Characterization of ( R )-selective amine transaminases identified by in silico motif sequence blast

Verfasser / Beitragende:
[Jinju Jiang, Xi Chen, Dalong Zhang, Qiaqing Wu, Dunming Zhu]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/6(2015-03-01), 2613-2621
Format:
Artikel (online)
ID: 605499314
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024 7 0 |a 10.1007/s00253-014-6056-1  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-014-6056-1 
245 0 0 |a Characterization of ( R )-selective amine transaminases identified by in silico motif sequence blast  |h [Elektronische Daten]  |c [Jinju Jiang, Xi Chen, Dalong Zhang, Qiaqing Wu, Dunming Zhu] 
520 3 |a Compared to (S)-selective amine transaminase ((S)-AT), the (R)-selective counterpart ((R)-AT) has been less studied. As such, a simplified "Motif Sequence Blast” search (Höhne et al. Nat Chem Biol 6:807-813, 2010) was carried out to identify new (R)-ATs from the protein databases. The combined conserved sequence motifs of (R)-ATs based on the previous in silico method of predicting (R)-selective amine transaminase were used as the template sequence for BLASTP search at default settings in NCBI, and six candidate sequences were identified. These putative (R)-AT genes were synthesized and overexpressed in Escherichia coli. Among them, five new (R)-ATs were expressed as soluble protein and showed unusual substrate specificity and high stereoselectivity. Furthermore, several unnatural amino acids, such as d-alanine, d-2-aminobutyric acid, and d-norvaline, were synthesized via the (R)-AT-catalyzed amino transfer reaction to the corresponding keto acids. Optically pure (S)-amines were also obtained by kinetic resolution of racemic amines catalyzed with these new (R)-ATs. Therefore, the Motif Sequence Blast search offers a quick and effective method for in silico identification of new (R)-ATs, and the newly identified (R)-ATs are attractive additions to the toolbox of (R)-ATs for further study and industrial application. 
540 |a Springer-Verlag Berlin Heidelberg, 2014 
690 7 |a ω-Transaminase  |2 nationallicence 
690 7 |a Chiral amine  |2 nationallicence 
690 7 |a Unnatural amino acid  |2 nationallicence 
690 7 |a Biocatalysis  |2 nationallicence 
700 1 |a Jiang  |D Jinju  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
700 1 |a Chen  |D Xi  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
700 1 |a Zhang  |D Dalong  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
700 1 |a Wu  |D Qiaqing  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
700 1 |a Zhu  |D Dunming  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/6(2015-03-01), 2613-2621  |x 0175-7598  |q 99:6<2613  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-014-6056-1  |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/s00253-014-6056-1  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Jiang  |D Jinju  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Chen  |D Xi  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Zhang  |D Dalong  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Wu  |D Qiaqing  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Zhu  |D Dunming  |u National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Center for Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 300308, Tianjin, China  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/6(2015-03-01), 2613-2621  |x 0175-7598  |q 99:6<2613  |1 2015  |2 99  |o 253