Aminotransferase from Thermoproteus uzoniensis
Enzyme Description
Species
Extremophile
Yes
"hyperthermophilic" organism
EC Number
Sequence
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
▼
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 TrisβHCl 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 TrisβHCl 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 TrisβHCl 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 TrisβHCl 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.