Preliminary note
The action of enterokinase on trypsinogen

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  • A combination strategy of solubility enhancers for effective production of soluble and bioactive human enterokinase

    2021, Journal of Biotechnology
    Citation Excerpt :

    Enterokinase, also known as enteropeptidase, belongs to a class of serine proteases and is a disulfide-linked heterodimeric enzyme, composed of a heavy chain (87 kDa) and a light chain (26 kDa) (Kitamoto et al., 1994). In the small intestine, enterokinase is mainly produced in the duodenal brush borders for activation of the digestive system by converting proenzyme trypsinogen into active proteolytic enzyme, trypsin (Lobley et al., 1973; Yamashina, 1956). Interestingly, the light chain of enterokinase exhibits a remarkable target specificity and catalytic activity, enabling the effective recognition of a pentapeptide sequence Asp-Asp-Asp-Asp-Lys (DDDDK) and hydrolysis of the bond located after the lysine residue (Light and Janska, 1989).

  • Enteropeptidase

    2013, Handbook of Proteolytic Enzymes
  • Enterokinase (enteropeptidase): comparative aspects

    1989, Trends in Biochemical Sciences
  • Trypsin

    1971, Enzymes
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