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Cryo-EM structures reveal the activation and substrate recognition mechanism of human enteropeptidase.
Nat Commun
November 2022
Department of Gastroenterology, Changhai Hospital, Navy/Second Military Medical University, Shanghai, China.
Enteropeptidase (EP) initiates intestinal digestion by proteolytically processing trypsinogen, generating catalytically active trypsin. EP dysfunction causes a series of pancreatic diseases including acute necrotizing pancreatitis. However, the molecular mechanisms of EP activation and substrate recognition remain elusive, due to the lack of structural information on the EP heavy chain.
View Article and Find Full Text PDFThe Global Status and Trends of Enteropeptidase: A Bibliometric Study.
Front Med (Lausanne)
February 2022
Department of Gastroenterology, Changhai Hospital, Naval Medical University, Shanghai, China.
Background: Enteropeptidase (EP) is a type II transmembrane serine protease and a physiological activator of trypsinogen. Extensive studies related to EP have been conducted to date. However, no bibliometric analysis has systematically investigated this theme.
View Article and Find Full Text PDFRecombinant Production of Bovine Enteropeptidase Light Chain in SHuffle® T7 Express and Optimization of Induction Parameters.
Protein J
December 2021
Cellular and Molecular Research Center, Birjand University of Medical Sciences, Birjand, Iran.
Enteropeptidase is a duodenum serine protease that triggers the activation of pancreatic enzymes by remarkably specific cleavages after lysine residues of peptidyl substrate (Asp)-Lys. This high specific cleavage makes the enzyme a widely used biotechnological tool in laboratory researches and industrial scale. Previous studies both in small and large scales were showed low expression and miss-folding of the expressed protein.
View Article and Find Full Text PDFA combination strategy of solubility enhancers for effective production of soluble and bioactive human enterokinase.
J Biotechnol
November 2021
Department of Biochemistry, Kangwon National University, Chuncheon 24341, South Korea; Institute of Life Sciences (ILS), Kangwon National University, Chuncheon 24341, South Korea; Global/Gangwon Innovative Biologics-Regional Leading Research Center (GIB-RLRC), Kangwon National University, Chuncheon 24341, South Korea. Electronic address:
Enterokinase is one of the hydrolases that catalyze hydrolysis to regulate biological processes in intestinal visceral mucosa. Enterokinase plays an essential role in accelerating the process of protein digestion as it converts trypsinogen into active trypsin by accurately recognizing and cleaving a specific peptide sequence, (Asp)4-Lys. Due to its exceptional substrate specificity, enterokinase is widely used as a versatile molecular tool in various bioprocessing, especially in removing fusion tags from recombinant proteins.
View Article and Find Full Text PDFSite-specific, covalent immobilization of an engineered enterokinase onto magnetic nanoparticles through transglutaminase-catalyzed bioconjugation.
Colloids Surf B Biointerfaces
May 2019
School of Pharmacy, Weifang Medical University, Weifang 261053, Shandong Province, China. Electronic address:
Enterokinase (EK) is one of the most popular enzymes for the in vitro cleavage of fusion proteins due to its high degree of specificity for the amino-acid sequence (Asp)-Lys. Enzyme reusability is desirable for reducing operating costs and facilitating the industrial application of EK. In this work, we report the controlled, site-specific and covalent cross-linking of an engineered EK on amine-modified magnetic nanoparticles (NH-MNPs) via microbial transglutaminase-catalyzed bioconjugation for the development of the oriented-immobilized enzyme, namely, EK@NH-MNP biocatalyst.
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