Characterization of a putative tropinone reductase from Tarenaya hassleriana with a broad substrate specificity.
Biotechnol Appl Biochem
; 69(6): 2530-2539, 2022 Dec.
Article
in En
| MEDLINE
| ID: mdl-34902878
ABSTRACT
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°C was the optimum temperature for ThTRL. The highest catalytic efficiency and substrate affinity for recombinant ThTRL were observed with (+)-camphorquinone (kcat /Km = 814.3 s-1 mM-1 , Km = 44.25 µM). ThTRL exhibited a broad substrate specificity and reduced various carbonyl compounds, including small lipophilic aldehydes and ketones, terpene ketones, and their structural analogs.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Alcohol Oxidoreductases
/
Escherichia coli
Language:
En
Journal:
Biotechnol Appl Biochem
Journal subject:
BIOQUIMICA
/
BIOTECNOLOGIA
Year:
2022
Document type:
Article
Affiliation country:
China