Characterization of ( R )-selective amine transaminases identified by in silico motif sequence blast
Gespeichert in:
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)
Online Zugang:
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 605499314 | ||
| 003 | CHVBK | ||
| 005 | 20210128100550.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 210128e20150301xx s 000 0 eng | ||
| 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 | ||