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Chromobacterium vio...
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Cassimjee, Karim EngelmarkKTH,Biokemi
(author)
Chromobacterium violaceum omega-transaminase variant Trp60Cys shows increased specificity for (S)-1-phenylethylamine and 4 '-substituted acetophenones, and follows Swain-Lupton parameterisation
- Article/chapterEnglish2012
Publisher, publication year, extent ...
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Royal Society of Chemistry (RSC),2012
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printrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:kth-99250
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https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-99250URI
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https://doi.org/10.1039/c2ob25893eDOI
Supplementary language notes
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Language:English
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Summary in:English
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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QC 20120724
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For biocatalytic production of pharmaceutically important chiral amines the.-transaminase enzymes have proven useful. Engineering of these enzymes has to some extent been accomplished by rational design, but mostly by directed evolution. By use of a homology model a key point mutation in Chromobacterium violaceum omega-transaminase was found upon comparison with engineered variants from homologous enzymes. The variant Trp60Cys gave increased specificity for (S)-1-phenylethylamine (29-fold) and 4'-substituted acetophenones (similar to 5-fold). To further study the effect of the mutation the reaction rates were Swain-Lupton parameterised. On comparison with the wild type, reactions of the variant showed increased resonance dependence; this observation together with changed pH optimum and cofactor dependence suggests an altered reaction mechanism.
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Added entries (persons, corporate bodies, meetings, titles ...)
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Humble, Maria SvedendahlKTH,Biokemi(Swepub:kth)u1mmbr9s
(author)
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Land, HenrikKTH,Biokemi(Swepub:kth)u13t7x1r
(author)
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Abedi, Vahak
(author)
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Berglund, PerKTH,Biokemi(Swepub:kth)u1271chh
(author)
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KTHBiokemi
(creator_code:org_t)
Related titles
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In:Organic and biomolecular chemistry: Royal Society of Chemistry (RSC)10:28, s. 5466-54701477-05201477-0539
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