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- Svedendahl, Maria, et al.
(författare)
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CASCAT : Redesign of omega-Transaminases for Synthesis of Chiral Amines
- 2010
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Ingår i: Journal of Biotechnology. - : Elsevier. - 0168-1656 .- 1873-4863. ; 150, s. S123-S124
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- Transaminases (EC 2.6.1.18) 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.
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