EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.11 | gene TK1814, phylogenetic analysis, recombinant overexpression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL | Thermococcus kodakarensis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.1.11 | additional information | construction of a TK1814 gene disruption strain, phenotype, overview. The TK1814 strain does not show growth for 24 h, suggesting that the ADC and/or GAD activities of TK1814 are essential for growth in this medium. When exogenous beta-alanine, the product of ADC activity, is added to the medium, the growth defects are almost fully recovered. In contrast, the addition of GABA, the product of GAD activity, does not complement TK1814 disruption at all | Thermococcus kodakarensis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.11 | additional information | - |
additional information | Michaelis-Menten kinetics | Thermococcus kodakarensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.11 | L-aspartate | Thermococcus kodakarensis | - |
beta-alanine + CO2 | - |
? | |
4.1.1.11 | L-aspartate | Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | - |
beta-alanine + CO2 | - |
? | |
4.1.1.11 | additional information | Thermococcus kodakarensis | the enzyme is a glutamate decarboxylase (GAD) homologue encoded by gene TK1814. The recombinant bifunctional TK1814 protein displays not only GAD activity but also ADC activity using pyridoxal 5'-phosphate as a cofactor | ? | - |
? | |
4.1.1.11 | additional information | Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | the enzyme is a glutamate decarboxylase (GAD) homologue encoded by gene TK1814. The recombinant bifunctional TK1814 protein displays not only GAD activity but also ADC activity using pyridoxal 5'-phosphate as a cofactor | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.11 | Thermococcus kodakarensis | Q5JJ82 | i.e. Pyrococcus kodakaraensis | - |
4.1.1.11 | Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | Q5JJ82 | i.e. Pyrococcus kodakaraensis | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.1.1.11 | additional information | anaerobic cultivation at 85°C in a nutrient-rich medium | Thermococcus kodakarensis | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.11 | L-aspartate | - |
Thermococcus kodakarensis | beta-alanine + CO2 | - |
? | |
4.1.1.11 | L-aspartate | - |
Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | beta-alanine + CO2 | - |
? | |
4.1.1.11 | additional information | the enzyme is a glutamate decarboxylase (GAD) homologue encoded by gene TK1814. The recombinant bifunctional TK1814 protein displays not only GAD activity but also ADC activity using pyridoxal 5'-phosphate as a cofactor | Thermococcus kodakarensis | ? | - |
? | |
4.1.1.11 | additional information | the kcat/Km value with Asp is much higher than that with Glu, suggesting that Asp is the preferred substrate of the TK1814 protein | Thermococcus kodakarensis | ? | - |
? | |
4.1.1.11 | additional information | the enzyme is a glutamate decarboxylase (GAD) homologue encoded by gene TK1814. The recombinant bifunctional TK1814 protein displays not only GAD activity but also ADC activity using pyridoxal 5'-phosphate as a cofactor | Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | ? | - |
? | |
4.1.1.11 | additional information | the kcat/Km value with Asp is much higher than that with Glu, suggesting that Asp is the preferred substrate of the TK1814 protein | Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.11 | dimer | recombinant GAD | Thermococcus kodakarensis |
4.1.1.11 | More | the Escherichia coli aspartate decarboxylase, ADC, is hexameric | Thermococcus kodakarensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.11 | ADC | - |
Thermococcus kodakarensis |
4.1.1.11 | aspartate decarboxylase | - |
Thermococcus kodakarensis |
4.1.1.11 | MfnA | - |
Thermococcus kodakarensis |
4.1.1.11 | TK1814 | - |
Thermococcus kodakarensis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.11 | 85 | - |
assay at | Thermococcus kodakarensis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.11 | 8 | - |
assay at | Thermococcus kodakarensis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.11 | pyridoxal 5'-phosphate | dependent on | Thermococcus kodakarensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.1.1.11 | evolution | TK1814 homologues are distributed in a wide range of archaea and may be responsible for beta-alanine biosynthesis in these organisms. The GAD-type proteins from bacteria and those from plants, fungi, and yeast are actually GADs, as diverse members of this clade have been experimentally shown to display GAD activity. The six members of GAD-type proteins from mammals and acari (an arachnid subclass) are proven to be authentic GADs, but GADL1 from mammals and GAD-type proteins from insects within this clade have been shown to be ADCs and do not harbor the corresponding Asn residues that are important for recognition of gamma-carboxylate of Glu in human GAD65 (Asn203 in human GAD65). The ADC-type proteins from bacteria can be expected to function as ADCs, but none of the ADC-type proteins from hyperthermophilic bacteria (from Aquifex aeolicus) or from archaea have been examined | Thermococcus kodakarensis |
4.1.1.11 | malfunction | gene disruption of TK1814 results in a strain that cannot grow in standard medium. Addition of beta-alanine, 4'-phosphopantothenate, or CoA complements the growth defect, whereas gamma-aminobutyrate (GABA) cannot complement | Thermococcus kodakarensis |
4.1.1.11 | physiological function | the enzyme is a a glutamate decarboxylase (GAD) homologue encoded by gene TK1814. The recombinant bifunctional TK1814 protein displays not only GAD activity but also ADC activity using pyridoxal 5'-phosphate as a cofactor. The GAD activity of TK1814 is not necessary for growth | Thermococcus kodakarensis |