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Literature summary for 4.1.1.11 extracted from

  • Tomita, H.; Yokooji, Y.; Ishibashi, T.; Imanaka, T.; Atomi, H.
    An archaeal glutamate decarboxylase homolog functions as an aspartate decarboxylase and is involved in beta-alanine and coenzyme A biosynthesis (2014), J. Bacteriol., 196, 1222-1230 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.11

Cloned(Commentary)

Cloned (Comment) Organism
gene TK1814, phylogenetic analysis, recombinant overexpression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL Thermococcus kodakarensis

Protein Variants

Protein Variants Comment Organism
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Thermococcus kodakarensis
-
 beta-alanine + CO2
-
 ?
L-aspartate Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1
-
 beta-alanine + CO2
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q5JJ82 i.e. Pyrococcus kodakaraensis
-
Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 Q5JJ82 i.e. Pyrococcus kodakaraensis
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information anaerobic cultivation at 85°C in a nutrient-rich medium Thermococcus kodakarensis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
 Thermococcus kodakarensis beta-alanine + CO2
-
 ?
L-aspartate
-
 Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 beta-alanine + CO2
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Subunits

Subunits Comment Organism
dimer recombinant GAD Thermococcus kodakarensis
More the Escherichia coli aspartate decarboxylase, ADC, is hexameric Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
ADC
-
 Thermococcus kodakarensis
aspartate decarboxylase
-
 Thermococcus kodakarensis
MfnA
-
 Thermococcus kodakarensis
TK1814
-
 Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
85
-
 assay at Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Thermococcus kodakarensis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Thermococcus kodakarensis

General Information

General Information Comment Organism
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
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
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