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Colipase is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides.

In humans, the colipase protein is encoded by the CLPS gene.^[1]

Protein domain

Colipase is also a family of evolutionarily related proteins.

Colipase is a small protein cofactor needed by pancreatic lipase for efficient dietary lipid hydrolyisis. Efficient absorption of dietary fats is dependent on the action of pancreatic triglyceride lipase. Colipase binds to the C-terminal, non-catalytic domain of lipase, thereby stabilising an active conformation and considerably increasing the hydrophobicity binding site. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture.^[2]^[3]

Colipase is a small protein with five conserved disulphide bonds. Structural analogies have been recognised between a developmental protein (Dickkopf), the pancreatic lipase C-terminal domain, the N-terminal domains of lipoxygenases and the C-terminal domain of alpha-toxin. These non-catalytic domains in the latter enzymes are important for interaction with membrane. It has not been established if these domains are also involved in eventual protein cofactor binding as is the case for pancreatic lipase.^[3]

Colipase C-terminal domain

solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr

Identifiers

Symbol

Colipase_C

Pfam

PF02740

InterPro

IPR017914

PROSITE

PDOC00111

SCOP

1lpb

SUPERFAMILY

1lpb

CDD

cd00039

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

References

^ Davis RC, Xia YR, Mohandas T, Schotz MC, Lusis AJ (May 1991). "Assignment of the human pancreatic colipase gene to chromosome 6p21.1 to pter". Genomics 10 (1): 262–5. doi:10.1016/0888-7543(91)90509-D. PMID 2045105.
^ Lowe ME (1997). "Structure and function of pancreatic lipase and colipase". Annu. Rev. Nutr. 17: 141–158. doi:10.1146/annurev.nutr.17.1.141. PMID 9240923.
^ ^a ^b Verger R, van Tilbeurgh H, Cambillau C, Bezzine S, Carriere F (1999). "Colipase: structure and interaction with pancreatic lipase". Biochim. Biophys. Acta 1441 (2–3): 173–184. doi:10.1016/s1388-1981(99)00149-3. PMID 10570245.
^ Egloff MP, Marguet F, Buono G, Verger R, Cambillau C, van Tilbeurgh H (March 1995). "The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate". Biochemistry 34 (9): 2751–62. doi:10.1021/bi00009a003. PMID 7893686.

External links

Colipases at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the public domain Pfam and InterPro IPR001981

This enzyme-related article is a stub. You can help Wikipedia by expanding it.

UpToDate Contents

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English Journal

A model for the structure and mechanism of action of pulmonary surfactant protein B.

Olmeda B1, García-Álvarez B1, Gómez MJ1, Martínez-Calle M1, Cruz A1, Pérez-Gil J2.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology.FASEB J.2015 Jun 18. pii: fj.15-273458. [Epub ahead of print]
Surfactant protein B (SP-B), from the saposin-like family of proteins, is essential to facilitate the formation and proper performance of surface active films at the air-liquid interface of mammalian lungs, and lack of or deficiency in this protein is associated with lethal respiratory failure. Desp
PMID 26089319

Rapid analysis of colipase gene variants by multicapillary electrophoresis.

Jaczó Z1, Pál E1, Dénes R1, Somogyi A2, Sasvári-Székely M1, Guttman A3,4, Rónai Z1.
Electrophoresis.Electrophoresis.2015 Jun;36(11-12):1237-43. doi: 10.1002/elps.201400551. Epub 2015 Mar 12.
Despite of the fact that the Human Genome Project was completed more than a decade ago, identification of the genetic background of polygenic diseases is still challenging. Several somewhat different approaches are available to investigate inheritable factors of complex phenotypes, all require, howe
PMID 25502231

Biochemical Characterization and Molecular Modeling of Pancreatic Lipase from a Cartilaginous Fish, the Common Stingray (Dasyatis pastinaca).

Bouchaâla E1, BouAli M, Ben Ali Y, Miled N, Gargouri Y, Fendri A.
Applied biochemistry and biotechnology.Appl Biochem Biotechnol.2015 May;176(1):151-69. doi: 10.1007/s12010-015-1564-8. Epub 2015 Mar 21.
In order to identify fish enzymes displaying novel biochemical properties, we have chosen the common stingray (Dasyatis pastinaca), one of the most primitive living jawed aquatic vertebrates as a starting biological material to purify a lipase. A stingray pancreatic lipase (SPL) was purified from de
PMID 25795061

Japanese Journal

Effects of Colipase, Bile Salts, Na^+, and Ca^<2+> on Pancreatic Lipase Activity

Naka Yasuhiro,Nakamura Teruo
Bioscience, Biotechnology, and Biochemistry 58(11), 2121-2122, 1994-11-23
… Unlike Borgstrom's theory that pancreatic colipase overcame the inhibition of pancreatic lipase activity caused by bile salts in tributyrin, pancreatic lipase activity in triolein was activated by bile salts and synergistically accelerated by colipase in the presence of NaCl and CaCl_2. …
NAID 110002677300

Procedures of amino acid sequencing of peptides in natural proteins collection of knowledge and intelligence for construction of reliable chemical inference system

Kudo Yoshihiro,Kanaya Shigehiko
山形大学紀要. 工学 23(1), 39-54, 1994-01-31
… bottoromycin A 2, A19009, galantin I, vancomycin, stenothricin, calf speleen profilin, neocarzinostatin, pancreatic spasmolytic polypeptide, cerebratulus toxin B-IV, RNAase U 2, ferredoxin II, SKO-III, bovine serum albumin, bovine pancrea DNase, porcine, bancreatic colipase, smallest unit of beef heart bc1 complex, papaya mosaic virus coat protein, human erythrocyte 2, 3-bisphosphoglycerate mutase, sialoglycoprotein D (glycophorin C), acidic phosphopase A 2, human big gastrin I, neuroparisons, bucillus subtillis glucose permease, His-rich …
NAID 110000354576

Related Pictures

lipase, complex with colipase from Pig complexe triaglylcérol lipase & colipase Pancreatic lipase–colipase complex with lagern sich mit Hilfe einer Colipase /COLIPASE COMPLEX ACTIVATIONBY A MICELLE Pancreatic lipase, complex with colipase of colipase is unknown. Chapitre 9 - Le suc pancréatique

★リンクテーブル★

リンク元	「膵リパーゼ」「コリパーゼ」

「膵リパーゼ」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Colipase N-terminal domain
	Structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate.
Identifiers
Symbol	Colipase
Pfam	PF01114
InterPro	IPR001981
PROSITE	PDOC00111
SCOP	1lpb
SUPERFAMILY	1lpb
CDD	cd00039
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Colipase, pancreatic
	Cartoon diagram of pig colipase (blue) in complex with human pancreatic lipase and a small molecule inhibitor. From PDB: 1LPB.
Identifiers
Symbol	CLPS
External IDs	OMIM: 120105 MGI: 88421 HomoloGene: 1383 GeneCards: CLPS Gene
Gene ontology
Molecular function	• enzyme activator activity;
Cellular component	• extracellular region; • extracellular exosome;
Biological process	• retinoid metabolic process; • lipid metabolic process; • phototransduction, visible light; • post-embryonic development; • lipid catabolic process; • response to food; • positive regulation of catalytic activity; • lipid digestion; • small molecule metabolic process;
	Sources: Amigo / QuickGO
Orthologs
	v; t; e;