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Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light chain consists of 235 amino acid residues. The calculated molecular weight of Recombinant Human Enterokinase is 108.7 kDa.
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This gene encodes an enzyme that converts the pancreatic proenzyme trypsinogen to trypsin, which activates other proenzymes including chymotrypsinogen and procarboxypeptidases. The precursor protein is cleaved into two chains that form a heterodimer linked by a disulfide bond. This protein is a member of the trypsin family of peptidases. Mutations in this gene cause enterokinase deficiency, a malabsorption disorder characterized by diarrhea and failure to thrive. [provided by RefSeq, Jul 2008].
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Protein Aliases: Enterokinase; enterokinase catalytic subunit; Enteropeptidase; protease, serine, 7 (enterokinase); Serine protease 7; Transmembrane protease serine 15
Gene Aliases: ENTK; PRSS7; TMPRSS15
UniProt ID: (Human) P98073
Entrez Gene ID: (Human) 5651
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