Bile Salt Activated Lipase
Bile Salt Activated Lipase | ||
---|---|---|
Properties of human protein | ||
Mass / length primary structure | 722 amino acids | |
Isoforms | Long, short | |
Identifier | ||
Gene name | CEL | |
External IDs | ||
Enzyme Classifications | ||
EC, category | 3.1.1.13 , lipases | |
Response type | Ester cleavage | |
Substrate | Sterol esters + H 2 O | |
Products | Sterol + fatty acid | |
EC, category | 3.1.1.3 , lipases | |
Response type | Ester cleavage | |
Substrate | Triacylglycerol + H 2 O | |
Products | Diacylglycerol + fatty acid | |
Orthologue | ||
human | House mouse | |
Entrez | 1056 | 12613 |
Ensemble | ENSG00000170835 | ENSMUSG00000026818 |
UniProt | B4DSX9 | Q64285 |
Refseq (mRNA) | NM_001807 | NM_009885 |
Refseq (protein) | NP_001798 | NP_034015 |
Gene locus | Chr 9: 133.06 - 133.09 Mb | Chr 2: 28.56 - 28.56 Mb |
PubMed search | 1056 |
12613
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The bile salt-activated lipase (BAL) (also: carboxyl ester lipase gene -Name: CEL ) is the lipase , the ingested Cholesterinester in the small intestine of mammals in long chain fatty acids and cholesterol splits. BAL is produced in acinar cells of the pancreas and in breast milk. Mutations in the CEL gene can cause enzyme deficiencies and this, a form of hereditary diabetes mellitus .
Medically, the cholesterol-lowering effect of statins is at least partly due to an inhibition of BAL. The use of the BAL in fat sensors for the food industry has been investigated several times. Another application in the paper industry has been suggested.
Catalyzed reaction
In addition to breaking down sterol esters, BAL is able to break down triglycerides into diglycerides and fatty acids. The activity of BAL is greatly increased by the bile salts cholate , chenodeoxycholate or their adducts with glycine or taurine , as well as by dimerization.
In the toddler, the BAL also breaks down monoglycerides into glycerine and fatty acids, which is the last step in the digestion of milk fats. It is unclear whether this function has any meaning in adults.
Individual evidence
- ↑ UniProt P19835
- ↑ Swiss Institute of Bioinformatics (SIB): PROSITE documentation PDOC00112. Type B carboxylesterases. Accessed August 12, 2011 .
- ↑ D'Eustachio / reactome.org: Digestion of cholesterol esters by extracellular CEL (bile salt-dependent lipase) ( page no longer available , search in web archives ) Info: The link was automatically marked as defective. Please check the link according to the instructions and then remove this notice.
- ↑ Chiou SY, Lai GW, Lin LY, Lin G: Kinetics and mechanisms of cholesterol esterase inhibition by cardiovascular drugs in vitro . In: Indian J. Biochem. Biophys. . 43, No. 1, February 2006, pp. 52-5. PMID 16955753 .
- ↑ Singh S, Solanki PR, Pandey MK, Malhotra BD: Covalent immobilization of cholesterol esterase and cholesterol oxidase on polyaniline films for application to cholesterol biosensor . In: Anal. Chim. Acta . 568, No. 1-2, May 2006, pp. 126-32. doi : 10.1016 / j.aca.2005.10.008 . PMID 17761252 .
- ↑ Calero-Rueda O, Plou FJ, Ballesteros A, Martínez AT, Martínez MJ: Production, isolation and characterization of a sterol esterase from Ophiostoma piceae . In: Biochim. Biophys. Acta . 1599, No. 1-2, September 2002, pp. 28-35. PMID 12479402 .
- ↑ D'Eustachio / reactome.org: Digestion of monoacylglycerols by extracellular CEL (bile salt-dependent lipase) ( page no longer available , search in web archives ) Info: The link was automatically marked as defective. Please check the link according to the instructions and then remove this notice.