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Literature summary extracted from

  • Richter, A.A.; Mais, C.N.; Czech, L.; Geyer, K.; Hoeppner, A.; Smits, S.H.J.; Erb, T.J.; Bange, G.; Bremer, E.
    Biosynthesis of the stress-protectant and chemical chaperon ectoine biochemistry of the transaminase EctB (2019), Front. Microbiol., 10, 2811 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.19 gene ectB, recombinant overexpression of codon-optimized version of (Pl)ectB as N-terminally Strep II-tagged protein from modified plasmid pLC52 in Escherichia coli strain BL21 and TOP10 cells Paenibacillus lautus
2.6.1.76 gene ectB, genetic structure, recombinant overexpression of codon-optimized version of (Pl)ectB as N-terminally Strep II-tagged protein from modified plasmid pLC52 in Escherichia coli strain BL21 and TOP 10 cells Paenibacillus lautus

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.19 K274A site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive Paenibacillus lautus
2.6.1.19 K274H site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein Paenibacillus lautus
2.6.1.19 K274R site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive Paenibacillus lautus
2.6.1.76 K274A site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive Paenibacillus lautus
2.6.1.76 K274H site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein Paenibacillus lautus
2.6.1.76 K274R site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive Paenibacillus lautus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.76 KCl activates slightly at up to 350 mM, inhibits by 50% at 1.5 M Paenibacillus lautus
2.6.1.76 NaCl activates slightly at up to 350 mM, inhibits by 50% at 1.25 M Paenibacillus lautus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.19 additional information
-
 additional information Michaelis-Menten kinetics Paenibacillus lautus
2.6.1.76 additional information
-
 additional information Michaelis-Menten kinetics Paenibacillus lautus
2.6.1.76 0.43
-
 L-2,4-diaminobutanoate pH 7.0, 45°C, recombinant enzyme Paenibacillus lautus
2.6.1.76 9.01
-
 2-oxoglutarate pH 7.0, 45°C, recombinant enzyme Paenibacillus lautus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.6.1.76 KCl activates slightly at up to 350 mM, inhibits by 50% at 1.5 M Paenibacillus lautus
2.6.1.76 NaCl activates slightly at up to 350 mM, inhibits by 50% at 1.25 M Paenibacillus lautus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.19 200000
-
 about, recombinant Strep II-tagged enzyme, gel filtration Paenibacillus lautus
2.6.1.76 200000
-
 about, recombinant Strep II-tagged enzyme, gel filtration Paenibacillus lautus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.19 4-aminobutanoate + 2-oxoglutarate Paenibacillus lautus
-
 succinate semialdehyde + L-glutamate
-
 ?
2.6.1.19 4-aminobutanoate + 2-oxoglutarate Paenibacillus lautus Y412MC10
-
 succinate semialdehyde + L-glutamate
-
 ?
2.6.1.76 L-2,4-diaminobutanoate + 2-oxoglutarate Paenibacillus lautus
-
 L-aspartate 4-semialdehyde + L-glutamate
-
 ?
2.6.1.76 L-2,4-diaminobutanoate + 2-oxoglutarate Paenibacillus lautus Y412MC10
-
 L-aspartate 4-semialdehyde + L-glutamate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.19 Paenibacillus lautus D3EKC0 cf. EC 2.6.1.76; isolated from the effluent of a hot spring in the Yellowstone National Park (United States)
-
2.6.1.19 Paenibacillus lautus Y412MC10 D3EKC0 cf. EC 2.6.1.76; isolated from the effluent of a hot spring in the Yellowstone National Park (United States)
-
2.6.1.76 Paenibacillus lautus D3EKC0 isolated from the effluent of a hot spring in the Yellowstone National Park (United States)
-
2.6.1.76 Paenibacillus lautus Y412MC10 D3EKC0 isolated from the effluent of a hot spring in the Yellowstone National Park (United States)
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.19 recombinant Strep II-tagged enzyme from Escherichia coli by streptavidin-affinity chromatography Paenibacillus lautus
2.6.1.76 recombinant Strep II-tagged enzyme from Escherichia coli by streptavidin-affinity chromatography Paenibacillus lautus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.6.1.19 cell culture growth at temperatures of up to 50°C Paenibacillus lautus
-
2.6.1.76 cell culture growth at temperatures of up to 50°C Paenibacillus lautus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.19 4-aminobutanoate + 2-oxoglutarate
-
 Paenibacillus lautus succinate semialdehyde + L-glutamate
-
 ?
2.6.1.19 4-aminobutanoate + 2-oxoglutarate
-
 Paenibacillus lautus Y412MC10 succinate semialdehyde + L-glutamate
-
 ?
2.6.1.19 additional information (Pl)EctB also preferably catalyzes a EctB-type reaction, EC 2.6.1.76 Paenibacillus lautus ?
-
-
2.6.1.19 additional information (Pl)EctB also preferably catalyzes a EctB-type reaction, EC 2.6.1.76 Paenibacillus lautus Y412MC10 ?
-
-
2.6.1.76 L-2,4-diaminobutanoate + 2-oxoglutarate
-
 Paenibacillus lautus L-aspartate 4-semialdehyde + L-glutamate
-
 ?
2.6.1.76 L-2,4-diaminobutanoate + 2-oxoglutarate preferred enzyme Paenibacillus lautus L-aspartate 4-semialdehyde + L-glutamate
-
 ?
2.6.1.76 L-2,4-diaminobutanoate + 2-oxoglutarate
-
 Paenibacillus lautus Y412MC10 L-aspartate 4-semialdehyde + L-glutamate
-
 ?
2.6.1.76 L-2,4-diaminobutanoate + 2-oxoglutarate preferred enzyme Paenibacillus lautus Y412MC10 L-aspartate 4-semialdehyde + L-glutamate
-
 ?
2.6.1.76 additional information (Pl)EctB also catalyzes a GABA-TA-type reaction, EC 2.6.1.19, but with less activity Paenibacillus lautus ?
-
-
2.6.1.76 additional information (Pl)EctB also catalyzes a GABA-TA-type reaction, EC 2.6.1.19, but with less activity Paenibacillus lautus Y412MC10 ?
-
-

