CASCAT: Redesign of omega-Transaminases for Synthesis of Chiral Amines
2010 (English)In: Journal of Biotechnology, ISSN 0168-1656, E-ISSN 1873-4863, Vol. 150, S123-S124 p.Article in journal (Other academic) Published
Transaminases (EC 18.104.22.168) are attractive biocatalysts for synthesis of chiral amines and alpha-amino acids. These enzymes catalyze transfer of an amine group from a donor substrate to an acceptor compound using the cofactor pyridoxal-5′-phoshate (PLP). omega-Transaminases are a versatile subgroup of the transaminases that does not require a carboxylic acid group in alpha-position (in contradiction toalpha-transaminases) and hence accept a wider spectrum of ketones or amines. The omega-transaminases are employed industrially for production of both R- and S-enantiopure amines.
One bottleneck is the unfavourable equilibrium in such reactions run in the synthesis mode. We have developed a one-pot multi-enzyme system in a cascade fashion for equilibrium displacement by removing formed acetone.
Another issue is the fact that most omega-transaminases show S-selectivity, however a few R-selective strains do exist. We have used an S-selective omega-transaminase variant from Arthrobacter citreus and created an R-selective variant by rational redesign using a homology enzyme model. This homology modelling/rational design approach was further explored on an omega-transaminase from Chromobacterium violaceum.
Place, publisher, year, edition, pages
Elsevier, 2010. Vol. 150, S123-S124 p.
Biocatalysis, Enzymology, Chiral amine, Transamination
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:kth:diva-33225DOI: 10.1016/j.jbiotec.2010.08.321ISI: 000288873400303OAI: oai:DiVA.org:kth-33225DiVA: diva2:416511
14th International Biotechnology Symposium and Exhibition (IBS-2008) Rimini, ITALY SEP 14-18, 2010
QC 201105122011-05-122011-05-022016-04-18Bibliographically approved