Insights into the substrate selectivity of Bambusa oldhamii phenylalanine ammonia-lyase 1 and 2 through mutational analysis

Hightlight [Display omitted] The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type...

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Bibliographic Details
Published in:Phytochemistry letters 2020-08, Vol.38, p.140-143
Main Authors: Hsieh, Chun-Yen, Huang, Yi-Hao, Lin, Zhih-Yu, Hsieh, Lu-Sheng
Format: Article
Language:English
Subjects:
Bambusa oldhamii
Phenylalanine ammonia-lyase
phenylalanine/tyrosine ammonia-lyase
Site-directed mutagenesis
Substrate selectivity
Tyrosine ammonia-lyase
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Summary:Hightlight [Display omitted] The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, Km and kcat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased kcat/Km values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity.
ISSN:1874-3900
1876-7486
DOI:10.1016/j.phytol.2020.06.002