Subunits

EC Number Subunits Comment Organism
2.6.1.19 homotetramer 4 * 49100, recombinant Strep II-tagged enzyme, SDS-PAGE Paenibacillus lautus
2.6.1.76 homotetramer 4 * 49100, recombinant Strep II-tagged enzyme, SDS-PAGE Paenibacillus lautus

Synonyms

EC Number Synonyms Comment Organism
2.6.1.19 GABA-TA
-
 Paenibacillus lautus
2.6.1.19 More see also EC 2.6.1.76 Paenibacillus lautus
2.6.1.76 (Pl)EctB
-
 Paenibacillus lautus
2.6.1.76 EctB
-
 Paenibacillus lautus
2.6.1.76 More see also EC 2.6.1.19 Paenibacillus lautus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.76 45
-
-
 Paenibacillus lautus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.6.1.76 10 60 activity range, profile overview Paenibacillus lautus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.76 6.5
-
-
 Paenibacillus lautus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.6.1.76 5.5 10 40% of maximal activity within this range Paenibacillus lautus

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.19 pyridoxal 5'-phosphate PLP, residue Lys274 attaches the PLP cofactor to enzyme (Pl)EctB. The architecture of the PLP-binding site, formed by two monomeric subunits, overview Paenibacillus lautus
2.6.1.76 pyridoxal 5'-phosphate PLP, residue Lys274 attaches the PLP cofactor to enzyme (Pl)EctB. The architecture of the PLP-binding site, formed by two monomeric subunits, overview Paenibacillus lautus

General Information

EC Number General Information Comment Organism
2.6.1.19 evolution EctB-type proteins are highly conserved Paenibacillus lautus
2.6.1.19 additional information structural homology modeling of (Pl)EctB usimg the crystal structure of the GABA transaminase from Arthrobacter aurescens (PDB ID 4ATP, EC 2.6.1.19) as template Paenibacillus lautus
2.6.1.76 evolution EctB-type proteins are highly conserved Paenibacillus lautus
2.6.1.76 additional information structural homology modeling of (Pl)EctB using the crystal structure of the GABA transaminase from Arthrobacter aurescens (PDB ID 4ATP, EC 2.6.1.19) as template Paenibacillus lautus