Adipocyte Triglyceride Lipase
| Adipocyte Triglyceride Lipase | ||
|---|---|---|
| other names |
ATGL, Patatin-like phospholipase domain containing protein 2, PNPLA2 |
|
| Mass / length primary structure | 504 amino acids , 55,330 Da | |
| Identifier | ||
| External IDs | ||
| Enzyme classification | ||
| EC, category | 3.1.1.3 | |
| Orthologue (human) | ||
| Entrez | 57104 | |
| Ensemble | ENSG00000177666 | |
| UniProt | L7NSP5 | |
| Refseq (mRNA) | NM_020376.3 | |
| Refseq (protein) | NP_065109.1 | |
| PubMed search |
57104
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The adipocyte triglyceride lipase (ATGL, synonym patatin-like phospholipase domain containing protein 2 ) is an enzyme from the metabolism of lipids .
properties
As a lipase, ATGL hydrolyzes triacylglycerides to fatty acids and diacylglycerides , less diacylglycerides, phospholipids and it also has hardly any transacylase activity. It hydrolyzes preferentially at the sn2 position, whereby 1,3-diacylglycerides and free fatty acids are formed from triacylglycerides. The reaction is the slowest and rate-limiting step in lipolysis . It is mainly formed in adipose tissue but also in the skeletal muscles and in the heart . The lipase protein domain is homologous to the lipase protein domain of the most abundant soluble protein in potatoes, patatin . The amino acids serine at position 47 and aspartic acid at position 166 form the catalytic center of the ATGL. At positions 45 and 49 are conserved glycines . ATGL is inhibited by the protein G0S2 . Furthermore, ATGL binds to CGI-58. The ATGL is activated by phosphorylation at the serine at position 406.
A deletion of the ATGL leads in mice to insufficient cold adaptation and to premature death due to excessive storage of triglycerides in the heart muscle.
Web links
Individual evidence
- ↑ a b G. Wölkart, A. Schrammel, K. Dörffel, G. Haemmerle, R. Zechner, B. Mayer: Cardiac dysfunction in adipose triglyceride lipase deficiency: treatment with a PPAR agonist. In: British journal of pharmacology. Volume 165, number 2, January 2012, pp. 380-389, doi : 10.1111 / j.1476-5381.2011.01490.x , PMID 21585347 , PMC 3268192 (free full text).
- ↑ a b c d e f g h S. G. Young, R. Zechner: Biochemistry and pathophysiology of intravascular and intracellular lipolysis. In: Genes & development. Volume 27, number 5, March 2013, pp. 459-484, doi : 10.1101 / gad.209296.112 , PMID 23475957 , PMC 3605461 (free full text).
- ↑ G. Haemmerle, A. Lass, R. Zimmermann, G. Gorkiewicz, C. Meyer, J. Rozman, G. Heldmaier, R. Maier, C. Theussl, S. Eder, D. Kratky, EF Wagner, M. Klingenspor, G. Hoefler, R. Zechner: Defective lipolysis and altered energy metabolism in mice lacking adipose triglyceride lipase. In: Science. Volume 312, number 5774, May 2006, pp. 734-737, doi : 10.1126 / science.1123965 , PMID 16675698 .
- ^ R. Zimmermann, JG Strauss, G. Haemmerle, G. Schoiswohl, R. Birner-Gruenberger, M. Riederer, A. Lass, G. Neuberger, F. Eisenhaber, A. Hermetter, R. Zechner: Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. In: Science. Volume 306, Number 5700, November 2004, pp. 1383-1386, doi : 10.1126 / science.1100747 , PMID 15550674 .