Literature DB >> 29453991

Identification of branched-chain amino acid aminotransferases active towards (R)-(+)-1-phenylethylamine among PLP fold type IV transaminases.

Ekaterina Yu Bezsudnova1, Daria V Dibrova2, Alena Yu Nikolaeva3, Tatiana V Rakitina3, Vladimir O Popov3.   

Abstract

New class IV transaminases with activity towards L-Leu, which is typical of branched-chain amino acid aminotransferases (BCAT), and with activity towards (R)-(+)-1-phenylethylamine ((R)-PEA), which is typical of (R)-selective (R)-amine:pyruvate transaminases, were identified by bioinformatics analysis, obtained in recombinant form, and analyzed. The values of catalytic activities in the reaction with L-Leu and (R)-PEA are comparable to those measured for characteristic transaminases with the corresponding specificity. Earlier, (R)-selective class IV transaminases were found to be active, apart from (R)-PEA, only with some other (R)-primary amines and D-amino acids. Sequences encoding new transaminases with mixed type of activity were found by searching for changes in the conserved motifs of sequences of BCAT by different bioinformatics tools.
Copyright © 2018 Elsevier B.V. All rights reserved.

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Keywords:  (R)-(+)-1-phenylethylamine; (R)-selectivity; Bioinformatics analysis; Branched-chain amino acid aminotransferases

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Year:  2018        PMID: 29453991     DOI: 10.1016/j.jbiotec.2018.02.005

Source DB:  PubMed          Journal:  J Biotechnol        ISSN: 0168-1656            Impact factor:   3.307


  1 in total

1.  Identification, Characterization, and Site-Specific Mutagenesis of a Thermostable ω-Transaminase from Chloroflexi bacterium.

Authors:  Chen Wang; Kexin Tang; Ya Dai; Honghua Jia; Yan Li; Zhen Gao; Bin Wu
Journal:  ACS Omega       Date:  2021-06-25
  1 in total

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