enterokinase


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Related to enterokinase: secretin, enterokinase deficiency

enteropeptidase

 [en″ter-o-pep´tĭ-dās]
an enzyme of the intestinal juice secreted by the duodenal mucosa; it activates the proteolytic enzyme of the pancreatic juice by converting trypsinogen into trypsin.

en·ter·o·pep·ti·dase

(en'tĕr-ō-pep'ti-dās),
An intestinal proteolytic glycoenzyme from the duodenal mucosa that converts trypsinogen into trypsin (removes a hexapeptide from trypsinogen).
Synonym(s): enterokinase

enterokinase

(ĕn′tə-rō-kī′nās′, -nāz′, -kĭn′ās′, -āz′)
n.
An enzyme secreted by the upper intestinal mucosa that catalyzes the conversion of trypsinogen to trypsin.

TMPRSS15

A gene on chromosome 21q21 that encodes a serine protease responsible for activating pancreatic proteolytic proenzymes by catalysing the conversion of trypsinogen to trypsin, which in turn activates other proenzymes, including chymotrypsinogen, procarboxypeptidases and proelastases. It is localised at the intestinal brush border.

Molecular pathology
Defects in TMPRSS15 are a cause of enterokinase deficiency.

enterokinase

See ENTEROPEPTIDASE.

enterokinase

see ENTEROPEPTIDASE.

enterokinase

) an ENZYME secreted by cells of the DUODENUM, which catalyses the conversion of inactive TRYPSINOGEN in the PANCREATIC JUICE to active TRYPSIN.
References in periodicals archive ?
(D) The fusion peptide and its cleaved forms by enterokinase. M, protein markers; Lane 1, pBD-2/cecropin P1 fusion peptide; Lane 2, pBD-2 (6 kDa) and cecropin P1 (8 kDa) peptides generated from the fusion peptide by enterokinase digestion.
By performing the previously described pilot digestion experiments, optimal cleavage was observed by using native enterokinase at protein: protease mass ratio of 1:20 after overnight incubation at room temperature.
Surprisingly, we found that the fusion proteins obtained from insect cells were resistant to enterokinase independently of the enzyme source and experimental conditions, whereas the proteins isolated from E.
However, we are more inclined to explain the enterokinase resistance of the fusion protein from insect cells with the specific posttranslational glycosylation of hIFN[gamma] proteins.
In this paper we describe the negative effect of the N-terminal [His.sub.6]-FLAG tag on the biological activity of two proteins with therapeutic application (hIFN[gamma] and its mutant K88Q) and its resistance to enterokinase digestion when the proteins are glycosylated.
Seong, "Recombinant enterokinase light chain with affinity tag: expression from Saccharomyces cerevisiae and its utilities in fusion protein technology," Biotechnology and Bioengineering, vol.
Janska, "Enterokinase (enteropeptidase): comparative aspects," Trends in Biochemical Sciences, vol.
Lim et al., "An SRLLR motif downstream ofthe scissile bond enhances enterokinase cleavage efficiency," Biochimie, vol.
Shin, "Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag," Protein Expression and Purification, vol.
Then, the fusion partner with 18 kDa, was separated from rhPTH through digestion with enterokinase (Figure 3).