Triacylglycerol lipase
{{Short description|Enzyme catalyst}}
{{Infobox enzyme
| Name = Triacylglycerol lipase
| EC_number = 3.1.1.3
| CAS_number = 9001-62-1
| GO_code =
| image =
| width =
| caption =
}}
{{Infobox protein family
| Symbol = Lipase_3
| Name = Lipase (class 3)
| image = PDB 3tgl EBI.jpg
| width =
| caption = Structure of Triacyl-glycerol acylhydrolase.
| Pfam= PF01764
| InterPro= IPR002921
| SMART=
| PROSITE = PDOC00110
| SCOP = 3tgl
| TCDB =
| CDD = cd00519
| OPM family= 127
| OPM protein= 3tgl
| PDB=
}}
The enzyme triacylglycerol lipase (also triglyceride lipase, EC 3.1.1.3;systematic name triacylglycerol acylhydrolase) catalyses the hydrolysis of ester linkages of triglycerides:{{cite journal |vauthors=Chapus C, Rovery M, Sarda L, Verger R |title=Minireview on pancreatic lipase and colipase |journal=Biochimie |volume=70 |issue=9 |pages=1223–1234 |year=1988 |pmid=3147715 |doi=10.1016/0300-9084(88)90188-5}}
: triacylglycerol + H2O {{eqm}} diacylglycerol + a carboxylate
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.{{cite journal | vauthors = Korn ED, Quigley TW | title = Lipoprotein lipase of chicken adipose tissue | journal = The Journal of Biological Chemistry | volume = 226 | issue = 2 | pages = 833–9 | date = June 1957 | doi = 10.1016/S0021-9258(18)70867-3 | pmid = 13438870 | doi-access = free }}{{cite journal | vauthors = Lynn WS, Perryman NC | title = Properties and purification of adipose tissue lipase | journal = The Journal of Biological Chemistry | volume = 235 | pages = 1912–6 | date = July 1960 | issue = 7 | doi = 10.1016/S0021-9258(18)69335-4 | pmid = 14419169 | doi-access = free }}{{cite journal | vauthors = Sarda L, Desnuelle P | title = [Actions of pancreatic lipase on esters in emulsions] | journal = Biochimica et Biophysica Acta | volume = 30 | issue = 3 | pages = 513–21 | date = December 1958 | pmid = 13618257 | doi = 10.1016/0006-3002(58)90097-0 }}{{cite journal | title = Studies on wheat germ lipase. I. Methods of estimation, purification and general properties of the enzyme |author1 = Singer, T.P. |author2 =Hofstee, B.H.J. |journal = Arch. Biochem. |date = 1948 |volume = 18 |issue = 2 |pages = 229–243 |pmid = 18875045}}{{cite journal | title = Studies on wheat germ lipase. II. Kinetics |author1 = Singer, T.P. |author2 =Hofstee, B.H.J. |journal = Arch. Biochem. |date = 1948 |volume = 18 |issue = 2 |pages = 245–259 |pmid = 18875046}}
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
References
{{reflist}}
External links
- {{MeshName|Triacylglycerol+lipase}}
{{Esterases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}
{{InterPro content|IPR002921}}