Microbial reduction of 2-norbornanone by Chlorella

Yoshizako, Fumiki; Nishimura, Atsuo; Chubachi, Mitsuo; Kirihata, Mitsunori

doi:10.1016/s0922-338x(97)81261-5

Cited by 11 publications

(6 citation statements)

References 12 publications

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“…The reaction mixture was shaken at 378C at 200 rpm for 72 h. This reaction yielded (R)- (1) [30][31][32][33][34] was obtained from basic hydrolysis (0.1 M KOH) of (R)-endo-norbornyl butyrate in ethanol (95%) in 99% yield. The enantiomeric excess (ee) values of (S)- (2)-endo-and (R)-(1)-endo-2-norborneols from the resolutions were calculated to be 90 and 92%, respectively, from the 19 F NMR spectra of their Mosher's esters (Table 1).…”

Section: (S)-(2)-endo-and ( R)-(1)-endo-2-norborneolmentioning

confidence: 99%

Synthesis of enantiomers of exo‐2‐norbornyl‐N‐n‐butylcarbamate and endo‐2‐norbornyl‐N‐n‐butylcarbamate for stereoselective inhibition of acetylcholinesterase

et al. 2009

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The acetylcholinesterase inhibition by enantiomers of exo- and endo-2-norbornyl-N-n-butylcarbamates shows high stereoselelectivity. For the acetylcholinesterase inhibitions by (R)-(+)- and (S)-(-)-exo-2-norbornyl-N-n-butylcarbamates, the R-enantiomer is more potent than the S-enantiomer. But, for the acetylcholinesterase inhibitions by (R)-(+)- and (S)-(-)-endo-2-norbornyl-N-n-butylcarbamates, the S-enantiomer is more potent than the R-enantiomer. Optically pure (R)-(+)-exo-, (S)-(-)-exo-, (R)-(+)-endo-, and (S)-(-)-endo-2-norbornyl-N-n-butylcarbamates are synthesized from condensations of optically pure (R)-(+)-exo-, (S)-(-)-exo-, (R)-(+)-endo-, and (S)-(-)-endo-2-norborneols with n-butyl isocyanate, respectively. Optically pure norborneols are obtained from kinetic resolutions of their racemic esters by lipase catalysis in organic solvent.

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Section: (S)-(2)-endo-and ( R)-(1)-endo-2-norborneolmentioning

confidence: 99%

Synthesis of enantiomers of exo‐2‐norbornyl‐N‐n‐butylcarbamate and endo‐2‐norbornyl‐N‐n‐butylcarbamate for stereoselective inhibition of acetylcholinesterase

et al. 2009

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“…To a t-butyl methyl ether (50 mL) solution of racemic (±)-endo-2-norborneol (44.6 mmol) and vinyl acetate (10 mL), porcine pancreatic lipase (30 g [34][35][36][37][38] ) was obtained from basic hydrolysis (0.1 M KOH) of (R)-endo-norbornyl butyrate in ethanol (95%) in 99% yield. The enantiomeric excess (e.e.)…”

Section: (S)-(-)-endo-and (R)-(+)-endo-2-norborneol (Scheme 2)mentioning

confidence: 99%

“…Duplicate sets of data were collected for each inhibitor concentration. [34][35][36][37][38] and the 19 F-NMR spectra of their Mosher's ester derivatives [39][40][41] (Table 1 and Scheme 3).…”

mentioning

confidence: 99%

Stereoselective inhibition of butyrylcholinesterase by enantiomers ofexo- andendo-2-norbornyl-N-n-butylcarbamates

Chiou

Huang

Yeh

et al. 2009

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…The possibility of using green algae as biocatalysts to synthesize chiral building blocks has been also investigated. For example, Yoshizako et al reported that the stereoselective reduction of various carbonyl compounds by Chlorella pyrenoidosa Chick yielded the corresponding chiral alcohols (Yoshizako et al 1992(Yoshizako et al , 1994(Yoshizako et al , 1995(Yoshizako et al , 1996(Yoshizako et al , 1998Kuramoto et al 1999). Furthermore, ethyl 2-methyl-3-oxobutanoate was exclusively reduced to the corresponding syn-(2R, 3S)-hydroxy ester by photoautotrophically cultivated Chlorella sorokiniana in the presence of glycerol (Ishihara et al 2000a(Ishihara et al , 2003.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a novel keto ester reductase from the green alga, Chlorella sorokiniana: comparison of enzymological properties with other microbial keto ester reductases

Ishihara

Iwai

Yoshida

et al. 2010

World J Microbiol Biotechnol

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A novel keto ester reductase (Chlorella sorokiniana keto ester reductase, CSKER) from Chlorella sorokiniana SAG 211-8k cells was purified. The CSKER had a monomeric structure based on gel filtration chromatography (37 kDa) and SDS-polyacrylamide gel electrophoresis (34 kDa). The purified CSKER showed a high reducing activity with b-keto esters, in particular, ethyl 4-chloro-3-oxobutanoate and ethyl 2-chloro-3-oxobutanoate. However, the purified enzyme did not show any reducing activity with a-keto esters and 2-chlorobenzoylformamide (aromatic a-keto amide). The CSKER catalyzed the reduction of ethyl 4-chloro-3-oxobutanoate, ethyl 3-oxobutanoate, and methyl 3-oxobutanoate to the corresponding (R)-, (S)-, and (S)-hydroxy ester, respectively, with high enantioselectivity ([99% e.e.), respectively. Furthermore, the reduction of ethyl 2-methyl-3-oxobutanoate by CSKER exclusively yielded the corresponding syn-(2R, 3S)-hydroxy ester. The purified CSKER was inactive with NADH, used instead of NADPH. None of the keto ester-reducing enzymes already isolated from other microorganisms was identical to the CSKER. These results suggested that CSKER is a novel keto ester reductase that has not yet been reported.

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Microbial reduction of 2-norbornanone by Chlorella

Cited by 11 publications

References 12 publications

Synthesis of enantiomers of exo‐2‐norbornyl‐N‐n‐butylcarbamate and endo‐2‐norbornyl‐N‐n‐butylcarbamate for stereoselective inhibition of acetylcholinesterase

Synthesis of enantiomers of exo‐2‐norbornyl‐N‐n‐butylcarbamate and endo‐2‐norbornyl‐N‐n‐butylcarbamate for stereoselective inhibition of acetylcholinesterase

Stereoselective inhibition of butyrylcholinesterase by enantiomers ofexo- andendo-2-norbornyl-N-n-butylcarbamates

Purification and characterization of a novel keto ester reductase from the green alga, Chlorella sorokiniana: comparison of enzymological properties with other microbial keto ester reductases

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