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K. Boyko, T. Stekhanova, A. Nikolaeva, A. Mardanov, A. Rakitin, N. Ravin, E. Bezsudnova, V. Popov (2016)
First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for l-amino acids and R-aminesExtremophiles, 20
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Y. Zeifman, K. Boyko, A. Nikolaeva, V. Timofeev, T. Rakitina, V. Popov, E. Bezsudnova (2019)
Functional characterization of PLP fold type IV transaminase with a mixed type of activity from Haliangium ochraceum.Biochimica et biophysica acta. Proteins and proteomics, 1867 6
T. Pavkov-Keller, Gernot Strohmeier, M. Diepold, W. Peeters, Natascha Smeets, Martin Schürmann, K. Gruber, H. Schwab, K. Steiner (2016)
Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme foldScientific Reports, 6
M. Gilski, Maciej Kazmierczyk, S. Krzywda, Helena Zábranská, S. Cooper, Zoran Popović, Firas Khatib, F. DiMaio, James Thompson, D. Baker, Iva Pichovác, Mariusz Jaskolskia (2011)
High-resolution structure of a retroviral protease folded as a monomer
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E. Bezsudnova, K. Boyko, A. Nikolaeva, Yulia Zeifman, T. Rakitina, D. Suplatov, V. Popov (2019)
Biochemical and structural insights into PLP fold type IV transaminase from Thermobaculum terrenum.Biochimie, 158
Fabian Steffen‐Munsberg, Clare Vickers, H. Kohls, Henrik Land, Hendrik Mallin, Alberto Nobili, L. Skalden, T. Bergh, H. Joosten, Per Berglund, M. Höhne, U. Bornscheuer (2015)
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M. Fuchs, Judith Farnberger, W. Kroutil (2015)
The Industrial Age of Biocatalytic TransaminationEuropean Journal of Organic Chemistry, 2015
Transaminases (aminotransferases) are stereospecific enzymes catalyzing the reversible amino group transfer from various substrates. Transaminases are key enzymes in amino acid metabolism in all organisms, and they show promise for fine organic synthesis. Among a diversity of transaminases, as-yet poorly characterized pyridoxal 5′-phosphate-dependent fold type IV transaminases have attracted great interest. This transaminase family shows specificity for both D- and L-amino acids and (R)-amines. The crystal structure of thermally stable fold type IV branched-chain amino acid transaminase from the archaeon Thermoproteus uzoniensis in complex with the non-natural substrate L-norvaline was established. The mechanism of substrate binding is considered. The key amino acids involved in the substrate binding are described.
Crystallography Reports – Springer Journals
Published: Sep 8, 2020
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