Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
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
Identifiers
URN: urn:nbn:se:kth:diva-37553DOI: 10.1002/ejoc.201001664ISI: 000293133100001Scopus ID: 2-s2.0-79959757238OAI: oai:DiVA.org:kth-37553DiVA: diva2:434436
Note

QC 20110815

Available from: 2011-08-15 Created: 2011-08-15 Last updated: 2017-12-08Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopus

Authority records BETA

Svedendahl Humble, MariaBerglund, Per

Search in DiVA

By author/editor
Svedendahl Humble, MariaBerglund, Per
By organisation
Biochemistry (closed 20130101)
In the same journal
European Journal of Organic Chemistry
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 138 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf