Aminotransferase from Thermoproteus uzoniensis

Enzyme Description

Extremophile
Yes "hyperthermophilic" organism
EC Number

Sequence

Length: 295 amino acids
MKVWLDGRLVDEEEAKVTVLSPSLNYGFGVFEGIRAYWNGENLYVFRLRDHMERLLRSAKIIGLDVPYTAEELSKAVVETVRANGFKEDLYIRPVAYISKPQISLDVRGLQASVAIAAIPFGKYLKVEGVRAAVVSWRRVHTSMMPVMAKATGIYLNSIMAAVEARARGYDEAIMLNAEGKVVEGSGENIFIVRRGVLMTPPLEDGILEGITRETVISIAGDLGIPLLEKSITREELYAADEAFFVGTAAEITPIIEIDGRVLQRGPITQKIAETYRRIVLGKEEKYLPWLTPVY
Konstantin M. Boyko et al. (2016) β€” First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for l-amino acids and R-amines
Extremophiles  Β· doi:10.1007/s00792-016-0816-z β†—  Β· Activity - Classical
4 measurements
Database ID
UniProt: F2L0W0 β†—
Sequence Annotation
Explicit - Provided
Protein Source
Recombinant, host bacterium Escherichia coli DLT1270

Experimental Data (4 measurements)

4 measurements
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Activity - Classical Activity measured by absorbance spectrophotometry (alanine dehydrogenase assay, L-alanine dehydrogenation by an alanine dehydrgenase from Bacillus cereus, and NADH absorbance measurement, 340 nm) in the presence of organic solvent Dimethyl Sulfoxide (DMSO) 15% 100 62 % 50 mM Tris–HCl buffer, 100 mM NaCl 9 65Β°C 20 mM L-Leucine, 20 mM Pyruvate L-Alanine , Ξ±-Ketoisocaproate 60 ΞΌM PLP β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (alanine dehydrogenase assay, L-alanine dehydrogenation by an alanine dehydrgenase from Bacillus cereus, and NADH absorbance measurement, 340 nm) in the presence of organic solvent Dimethylformamide (DMF) 15% 100 17 % 50 mM Tris–HCl buffer, 100 mM NaCl 9 65Β°C 20 mM L-Leucine, 20 mM Pyruvate L-Alanine , Ξ±-Ketoisocaproate 60 ΞΌM PLP β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (alanine dehydrogenase assay, L-alanine dehydrogenation by an alanine dehydrgenase from Bacillus cereus, and NADH absorbance measurement, 340 nm) in the presence of organic solvent Methanol 15% 100 31 % 50 mM Tris–HCl buffer, 100 mM NaCl 9 65Β°C 20 mM L-Leucine, 20 mM Pyruvate L-Alanine , Ξ±-Ketoisocaproate 60 ΞΌM PLP β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (alanine dehydrogenase assay, L-alanine dehydrogenation by an alanine dehydrgenase from Bacillus cereus, and NADH absorbance measurement, 340 nm) in the presence of organic solvent Acetonitrile 15% 100 6 % 50 mM Tris–HCl buffer, 100 mM NaCl 9 65Β°C 20 mM L-Leucine, 20 mM Pyruvate L-Alanine , Ξ±-Ketoisocaproate 60 ΞΌM PLP β€” Classical aqueous control (in %)

Visualization : Activity β€” Classical

One bar per measurement. Colour = solvent, shade = solvent volume.

Structure

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