Abstract
Data in this article are associated with the research article “High-throughput screening of enzyme mutants by comparison of their activity ratios to an enzyme tag” (Li et al., 2019) [1]. Data are provided on the development of a system for high-throughput (HTP) screening of mutants through the comparison of the activity ratios of an applicable enzyme and its mutants to a suitable tag enzyme in cell lysates of their fused forms, with Escherichia coli alkaline phosphatase (ECAP) as the tag fused to the N-terminus of Pseudomonas Aeruginosa arylsulfatase (PAAS) and its mutants via a flexible linker. Data were made publicly available for further analyses.
Highlights
Data for high-throughput screening of enzyme mutants by comparison of their activity ratios to an enzyme tag Yaping Li a, 1, Huimin Chong a, 1, Xiang Zhang a, Xiaolan Yang a, **, Fei Liao a, b, *
Data are provided on the development of a system for high-throughput (HTP) screening of mutants through the comparison of the activity ratios of an applicable enzyme and its mutants to a suitable tag enzyme in cell lysates of their fused forms, with Escherichia coli alkaline phosphatase (ECAP) as the tag fused to the N-terminus of Pseudomonas Aeruginosa arylsulfatase (PAAS) and its mutants via a flexible linker
Through the analyses of the data of the activities of ECAP in lysates of both Escherichia coli BL21 (DE3) transformed with a blank plasmid and host cells transformed with the fused mutants of PAAS, a rational threshold of ECAP activities in cell lysates can be developed for physical significance of the activity ratios of their fused forms at a preset confidence limit
Summary
The data in this article provides information on how to develop an experimental system for HTP screening of mutants through the comparison of the activity ratios of an applicable enzyme and its mutants to a suitable enzyme tag in cell lysates of their fused forms (Figs. 1e4 and Tables 1e7). The data in this article provides information on how to develop an experimental system for HTP screening of mutants through the comparison of the activity ratios of an applicable enzyme and its mutants to a suitable enzyme tag in cell lysates of their fused forms Supported validity of the proposed strategy and the advantage to recognize the positive mutant in each pair of PAAS/mutants during HTP screening and elucidate the sequence-activity relationship of PAAS in HTP mode (Fig. 5) (see Scheme 1). The lane of the same label in figures stood for the same sample, as follows.
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