Fluorescence-based high-throughput screening system for R-ω-transaminase engineering and its substrate scope extension View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2020-02-17

AUTHORS

Feng Cheng, Xiu-Ling Chen, Chao Xiang, Zhi-Qiang Liu, Ya-Jun Wang, Yu-Guo Zheng

ABSTRACT

ω-Transaminase (ω-TA) is an attractive alternative to metal catalysts for the stereoselective amination of prochiral ketones. The narrow substrate scope of an R-ω-transaminase from Mycobacterium vanbaalenii (MvTA) limits its application in R-amine synthesis. A fluorescence-based TA activity screening system was developed to extend its substrate scope. The reactions were conducted in microtiter plates (MTPs) and displayed low background interference, high sensitivity (μM magnitude), and a wide dynamic range (ɀ-factor > 0.9). A KnowVolution campaign was performed on this enzyme, and screening ~ 8000 clones with this fluorescence-based screening system resulted in two beneficial substitutions (G68Y and F129A) and three improved variants (M3, M4, and M5). The best variant, MvTA M5 (WT+G68Y+F129A), achieved the highest catalytic efficiency (toward fluorogenic substrate NMA) which was 3.2-fold higher than that of the WT enzyme. MvTA M5 exhibited significantly enhanced activity toward six different prochiral ketones with e.e. > 99% (R). The specific activity of MvTA M5 was more than 100 times higher than that of the WT enzyme toward acetonaphthone (M5: 8.1 U/mg, WT: ~ 0.07 U/mg), and it showed the highest activity on acetonaphthone, p-ethylacetophenone, and phenylacetone. More... »

PAGES

2999-3009

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00253-020-10444-y

DOI

http://dx.doi.org/10.1007/s00253-020-10444-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1124905303

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/32064550


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