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Biocatalytic Promiscuity
KTH, School of Biotechnology (BIO), Biochemistry (closed 20130101).ORCID iD: 0000-0003-2371-8755
KTH, School of Biotechnology (BIO), Biochemistry (closed 20130101).ORCID iD: 0000-0002-9577-832X
2011 (English)In: European Journal of Organic Chemistry, ISSN 1434-193X, E-ISSN 1099-0690, no 19, 3391-3401 p.Article, review/survey (Refereed) Published
Abstract [en]

Enzymes are attractive catalysts because of their promiscuity and their ability to perform highly regio-, chemo- and stereo-selective transformations. Enzyme promiscuity allows optimisation of industrial processes that require reaction conditions different from those in nature. Many enzymes can be used in reactions completely different from the reaction the enzyme originally evolved to perform. Such catalytically promiscuous reactions can be secondary activities hidden behind a native activity and might be discovered either in screening for that particular activity or, alternatively, by chance. Recently, researchers have designed enzymes to show catalytic promiscuity. It is also possible to design new enzymes from scratch by computer modelling (de novo design), but most work published to date starts from a known enzyme backbone. Promiscuous activity might also be induced or enhanced by rational design or directed evolution (or combinations thereof). Enzyme catalytic promiscuity provides fundamental knowledge about enzyme/substrate interactions and the evolution of new enzymes. New enzymes are required by industry, which needs to optimise chemical processes in an environmentally sustainable way. In this review various aspects of enzyme catalytic promiscuity are considered from a biocatalytic perspective.

Place, publisher, year, edition, pages
John Wiley & Sons, 2011. no 19, 3391-3401 p.
Keyword [en]
Enzyme catalysis, Biocatalysis, Biotransformations, Catalytic promiscuity, Protein engineering
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-37553DOI: 10.1002/ejoc.201001664ISI: 000293133100001ScopusID: 2-s2.0-79959757238OAI: diva2:434436

QC 20110815

Available from: 2011-08-15 Created: 2011-08-15 Last updated: 2015-12-08Bibliographically approved

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Svedendahl Humble, MariaBerglund, Per
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Biochemistry (closed 20130101)
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