Journal
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
Volume 69, Issue 6, Pages 2530-2539Publisher
WILEY
DOI: 10.1002/bab.2302
Keywords
enzyme kinetics; short-chain alcohol dehydrogenases/reductases; substrate specificity; terpene ketones; tropinone reductase-like enzyme
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The novel enzyme ThTRL from T. hassleriana exhibits broad substrate specificity, able to reduce various compounds with carbonyl groups, and shows high catalytic efficiency under specific conditions.
A novel short-chain alcohol dehydrogenase from Tarenaya hassleriana labeled as putative tropinone reductase was heterologously expressed in Escherichia coli. Purified recombinant protein had molecular weight of approximately 30 kDa on 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis. T. hassleriana tropinone reductase-like enzyme (ThTRL) had not detected oxidative activity. The optimum pH for enzyme activity of ThTRL was weakly acidic (pH 5.0). 50 degrees C was the optimum temperature for ThTRL. The highest catalytic efficiency and substrate affinity for recombinant ThTRL were observed with (+)-camphorquinone (k(cat)/K-m = 814.3 s(-1) mM(-1), K-m = 44.25 mu M). ThTRL exhibited a broad substrate specificity and reduced various carbonyl compounds, including small lipophilic aldehydes and ketones, terpene ketones, and their structural analogs.
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