Transaminase from Vulcanisaeta moutnovskia

Enzyme Description

Extremophile
Yes "hyperthermophilic" organism
EC Number

Sequence

Length: 314 amino acids
MIMLNKEPIVQHLMKYVWVNGKLIPEKEATIPILTHALHYGTSIFEGIRAYWNSDNNNLYVFRARDHYVRFHDSAKIMSIKVGYSVDELIDATVELLRANDVHEDVYIRPITFVSASTVNLDIRNLDVTTAIITVPFGHYLEPKGIKAKVVSWLRVHNSMFPMKAKVSGIYVNSVIAIIDAKVSGFDEAILLNRDGYVAEGSGENIFIIKDGILYTPPVYDSILEGITRDTVITIARDLGLTVTEKRITREELYTADEVFFTGTAAEVTPVVNIDGRVIGNGEPGPIALKVRSYYMDVVHGRVSKYKNWLTPIY
Tatiana N. Stekhanova et al. (2017) β€” A Novel highly thermostable branched-chain amino acid aminotransferase from the crenarchaeon Vulcanisaeta moutnovskia
Enzyme and Microbial Technology  Β· doi:10.1016/j.enzmictec.2016.10.002 β†—  Β· Activity - Classical
4 measurements
Database ID
UniProt: F0QW25 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, NADH absorbance measurement, with reaction catalyzed by an alanine dehydrogenase from Bacillus cereus) in the presence of organic solvent Dimethyl Sulfoxide (DMSO) 15% 3.7 2.6 % 50 mM Tris-HCl buffer, 100 mM NaCl 8 65Β°C 20 mM L-ornithine, 40 mM Pyruvate Glutamate-5-semialdehyde , L-Alanine 60 Β΅M PLP β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (alanine dehydrogenase assay, NADH absorbance measurement, with reaction catalyzed by an alanine dehydrogenase from Bacillus cereus) in the presence of organic solvent Dimethylformamide (DMF) 15% 3.7 1.4 % 50 mM Tris-HCl buffer, 100 mM NaCl 8 65Β°C 20 mM L-ornithine, 40 mM Pyruvate Glutamate-5-semialdehyde , L-Alanine 60 Β΅M PLP β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (alanine dehydrogenase assay, NADH absorbance measurement, with reaction catalyzed by an alanine dehydrogenase from Bacillus cereus) in the presence of organic solvent Methanol 15% 3.7 2.4 % 50 mM Tris-HCl buffer, 100 mM NaCl 8 65Β°C 20 mM L-ornithine, 40 mM Pyruvate Glutamate-5-semialdehyde , L-Alanine 60 Β΅M PLP β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (alanine dehydrogenase assay, NADH absorbance measurement, with reaction catalyzed by an alanine dehydrogenase from Bacillus cereus) in the presence of organic solvent Acetonitrile 15% 3.7 1.2 % 50 mM Tris-HCl buffer, 100 mM NaCl 8 65Β°C 20 mM L-ornithine, 40 mM Pyruvate Glutamate-5-semialdehyde , L-Alanine 60 Β΅M PLP β€” Classical aqueous control (in %)

Visualization : Activity β€” Classical

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

Structure

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