Colipase

Last updated
CLPS
Pancreatic lipase-colipase complex with inhibitor 1LPB.png
Identifiers
Aliases CLPS , entrez:1208, colipase
External IDs OMIM: 120105 MGI: 88421 HomoloGene: 1383 GeneCards: CLPS
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001832
NM_001252597
NM_001252598

NM_025469
NM_001317065

RefSeq (protein)

NP_001239526
NP_001239527
NP_001823

NP_001303994
NP_079745

Location (UCSC) Chr 6: 35.79 – 35.8 Mb Chr 17: 28.78 – 28.78 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Colipase, abbreviated CLPS, 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.

Contents

In humans, the colipase protein is encoded by the CLPS gene. [5]

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 hydrolysis. 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 of its binding site. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture. [6] [7]

Colipase is a small protein (12K) 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. [7]

Colipase N-terminal domain
PDB 1lpb EBI.jpg
Structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. [8]
Identifiers
SymbolColipase
Pfam PF01114
InterPro IPR001981
PROSITE PDOC00111
SCOP2 1lpb / SCOPe / SUPFAM
CDD cd00039
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
PDB 1eth , 1lpa , 1lpb , 1n8s , 1pcn , 1pco
Colipase C-terminal domain
PDB 1pcn EBI.jpg
solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr
Identifiers
SymbolColipase_C
Pfam PF02740
InterPro IPR017914
PROSITE PDOC00111
SCOP2 1lpb / SCOPe / SUPFAM
CDD cd00039
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

See also

Related Research Articles

<span class="mw-page-title-main">Lipoprotein lipase</span> Mammalian protein found in Homo sapiens

Lipoprotein lipase (LPL) (EC 3.1.1.34, systematic name triacylglycerol acylhydrolase (lipoprotein-dependent)) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. It is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule:

<span class="mw-page-title-main">Perilipin-1</span> Protein in humans

Perilipin, also known as lipid droplet-associated protein, perilipin 1, or PLIN, is a protein that, in humans, is encoded by the PLIN gene. The perilipins are a family of proteins that associate with the surface of lipid droplets. Phosphorylation of perilipin is essential for the mobilization of fats in adipose tissue.

<span class="mw-page-title-main">Hormone-sensitive lipase</span> Enzyme

Hormone-sensitive lipase (EC 3.1.1.79, HSL), also previously known as cholesteryl ester hydrolase (CEH), sometimes referred to as triacylglycerol lipase, is an enzyme that, in humans, is encoded by the LIPE gene, and catalyzes the following reaction:

<span class="mw-page-title-main">Hepatic lipase</span> Mammalian protein found in Homo sapiens

Hepatic lipase (HL), also called hepatic triglyceride lipase (HTGL) or LIPC (for "lipase, hepatic"), is a form of lipase, catalyzing the hydrolysis of triacylglyceride. Hepatic lipase is coded by chromosome 15 and its gene is also often referred to as HTGL or LIPC. Hepatic lipase is expressed mainly in liver cells, known as hepatocytes, and endothelial cells of the liver. The hepatic lipase can either remain attached to the liver or can unbind from the liver endothelial cells and is free to enter the body's circulation system. When bound on the endothelial cells of the liver, it is often found bound to heparan sulfate proteoglycans (HSPG), keeping HL inactive and unable to bind to HDL (high-density lipoprotein) or IDL (intermediate-density lipoprotein). When it is free in the bloodstream, however, it is found associated with HDL to maintain it inactive. This is because the triacylglycerides in HDL serve as a substrate, but the lipoprotein contains proteins around the triacylglycerides that can prevent the triacylglycerides from being broken down by HL.

<span class="mw-page-title-main">Gastric lipase</span> Class of enzymes

Gastric lipase, also known as LIPF, is an enzymatic protein that, in humans, is encoded by the LIPF gene.

