Increased availability of NADH in metabolically engineered baker's yeast improves transaminase-oxidoreductase coupled asymmetric whole-cell bioconversion.
(2016) In Microbial Cell Factories 15(1).- Abstract
- Saccharomyces cerevisiae can be engineered to perform a multitude of different chemical reactions that are not programmed in its original genetic code. It has a large potential to function as whole-cell biocatalyst for one-pot multistep synthesis of various organic molecules, and it may thus serve as a powerful alternative or complement to traditional organic synthetic routes for new chemical entities (NCEs). However, although the selectivity in many cases is high, the catalytic activity is often low which results in low space-time-yields. In the case for NADH-dependent heterologous reductive reactions, a possible constraint is the availability of cytosolic NADH, which may be limited due to competition with native oxidative enzymes that... (More)
- Saccharomyces cerevisiae can be engineered to perform a multitude of different chemical reactions that are not programmed in its original genetic code. It has a large potential to function as whole-cell biocatalyst for one-pot multistep synthesis of various organic molecules, and it may thus serve as a powerful alternative or complement to traditional organic synthetic routes for new chemical entities (NCEs). However, although the selectivity in many cases is high, the catalytic activity is often low which results in low space-time-yields. In the case for NADH-dependent heterologous reductive reactions, a possible constraint is the availability of cytosolic NADH, which may be limited due to competition with native oxidative enzymes that act to maintain redox homeostasis. In this study, the effect of increasing the availability of cytosolic NADH on the catalytic activity of engineered yeast for transamination-reduction coupled asymmetric one-pot conversion was investigated. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8825433
- author
- Knudsen, Jan LU ; Hägglöf, Cecilia ; Weber, Nora LU and Carlquist, Magnus LU
- organization
- publishing date
- 2016
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Microbial Cell Factories
- volume
- 15
- issue
- 1
- article number
- 37
- publisher
- BioMed Central (BMC)
- external identifiers
-
- pmid:26879378
- scopus:84957956469
- wos:000370027700002
- pmid:26879378
- ISSN
- 1475-2859
- DOI
- 10.1186/s12934-016-0430-x
- language
- English
- LU publication?
- yes
- id
- 572c5aa7-a979-4e1c-9eb2-4ff5e9986f68 (old id 8825433)
- date added to LUP
- 2016-04-01 15:02:41
- date last changed
- 2022-01-28 03:48:41
@article{572c5aa7-a979-4e1c-9eb2-4ff5e9986f68,
abstract = {{Saccharomyces cerevisiae can be engineered to perform a multitude of different chemical reactions that are not programmed in its original genetic code. It has a large potential to function as whole-cell biocatalyst for one-pot multistep synthesis of various organic molecules, and it may thus serve as a powerful alternative or complement to traditional organic synthetic routes for new chemical entities (NCEs). However, although the selectivity in many cases is high, the catalytic activity is often low which results in low space-time-yields. In the case for NADH-dependent heterologous reductive reactions, a possible constraint is the availability of cytosolic NADH, which may be limited due to competition with native oxidative enzymes that act to maintain redox homeostasis. In this study, the effect of increasing the availability of cytosolic NADH on the catalytic activity of engineered yeast for transamination-reduction coupled asymmetric one-pot conversion was investigated.}},
author = {{Knudsen, Jan and Hägglöf, Cecilia and Weber, Nora and Carlquist, Magnus}},
issn = {{1475-2859}},
language = {{eng}},
number = {{1}},
publisher = {{BioMed Central (BMC)}},
series = {{Microbial Cell Factories}},
title = {{Increased availability of NADH in metabolically engineered baker's yeast improves transaminase-oxidoreductase coupled asymmetric whole-cell bioconversion.}},
url = {{http://dx.doi.org/10.1186/s12934-016-0430-x}},
doi = {{10.1186/s12934-016-0430-x}},
volume = {{15}},
year = {{2016}},
}