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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
URN: urn:nbn:se:kth:diva-16626DOI: 10.1016/j.tibtech.2007.03.002ISI: 000246428500009ScopusID: 2-s2.0-34247131307OAI: diva2:334668

QC 20100525

Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2015-12-08Bibliographically approved

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Hult, KarlBerglund, Per
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