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Results 1 - 8 of 8
EC Number
General Information
Commentary
Reference
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enterokinase shows no strict cleavage site specificity because of sporadic cleavage at other sites, which consist of acidic and basic residues
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improved efficiency of fusion proteins cleavage by enteropeptidase by substitution of the Lys residue by Arg in specific cleavage sequence (Asp)4-Lys. 3-6fold lower amounts of the catalytic subunit of enteropeptidase is required for 95% cleavage of Trx/TRAIL and Trx/FGF-2 fusions with (Asp)4-Arg cleavage sequence in comparison to native sequence (Asp)4-Lys. Reduced amount of non-specifically cleaved peptide fragments are observed during cleavage of (Asp)4-Lys/Arg mutated fusions
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low enzyme concentrations protect hippocampal neurons against the death caused by 0.1 mM glutamate, via a proteinase activated receptor PAR1-dependent mechanism, while High concentrations of the enzyme causes the death of neurons mainly through necrosis
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low enzyme light chain concentrations protect hippocampal neurons against the death caused by 0.1 mM glutamate, via a proteinase activated receptor PAR1-dependent mechanism, while high concentrations of enzyme light chain causes the death of neurons mainly through necrosis
physiological function
enteropeptidase is a serine protease secreted by the pancreas that converts inactive trypsinogen to active trypsin
physiological function
in duodenal fluid, the enzyme is responsible for causing pancreatitis in case of duodeno-pancreatic reflux
physiological function
the enzyme converts the inactive form of trypsinogen to active trypsin by endoproteolytic cleavage
physiological function
the enzyme triggers the activation of the zymogens in pancreatic juice by converting trypsinogen into trypsin
Results 1 - 8 of 8