Abstract
Rhodococcus rhodochrous IFO 15564 enantioselectively hydrolysed racemic 3-benzoyloxypentanenitrile and 3-benzoyloxypentanamide to afford (R)-amide and (S)-carboxylic acid with high enantiomeric excess (> 90%). In this reaction, both enantiomers of the starting nitrile were converted to the amide by nitrile hydratase, and amidase-catalysed enantioselective hydrolysis of the amide was responsible for the kinetic resolution. The lack of enantioselectivity of the nitrile hydratase toward the racemic nitrile forms a marked contrast to the case of previously reported highly enantioselective conversion of prochiral 3-benzoyloxypentanedinitrile by this enzyme. Since (R)-amide could be hydrolysed chemically to (R)-carboxylic acid without any loss of its ee, the present microbial kinetic resolution serves as an effective method for preparing both enantiomers of synthetically useful 3-hydroxypentanoic acid derivatives.
| Original language | English |
|---|---|
| Pages (from-to) | 135-141 |
| Number of pages | 7 |
| Journal | Journal of Molecular Catalysis B: Enzymatic |
| Volume | 1 |
| Issue number | 3-6 |
| Publication status | Published - 1996 Jun |
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Keywords
- 3-Hydroxypentanoate derivatives
- Amidase
- Kinetic resolution
- Nitrile hydratase
- Rhodococcus rhodochrous
ASJC Scopus subject areas
- Biochemistry
- Catalysis
- Process Chemistry and Technology
Cite this
Preparation of both enantiomers of methyl 3-benzoyloxypentanoate by enzyme-catalysed hydrolysis of corresponding racemic nitrile and amide. / Yokoyama, Masahiro; Imai, Nori; Sugai, Takeshi; Ohta, Hiromichi.
In: Journal of Molecular Catalysis B: Enzymatic, Vol. 1, No. 3-6, 06.1996, p. 135-141.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Preparation of both enantiomers of methyl 3-benzoyloxypentanoate by enzyme-catalysed hydrolysis of corresponding racemic nitrile and amide
AU - Yokoyama, Masahiro
AU - Imai, Nori
AU - Sugai, Takeshi
AU - Ohta, Hiromichi
PY - 1996/6
Y1 - 1996/6
N2 - Rhodococcus rhodochrous IFO 15564 enantioselectively hydrolysed racemic 3-benzoyloxypentanenitrile and 3-benzoyloxypentanamide to afford (R)-amide and (S)-carboxylic acid with high enantiomeric excess (> 90%). In this reaction, both enantiomers of the starting nitrile were converted to the amide by nitrile hydratase, and amidase-catalysed enantioselective hydrolysis of the amide was responsible for the kinetic resolution. The lack of enantioselectivity of the nitrile hydratase toward the racemic nitrile forms a marked contrast to the case of previously reported highly enantioselective conversion of prochiral 3-benzoyloxypentanedinitrile by this enzyme. Since (R)-amide could be hydrolysed chemically to (R)-carboxylic acid without any loss of its ee, the present microbial kinetic resolution serves as an effective method for preparing both enantiomers of synthetically useful 3-hydroxypentanoic acid derivatives.
AB - Rhodococcus rhodochrous IFO 15564 enantioselectively hydrolysed racemic 3-benzoyloxypentanenitrile and 3-benzoyloxypentanamide to afford (R)-amide and (S)-carboxylic acid with high enantiomeric excess (> 90%). In this reaction, both enantiomers of the starting nitrile were converted to the amide by nitrile hydratase, and amidase-catalysed enantioselective hydrolysis of the amide was responsible for the kinetic resolution. The lack of enantioselectivity of the nitrile hydratase toward the racemic nitrile forms a marked contrast to the case of previously reported highly enantioselective conversion of prochiral 3-benzoyloxypentanedinitrile by this enzyme. Since (R)-amide could be hydrolysed chemically to (R)-carboxylic acid without any loss of its ee, the present microbial kinetic resolution serves as an effective method for preparing both enantiomers of synthetically useful 3-hydroxypentanoic acid derivatives.
KW - 3-Hydroxypentanoate derivatives
KW - Amidase
KW - Kinetic resolution
KW - Nitrile hydratase
KW - Rhodococcus rhodochrous
UR - http://www.scopus.com/inward/record.url?scp=0030568601&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030568601&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0030568601
VL - 1
SP - 135
EP - 141
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
SN - 1381-1177
IS - 3-6
ER -