expression of CBR mRNA is a significant prognostic factor in nonsmall-cell lung cancer and is inversely associated with tumor progression and angiogenesis
the cardioprotectant 7-monohydroxyethylrutoside inhibits CBR1 activity. CBR1 V88I genotype status and the type of anthracycline substrate dictate the inhibition of CBR1 activity. Inhibition of CBR1 activity shall be considered during the development of novel cardioprotectants against anthracycline-related cardiotoxicity
improved (R)-1-phenyl-1,2-ethanediol production by a codon optimized R-specific carbonyl reductase whose coding gene rcr is engineered by truncating its disorder sequence of 4-27 bp at 5'-terminus and adaption of codon usage bias in Escherichia coli. It will provide a new method to establish an effective expression system for improving chiral alcohol productivity by codon optimization
modification of coenzyme specificity and alteration of product enantioselectivity in SDRs by using the protein engineering approach, which will have valuable industrial applications
the single nucleotide polymorphisms in the human CBR1 gene generating the V88I and P131S mutations may prove to be clinically useful genetic biomarkers for guiding anthracycline therapy in cancer patients to minimize adverse effects
enzyme is useful for production of ethyl (S)-4-chloro-3-hydroxybutanoate, which is used in the synthesis of pharmacologically and biologically important compouds
enzyme might be useful for production of ethyl (S)-4-chloro-3-hydroxybutanoate, which is used in the synthesis of pharmacologically and biologically important compounds
production of carbonyl reductase by Candida viswanathii in 6.6 l fermentor, using controlled pH value at 8.0, aeration rate 1 vvm and an agitation speed of 250 rpm at 25°C. Use of enzyme for preparative scale reduction of N,N-dimethyl-3-keto-2-thienyl-propanamine to (S)-N,N-dimethyl-3-keto-2-thienyl-propanamine
production of Geotrichum candidum carbonyl reductase in a laboratory scale stirred tank bioreactor, optimization of conditions. At controlled pH value of 5.5 the specific enzyme activity is highest with 306 U/mg. Optimization of glucose concentration yields 21 g/l cell mass with 9770 U enzyme activity/g glucose
synthesis of (R)-beta-hydroxynitriles with good optical purity by use of recombinant carbonyl reductase and further conversion to (R)-beta-hydroxy carboxylic acids via a nitrilase-catalyzed hydrolysis
synthesis of (3S)-acetoin in a coupled system consisting of glucose dehydrogenase from Bacillus subtilis 168 and the NADPH-dependent carbonyl reductase. Under the optimal conditions, 12.2 g/l (3S)-acetoin is produced from 14.3 g/l diacetyl in 75 min
optimum substrate, 2,2,2-trifluoroacetophenone, is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98%
coexpression with glucose dehydrogenase from Bacillus subtilis for NADPH regeneration in Escherichia coli and optimization of linker peptides used for the fusion expression of carbonyl reductase and glucose dehydrogenase. Up to 297.3 g/L (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol with enantiopurity >99.9% ee is produced via reduction of 1.2 M of substrate with a 96.7% yield and productivity of 29.7 g/(L h)
in situ expression in Candida leads to over fourfold higher activity for conversion of racemic (R,S)-1-phenyl-1,2-ethanediol to 2-hydroxyacetophenone, while maintaining the activity for catalyzing 2-hydroxyacetophenone to (S)-1-phenyl-1,2-ethanediol. A recombinant Candida parapsilosis converts racemic (R,S)-1-phenyl-1,2-ethanediol to its (S)-isomer with an optical purity of 98.8% and a yield of 48.4%. The biotransformation duration is reduced from 48 to 13 h
optimum substrate, 2,2,2-trifluoroacetophenone, is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98%
synthesis of (3S)-acetoin in a coupled system consisting of glucose dehydrogenase from Bacillus subtilis 168 and the NADPH-dependent carbonyl reductase. Under the optimal conditions, 12.2 g/l (3S)-acetoin is produced from 14.3 g/l diacetyl in 75 min
production of Geotrichum candidum carbonyl reductase in a laboratory scale stirred tank bioreactor, optimization of conditions. At controlled pH value of 5.5 the specific enzyme activity is highest with 306 U/mg. Optimization of glucose concentration yields 21 g/l cell mass with 9770 U enzyme activity/g glucose
optimum substrate, 2,2,2-trifluoroacetophenone, is asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8% and a conversion of 98%