Reassessment of the catalytic activity and substrate specificity of fkbp35 from plasmodium knowlesi using protease-free assay

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Reassessment of the catalytic activity and substrate specificity of fkbp35 from plasmodium knowlesi using protease-free assay

FK506-binding protein35 of Plasmodium knowlesi (Pk-FKBP35) is a member of peptidyl prolyl cis-trans isomerase (PPIase) and is considered as a promising avenue of antimalarial drug target development. This protein is organized into the N-terminal domain responsible for PPIase catalytic activity follo...

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Bibliographic Details
Main Authors:	Budiman, Cahyo, Goh, Carlmond Kah Wun, Lee, Ping Chin, Razali, Rafida, Thean, Chor Leow
Format:	Article
Published:	Universiti Malaysia Sabah 2020
Online Access:	http://psasir.upm.edu.my/id/eprint/87406/

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