Abcam's Enterokinase Activity Assay Kit (Fluorometric) utilizes a peptide substrate containing the Enterokinase recognition sequence along with a fluorescent label ‘AFC’. Enterokinase catalyzes the cleavage of this substrate and releases the AFC molecule, which can be easily quantified by measuring its fluorescence at Ex/Em = 380/500 nm. This assay kit is simple and rapid and can detect Enterokinase activity as low as 1 mU.
Enterokinase (Enteropeptidase, EC 188.8.131.52) is a serine protease involved in activation of trypsinogen to trypsin, which in turn results in the activation of various digestive enzymes. It recognizes a highly specific amino acid sequence ‘DDDDK’ and cleaves after the lysine residue. High specific activity of Enterokinase has been utilized in cleaving a variety of native or fusion protein tags containing the above recognition motif.
Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.
Intestinal brush border.
Involvement in disease
Defects in TMPRSS15 are a cause of enterokinase deficiency (ENTKD) [MIM:226200]; a life-threatening intestinal malabsorption disorder characterized by diarrhea and failure to thrive.
Belongs to the peptidase S1 family. Contains 2 CUB domains. Contains 2 LDL-receptor class A domains. Contains 1 MAM domain. Contains 1 peptidase S1 domain. Contains 1 SEA domain. Contains 1 SRCR domain.
The chains are derived from a single precursor that is cleaved by a trypsin-like protease.