<span class="mw-page-title-main">Bile salt-dependent lipase</span> Mammalian protein found in Homo sapiens

Bile salt-dependent lipase, also known as carboxyl ester lipase is an enzyme produced by the adult pancreas and aids in the digestion of fats. Bile salt-stimulated lipase is an equivalent enzyme found within breast milk. BSDL has been found in the pancreatic secretions of all species in which it has been looked for. BSSL, originally discovered in the milk of humans and various other primates, has since been found in the milk of many animals including dogs, cats, rats, and rabbits.

<span class="mw-page-title-main">PLAT domain</span>

In molecular biology the PLAT domain is a protein domain that is found in a variety of membrane or lipid associated proteins. It is called the PLAT domain or LH2 domain. The known structure of pancreatic lipase shows this domain binds to procolipase Pfam PF01114, which mediates membrane association.

<span class="mw-page-title-main">Microsomal triglyceride transfer protein</span>

Microsomal triglyceride transfer protein large subunit is a protein that in humans is encoded by the MTTP gene.

<span class="mw-page-title-main">PLA2G1B</span> Protein-coding gene in the species Homo sapiens

Phospholipase A2, group 1B is an enzyme that in humans is encoded by the PLA2G1B gene.

<span class="mw-page-title-main">PHKG1</span> Protein-coding gene in the species Homo sapiens

Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform is an enzyme that in humans is encoded by the PHKG1 gene.

<span class="mw-page-title-main">FABP6</span> Mammalian protein found in Homo sapiens

Fatty acid binding protein 6, ileal (gastrotropin), also known as FABP6, is a protein which in humans is encoded by the FABP6 gene.

<span class="mw-page-title-main">Adipose triglyceride lipase</span> Mammalian protein found in Homo sapiens

Adipose triglyceride lipase, also known as patatin-like phospholipase domain-containing protein 2 and ATGL, is an enzyme that in humans is encoded by the PNPLA2 gene. ATGL catalyses the first reaction of lipolysis, where triacylglycerols are hydrolysed to diacylglycerols.

<span class="mw-page-title-main">GP2 (gene)</span> Protein-coding gene in the species Homo sapiens

Pancreatic secretory granule membrane major glycoprotein GP2 is a protein that in humans is encoded by the GP2 gene.

<span class="mw-page-title-main">TPK1</span> Protein-coding gene in the species Homo sapiens

Thiamin pyrophosphokinase 1 is an enzyme that in humans is encoded by the TPK1 gene.

<span class="mw-page-title-main">Pancreatic lipase family</span> Mammalian protein found in Homo sapiens

Triglyceride lipases are a family of lipolytic enzymes that hydrolyse ester linkages of triglycerides. Lipases are widely distributed in animals, plants and prokaryotes.

<span class="mw-page-title-main">ANGPTL3</span> Protein-coding gene in the species Homo sapiens

Angiopoietin-like 3, also known as ANGPTL3, is a protein that in humans is encoded by the ANGPTL3 gene.

<span class="mw-page-title-main">LYPLA1</span> Protein-coding gene in the species Homo sapiens

Acyl-protein thioesterase 1 is an enzyme that in humans is encoded by the LYPLA1 gene.

<span class="mw-page-title-main">Lipase</span> Class of enzymes which cleave fats via hydrolysis

In biochemistry, lipase refers to a class of enzymes that catalyzes the hydrolysis of fats. Some lipases display broad substrate scope including esters of cholesterol, phospholipids, and of lipid-soluble vitamins and sphingomyelinases; however, these are usually treated separately from "conventional" lipases. Unlike esterases, which function in water, lipases "are activated only when adsorbed to an oil–water interface". Lipases perform essential roles in digestion, transport and processing of dietary lipids in most, if not all, organisms.

<span class="mw-page-title-main">Stomatin</span> Mammalian protein found in Homo sapiens

Stomatin also known as human erythrocyte integral membrane protein band 7 is a protein that in humans is encoded by the STOM gene.

<span class="mw-page-title-main">Triacylglycerol lipase</span>

The enzyme triacylglycerol lipase (also triglyceride lipase, EC 3.1.1.3;systematic name triacylglycerol acylhydrolase) catalyses the hydrolysis of ester linkages of triglycerides:

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000137392 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024225 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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.
  6. 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.
  7. 1 2 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.
  8. 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.

Further reading

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