Preliminary noteThe 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 BiotechnologyCitation 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 EnzymesEnterokinase (enteropeptidase): comparative aspects
1989, Trends in Biochemical SciencesTrypsin
1971, EnzymesRegulation of Peptidase Activity beyond the Active Site in Human Health and Disease
2023, International Journal of Molecular Sciences
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