enteropeptidase
Sign in to saveEnteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of digestive enzymes from the pancreas. Absence of enteropeptidase results in intestinal digestion impairment.
Key facts
- Enzyme.Name
- enteropeptidase
- Enzyme.EC_number
- 3.4.21.9
- Enzyme.CAS_number
- 9014-74-8
- Enzyme.GO_code
- 0004275
- Enzyme.image
- 1EKB.png
- Enzyme.caption
- Crystal structure of Enteropeptidase with an inhibitor
- Protein.Name
- protease, serine, 7 (enteropeptidase)
- Protein.HGNCid
- 9490
- Protein.Symbol
- TMPRSS15
- Protein.EntrezGene
- 5651
- Protein.OMIM
- 606635
- Protein.RefSeq
- NM_002772
- Protein.UniProt
- P98073
- Protein.Chromosome
- 21
- Protein.Arm
- q
- Protein.Band
- 21
via Wikipedia infobox
Article
7 sectionsContents
- Historical significance
- Enzyme structure
- Activity
- Genetics and disease relevance
- Applications
- References
- External links
Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of digestive enzymes from the pancreas. Absence of enteropeptidase results in intestinal digestion impairment.
Enteropeptidase is a serine protease () consisting of a disulfide-linked heavy-chain of 82-140 kDa that anchors enterokinase in the intestinal brush border membrane and a light-chain of 35–62 kDa that contains the catalytic subunit. Enteropeptidase is a part of the chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.