NDLI: Improvement of the activity of arylmalonate decarboxylase by random mutagenesis

Content Provider	Springer Nature Link
Author	Terao, Y. Miyamoto, K. Ohta, H.
Copyright Year	2006
Abstract	Arylmalonate decarboxylase (EC 4.1.1.76) catalyzes enantioselective decarboxylation of α-aryl-α-methylmalonates to give optically pure α-arylpropionates. Recently, we have succeeded in creating a double mutant enzyme that gave opposite enantionmer as the product. Unfortunately, however, the activity of the mutant decreased far lower than that of the native enzyme. Thus, we performed the directed evolution of the mutant via the random mutagenesis method employing the mutator strain Escherichia coli XL1-Red. About 50,000 mutants were screened on color assay plate, and one mutant with higher activity was obtained. Gene analysis of this mutant indicated that the obtained enzyme had an S36N mutation in addition to its original G74C/C188S mutations. The activity of the triple mutant enzyme was tenfold higher than that of the starting doubly mutated enzyme.
Starting Page	647
Ending Page	653
Page Count	7
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	73
Issue Number	3
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2006-07-25
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Arylmalonate decarboxylase Random-mutagenesis XL1-Red Activity Microbial Genetics and Genomics Microbiology Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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Improvement of the activity of arylmalonate decarboxylase by random mutagenesis