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B6db references: 27871372

type Journal Article
authors Stekhanova TN, Rakitin AL, Mardanov AV, Bezsudnova EY, Popov VO
title A Novel highly thermostable branched-chain amino acid aminotransferase from the crenarchaeon Vulcanisaeta moutnovskia
journal Enzyme Microb Technol
Activity tuzn1299
Family tuzn1299
sel selected
ui 27871372
year (2017)
volume 96
pages 127-134
keywords Branched-chain amino acid aminotransferase; Sequence motifs; Substrate specificity; Thermostability
abstract A new fold-type IV branched-chain amino acid aminotransferase VMUT0738 from the hyperthermophilic Crenarchaeon Vulcanisaeta moutnovskia was successfully expressed in Escherichia coli. Purified VMUT0738 showed activity toward numerous aliphatic and aromatic l-amino acids and 2-oxo acids at optimal pH 8.0. Distinguishing features of the VMUT0738 compared with typical BCAT are the absence of activity toward acidic substrates, high activity toward basic ones, and low but detectable activity toward the (R)-enantiomer of α-methylbenzylamine (0.0076U/mg) The activity of VMUT0738 increases with a rise in the temperature from 60C to 90C. VMUT0738 showed high thermostability (after 24h incubation at 70C the enzyme lost only 27% of the initial activity) and the resistance to organic solvents. The sequence alignment revealed two motifs (V/I)xLDxR and PFG(K/H)YL characteristic of BCATs from species of the related genera Vulcanisaeta, Pyrobaculum and Thermoproteus that might be responsible for the unique substrate recognition profile of the enzyme.
last changed 2017/12/22 08:42

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