Colipase
Sign in to saveAlso known as uniprot:P04118, CLPS, colipase, pancreatic, pancreatic colipase preproprotein
Colipase, abbreviated CLPS, is a protein co-enzyme that counteracts the inhibitory effect of intestinal bile acid on the enzymatic activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin.
Key facts
- Protein family.Symbol
- Colipase_C
- Protein family.Name
- Colipase C-terminal domain
- Protein family.image
- PDB 1pcn EBI.jpg
- Protein family.caption
- solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr
- Protein family.Pfam
- PF02740
- Protein family.InterPro
- IPR017914
- Protein family.PROSITE
- PDOC00111
- Protein family.SCOP
- 1lpb
- Protein family.CDD
- cd00039
- Protein family.PDB
- , , , , ,
via Wikipedia infobox
Protein · UniProt
Colipase
- Gene
- CLPS
- Organism
- Homo sapiens (Human)
- Length
- 112 aa
- Molecular mass
- 11,954 Da
- Evidence
- 1: Evidence at protein level
Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase
Swiss-Prot (reviewed) · via UniProt
Research
674 papers- Colipase: structure and interaction with pancreatic lipase.Biochimica et biophysica acta · 1999
- [Pancreatic colipase].Sheng li ke xue jin zhan [Progress in physiology] · 1992
- Minireview on pancreatic lipase and colipase.Biochimie · 1988
- Pancreatic colipase: chemistry and physiology.Journal of lipid research · 1979
- Pancreatic colipase. Structural and physiological aspects.Biochimica et biophysica acta · 1992
via PubMed
Wikidata facts
Show 1 more fact
- Commons category
- (Pro)colipase
via Wikidata · CC0
~2 min read
Article
5 sectionsContents
- Protein domain
- See also
- References
- Further reading
- External links
Colipase, abbreviated CLPS, is a protein co-enzyme that counteracts the inhibitory effect of intestinal bile acid on the enzymatic activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin.
Intestinal bile acids (which aid lipid digestion by facilitating micelle formation) adhere to the surface of emulsified fat droplets, displacing lipase (which is only active at the water-fat interface) from the droplet surface. Colipase acts as a bridging molecule, binding to both lipase and bile acids, thus anchoring lipase onto the droplet surface, preventing its displacement.