.1.11 pyridoxal 5'-phosphate
-
 Synechococcus sp. PCC 6803
2.6.1.19 pyridoxal 5'-phosphate
-
 Synechococcus sp. PCC 7002
2.6.1.19 pyridoxal 5'-phosphate
-
 Synechococcus sp. PCC 6803

General Information

EC Number General Information Comment Organism
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 Synechococcus sp. PCC 7002
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 Synechococcus sp. PCC 6803
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 Synechococcus sp. PCC 6803
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 Synechococcus sp. PCC 7002
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 Synechococcus sp. PCC 7002
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 Synechococcus sp. PCC 6803
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 Synechococcus sp. PCC 6803
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 Synechococcus sp. PCC 7002