This title appears in the Scientific Report :
2005
Please use the identifier:
http://dx.doi.org/10.1007/s00253-004-1765-5 in citations.
Enantioselective reduction of carbonyl-compounds by whole-cell biotransformation, combining a formate dehydrogenase and a (R)-specific alcohol dehydrogenase
Enantioselective reduction of carbonyl-compounds by whole-cell biotransformation, combining a formate dehydrogenase and a (R)-specific alcohol dehydrogenase
A whole-cell biotransformation system for the reduction of prochiral carbonyl compounds, such as methyl acetoacetate, to chiral hydroxy acid derivatives [methyl (R)-3-hydroxy butanoate] was developed in Escherichia coli by construction of a recombinant oxidation/reduction cycle. Alcohol dehydrogenas...
Saved in:
Personal Name(s): | Ernst, M. |
---|---|
Kaup, B. / Müller, M. / Bringer-Meyer, S. / Sahm, H. | |
Contributing Institute: |
Biotechnologie 1; IBT-1 Biotechnologie 2; IBT-2 |
Published in: | Applied Microbiology and Biotechnology, 66 (2005) S. 629 - 634 |
Imprint: |
Berlin
Springer
2005
|
Physical Description: |
629 - 634 |
DOI: |
10.1007/s00253-004-1765-5 |
PubMed ID: |
15549291 |
Document Type: |
Journal Article |
Research Program: |
Biotechnologie |
Series Title: |
Applied Microbiology and Biotechnology
66 |
Subject (ZB): | |
Publikationsportal JuSER |
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100 | 1 | |a Ernst, M. |b 0 |u FZJ |0 P:(DE-Juel1)VDB28976 | |
245 | |a Enantioselective reduction of carbonyl-compounds by whole-cell biotransformation, combining a formate dehydrogenase and a (R)-specific alcohol dehydrogenase | ||
260 | |c 2005 |a Berlin |b Springer | ||
300 | |a 629 - 634 | ||
440 | 0 | |a Applied Microbiology and Biotechnology |x 0175-7598 |0 555 |y 6 |v 66 | |
500 | |a Record converted from VDB: 12.11.2012 | ||
520 | |a A whole-cell biotransformation system for the reduction of prochiral carbonyl compounds, such as methyl acetoacetate, to chiral hydroxy acid derivatives [methyl (R)-3-hydroxy butanoate] was developed in Escherichia coli by construction of a recombinant oxidation/reduction cycle. Alcohol dehydrogenase from Lactobacillus brevis catalyzes a highly regioselective and enantioselective reduction of several ketones or keto acid derivatives to chiral alcohols or hydroxy acid esters. The adh gene encoding for the alcohol dehydrogenase of L. brevis was expressed in E. coli. As expected, whole cells of the recombinant strain produced only low quantities of methyl (R)-3-hydroxy butanoate from the substrate methyl acetoacetate. Therefore, the fdh gene from Mycobacterium vaccae N10, encoding NAD+-dependent formate dehydrogenase, was functionally coexpressed. The resulting two-fold recombinant strain exhibited an in vitro catalytic alcohol dehydrogenase activity of 6.5 units mg-1 protein in reducing methyl acetoacetate to methyl (R)-3-hydroxy butanoate with NADPH as the cofactor and 0.7 units mg-1 protein with NADH. The in vitro formate dehydrogenase activity was 1.3 units mg-1 protein. Whole resting cells of this strain catalyzed the formation of 40 mM methyl (R)-3-hydroxy butanoate from methyl acetoacetate. The product yield was 100 mol% at a productivity of 200 micromol g-1 (cell dry weight) min-1. In the presence of formate, the intracellular [NADH]/[NAD+] ratio of the cells increased seven-fold. Thus, the functional overexpression of alcohol dehydrogenase in the presence of formate dehydrogenase was sufficient to enable and sustain the desired reduction reaction via the relatively low specific activity of alcohol dehydrogenase with NADH, instead of NADPH, as a cofactor. | ||
588 | |a Dataset connected to Web of Science, Pubmed | ||
650 | 2 | |2 MeSH |a Acetoacetates: metabolism | |
650 | 2 | |2 MeSH |a Alcohol Dehydrogenase: genetics | |
650 | 2 | |2 MeSH |a Alcohol Dehydrogenase: metabolism | |
650 | 2 | |2 MeSH |a Alcohol Oxidoreductases: metabolism | |
650 | 2 | |2 MeSH |a Biotransformation | |
650 | 2 | |2 MeSH |a Coenzymes: pharmacology | |
650 | 2 | |2 MeSH |a Escherichia coli: enzymology | |
650 | 2 | |2 MeSH |a Escherichia coli: genetics | |
650 | 2 | |2 MeSH |a Escherichia coli: metabolism | |
650 | 2 | |2 MeSH |a Formate Dehydrogenases: genetics | |
650 | 2 | |2 MeSH |a Formate Dehydrogenases: metabolism | |
650 | 2 | |2 MeSH |a Lactobacillus: enzymology | |
650 | 2 | |2 MeSH |a Lactobacillus: genetics | |
650 | 2 | |2 MeSH |a Mycobacterium: enzymology | |
650 | 2 | |2 MeSH |a Mycobacterium: genetics | |
650 | 2 | |2 MeSH |a Organic Chemicals: metabolism | |
650 | 2 | |2 MeSH |a Oxidation-Reduction | |
650 | 2 | |2 MeSH |a Recombinant Proteins: genetics | |
650 | 2 | |2 MeSH |a Recombinant Proteins: metabolism | |
650 | 2 | |2 MeSH |a Stereoisomerism | |
650 | 2 | |2 MeSH |a Substrate Specificity | |
650 | 7 | |0 0 |2 NLM Chemicals |a Acetoacetates | |
650 | 7 | |0 0 |2 NLM Chemicals |a Coenzymes | |
650 | 7 | |0 0 |2 NLM Chemicals |a Organic Chemicals | |
650 | 7 | |0 0 |2 NLM Chemicals |a Recombinant Proteins | |
650 | 7 | |0 105-45-3 |2 NLM Chemicals |a methyl acetoacetate | |
650 | 7 | |0 EC 1.1.- |2 NLM Chemicals |a Alcohol Oxidoreductases | |
650 | 7 | |0 EC 1.1.1.1 |2 NLM Chemicals |a Alcohol Dehydrogenase | |
650 | 7 | |0 EC 1.2.1.2 |2 NLM Chemicals |a Formate Dehydrogenases | |
650 | 7 | |0 EC 1.2.1.43 |2 NLM Chemicals |a formate dehydrogenase (NADP+) | |
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700 | 1 | |a Sahm, H. |b 4 |u FZJ |0 P:(DE-Juel1)128985 | |
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