Triacylglycerol lipase
| Triacylglycerol lipase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.3 | ||||||||
| CAS no. | 9001-62-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| Lipase (class 3) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of Triacyl-glycerol acylhydrolase. | |||||||||
| Identifiers | |||||||||
| Symbol | Lipase_3 | ||||||||
| Pfam | PF01764 | ||||||||
| InterPro | IPR002921 | ||||||||
| PROSITE | PDOC00110 | ||||||||
| SCOP2 | 3tgl / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 127 | ||||||||
| OPM protein | 3tgl | ||||||||
| CDD | cd00519 | ||||||||
| |||||||||
Triacylglycerol lipase (also Triglyceride lipase) EC 3.1.1.3, are enzymes that hydrolyse ester linkages of triglycerides.[1] These lipases are widely distributed in animals, plants and prokaryotes. This family was also called class 3 lipases as they are only distantly related to other lipase families.[2][3][4][5][6] This enzyme catalyses the following chemical reaction
- triacylglycerol + H2O ⇌ diacylglycerol + a carboxylate
Human proteins containing this domain[]
; ; ; The pancreatic enzyme acts only on an ester-water interface.
Nomenclature[]
Other names include lipase, butyrinase, tributyrinase, Tween hydrolase, steapsin, triacetinase, tributyrin esterase, Tweenase, amno N-AP, Takedo 1969-4-9, Meito MY 30, Tweenesterase, GA 56, capalase L, triglyceride hydrolase, triolein hydrolase, tween-hydrolyzing esterase, amano CE, cacordase, triglyceridase, triacylglycerol ester hydrolase, amano P, amano AP, PPL, glycerol-ester hydrolase, GEH, meito Sangyo OF lipase, hepatic lipase, lipazin, post-heparin plasma protamine-resistant lipase, salt-resistant post-heparin lipase, heparin releasable hepatic lipase, amano CES, amano B, tributyrase, triglyceride lipase, liver lipase, hepatic monoacylglycerol acyltransferase).
See also[]
- Pancreatic lipase
- Gastric lipase
- Lingual lipase
References[]
- ^ Chapus C, Rovery M, Sarda L, Verger R (1988). "Minireview on pancreatic lipase and colipase". Biochimie. 70 (9): 1223–1234. doi:10.1016/0300-9084(88)90188-5. PMID 3147715.
- ^ Korn ED, Quigley TW (June 1957). "Lipoprotein lipase of chicken adipose tissue". The Journal of Biological Chemistry. 226 (2): 833–9. doi:10.1016/S0021-9258(18)70867-3. PMID 13438870.
- ^ Lynn WS, Perryman NC (July 1960). "Properties and purification of adipose tissue lipase". The Journal of Biological Chemistry. 235 (7): 1912–6. doi:10.1016/S0021-9258(18)69335-4. PMID 14419169.
- ^ Sarda L, Desnuelle P (December 1958). "[Actions of pancreatic lipase on esters in emulsions]". Biochimica et Biophysica Acta. 30 (3): 513–21. doi:10.1016/0006-3002(58)90097-0. PMID 13618257.
- ^ Singer, T.P.; Hofstee, B.H.J. (1948). "Studies on wheat germ lipase. I. Methods of estimation, purification and general properties of the enzyme". Arch. Biochem. 18 (2): 229–243. PMID 18875045.
- ^ Singer, T.P.; Hofstee, B.H.J. (1948). "Studies on wheat germ lipase. II. Kinetics". Arch. Biochem. 18 (2): 245–259. PMID 18875046.
External links[]
- Triacylglycerol+lipase at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.1.1
- Protein domains
- Protein families
- Peripheral membrane proteins