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7.18 C-X Bond Formation: Transaminases as Chiral Catalysts: Mechanism, Engineering, and Applications
KTH, School of Biotechnology (BIO), Biochemistry (closed 20130101).ORCID iD: 0000-0002-9577-832X
2012 (English)In: Comprehensive Chirality, Elsevier, 2012, Vol. 7, 390-401 p.Chapter in book (Refereed)
Abstract [en]

Enantiomerically pure amines and amino acids are important building blocks in academic research as well as in industrial-scale chemical production. Transaminases are versatile enzymes providing access to such compounds of high enantiomeric excess. This chapter illustrates the available strategies with transaminases such as kinetic resolution or stereoselective synthesis and highlights many successful examples for amino acid and chiral amines synthesis. There are some known challenges linked to the use of transaminases, for example in terms of unfavorable equilibria and inhibition. Several successful examples to overcome these limitations are presented. Also, the classification of transaminases, mechanistic details, and various strategies for optimization are discussed.

Place, publisher, year, edition, pages
Elsevier, 2012. Vol. 7, 390-401 p.
Keyword [en]
Amino acids, Aminotransferase, Chiral amines, Enzyme engineering, Equilibrium displacement, Product inhibition, Pyridoxal 5'-phosphate
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Identifiers
URN: urn:nbn:se:kth:diva-162995DOI: 10.1016/B978-0-08-095167-6.00723-0Scopus ID: 2-s2.0-84899893722ISBN: 978-008095168-3 OAI: oai:DiVA.org:kth-162995DiVA: diva2:798861
Note

QC 20150327. QC 20160207

Available from: 2015-03-27 Created: 2015-03-26 Last updated: 2016-02-07Bibliographically approved

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Berglund, PerSvedendahl Humble, Maria

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