Expanding the threonine aldolase toolbox for the asymmetric synthesis of tertiary α-amino acids

Verfasser / Beitragende:
[Kateryna Fesko, Gernot Strohmeier, Rolf Breinbauer]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/22(2015-11-01), 9651-9661
Format:
Artikel (online)
ID: 605500789
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024 7 0 |a 10.1007/s00253-015-6803-y  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-015-6803-y 
245 0 0 |a Expanding the threonine aldolase toolbox for the asymmetric synthesis of tertiary α-amino acids  |h [Elektronische Daten]  |c [Kateryna Fesko, Gernot Strohmeier, Rolf Breinbauer] 
520 3 |a The direct biochemical synthesis of tertiary α-amino acids with a wide range of diversity was recently reported using natural threonine aldolases LTA from Aeromonas jandei and DTA from Pseudomonas sp. Here, we describe the identification of five novel threonine aldolases which accept alanine and serine as amino acid donors. The enzymes were found by sequence database analysis using known aldolases as template. All enzymes were overexpressed in Escherichia coli and purified, and their biochemical properties were characterized. The new enantiocomplementary l- and d-threonine aldolases catalyze the asymmetric synthesis of β-hydroxy α-methyl- and α-hydroxymethyl-α-amino acids with good conversion and perfect enantioselectivity at α-carbon of the products (e.e. >99%). The structural basis for the broad donor specificity of these threonine aldolases is analyzed based on crystal structure alignments and amino acid sequences comparison. 
540 |a Springer-Verlag Berlin Heidelberg, 2015 
690 7 |a Threonine aldolase  |2 nationallicence 
690 7 |a Aldol reactions  |2 nationallicence 
690 7 |a Tertiary amino acids  |2 nationallicence 
690 7 |a Enzyme catalysis  |2 nationallicence 
690 7 |a Biocatalysis  |2 nationallicence 
700 1 |a Fesko  |D Kateryna  |u Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, A-8010, Graz, Austria  |4 aut 
700 1 |a Strohmeier  |D Gernot  |u Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, A-8010, Graz, Austria  |4 aut 
700 1 |a Breinbauer  |D Rolf  |u Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, A-8010, Graz, Austria  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/22(2015-11-01), 9651-9661  |x 0175-7598  |q 99:22<9651  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-015-6803-y  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00253-015-6803-y  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Fesko  |D Kateryna  |u Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, A-8010, Graz, Austria  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Strohmeier  |D Gernot  |u Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, A-8010, Graz, Austria  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Breinbauer  |D Rolf  |u Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, A-8010, Graz, Austria  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/22(2015-11-01), 9651-9661  |x 0175-7598  |q 99:22<9651  |1 2015  |2 99  |o 253