Structural insight into the substrate specificity of PLP fold type IV transaminases
Author:
Funder
Russian Science Foundation
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Biotechnology
Link
http://link.springer.com/content/pdf/10.1007/s00253-020-10369-6.pdf
Reference93 articles.
1. Amorim Franco TM, Hegde S, Blanchard JS (2016) Chemical mechanism of the branched-chain aminotransferase IlvE from Mycobacterium tuberculosis. Biochemistry 55:6295–6303. https://doi.org/10.1021/acs.biochem.6b00928
2. Barber JEB, Damry AM, Calderini GF, Walton CJW, Chica RA (2014) Continuous colorimetric screening assay for detection of d-amino acid aminotransferase mutants displaying altered substrate specificity. Anal Biochem 463:23–30. https://doi.org/10.1016/j.ab.2014.06.006
3. Bezsudnova EY, Boyko KM, Nikolaeva AY, Zeifman YS, Rakitina TV, Suplatov DA, Popov VO (2019) Biochemical and structural insights into PLP fold type IV transaminase from Thermobaculum terrenum. Biochimie 158:130–138. https://doi.org/10.1016/j.biochi.2018.12.017
4. Bezsudnova EY, Boyko KM, Popov VO (2017) Properties of bacterial and archaeal branched-chain amino acid aminotransferases. Biochemistry (Mosc) 82:1572–1591. https://doi.org/10.1134/S0006297917130028
5. Bezsudnova EY, Dibrova DV, Nikolaeva AY, Rakitina TV, Popov VO (2018) Identification of branched-chain amino acid aminotransferases active towards (R)-(+)-1-phenylethylamine among PLP fold type IV transaminases. J Biotechnol 271:26–28. https://doi.org/10.1016/j.jbiotec.2018.02.005
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