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
Enzyme promiscuity: mechanism and applications
KTH, School of Biotechnology (BIO), Biochemistry (closed 20130101).
KTH, School of Biotechnology (BIO), Biochemistry (closed 20130101).ORCID iD: 0000-0002-9577-832X
2007 (English)In: Trends in Biotechnology, ISSN 0167-7799, E-ISSN 1879-3096, Vol. 25, no 5, 231-238 p.Article, review/survey (Refereed) Published
Abstract [en]

Introductory courses in biochemistry teach that enzymes are specific for their substrates and the reactions they catalyze. Enzymes diverging from this statement are sometimes called promiscuous. It has been suggested that relaxed substrate and reaction specificities can have an important role in enzyme evolution; however, enzyme promiscuity also has an applied aspect. Enzyme condition promiscuity has, for a long time, been used to run reactions under conditions of low water activity that favor ester synthesis instead of hydrolysis. Together with enzyme substrate promiscuity, it is exploited in numerous synthetic applications, from the laboratory to industrial scale. Furthermore, enzyme catalytic promiscuity, where enzymes catalyze accidental or induced new reactions, has begun to be recognized as a valuable research and synthesis tool. Exploiting enzyme catalytic promiscuity might lead to improvements in existing catalysts and provide novel synthesis pathways that are currently not available.

Place, publisher, year, edition, pages
Elsevier, 2007. Vol. 25, no 5, 231-238 p.
Keyword [en]
catalyzed markovnikov addition, pyridoxal-phosphate enzymes, active-site mutation, enolase superfamily, michael addition, reaction specificity, mutant glycosidases, organic media, oligosaccharide synthesis, thioglycoside synthesis
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-16626DOI: 10.1016/j.tibtech.2007.03.002ISI: 000246428500009Scopus ID: 2-s2.0-34247131307OAI: oai:DiVA.org:kth-16626DiVA: diva2:334668
Note

QC 20100525

Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopus

Authority records BETA

Berglund, Per

Search in DiVA

By author/editor
Hult, KarlBerglund, Per
By organisation
Biochemistry (closed 20130101)
In the same journal
Trends in Biotechnology
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 96 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