ExplorEnz: EC 3.1.1.3

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3.1.1.3

Accepted name:

triacylglycerol lipase

Reaction:

triacylglycerol + H₂O = diacylglycerol + a carboxylate

For diagram of retinal and derivatives biosynthesis, click here

Other name(s):

lipase (ambiguous); 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; PNLIP (gene name); LIPF (gene name)

Systematic name:

triacylglycerol acylhydrolase

Comments:

The enzyme is found in diverse organisms including animals, plants, fungi, and bacteria. It hydrolyses triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. The enzyme is highly soluble in water and acts at the surface of oil droplets. Access to the active site is controlled by the opening of a lid, which, when closed, hides the hydrophobic surface that surrounds the active site. The lid opens when the enzyme contacts an oil-water interface (interfacial activation). The pancreatic enzyme requires a protein cofactor, namely colipase, to counteract the inhibitory effects of bile salts.

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-62-1

References:

1.	Singer, T.P. and Hofstee, B.H.J. Studies on wheat germ lipase. I. Methods of estimation, purification and general properties of the enzyme. Arch. Biochem. 18 (1948) 229–243. [PMID: 18875045]
2.	Singer, T.P. and Hofstee, B.H.J. Studies on wheat germ lipase. II. Kinetics. Arch. Biochem. 18 (1948) 245–259. [PMID: 18875046]
3.	Sarda, L. and Desnuelle, P. Action de la lipase pancréatique sur les esters en émulsion. Biochim. Biophys. Acta 30 (1958) 513–521. [DOI] [PMID: 13618257]
4.	Lynn, W.S. and Perryman, N.C. Properties and purification of adipose tissue lipase. J. Biol. Chem. 235 (1960) 1912–1916. [PMID: 14419169]
5.	Paznokas, J.L. and Kaplan, A. Purification and properties of a triacylglycerol lipase from Mycobacterium phlei. Biochim. Biophys. Acta 487 (1977) 405–421. [PMID: 18200]
6.	Tiruppathi, C. and Balasubramanian, K.A. Purification and properties of an acid lipase from human gastric juice. Biochim. Biophys. Acta 712 (1982) 692–697. [PMID: 7126632]
7.	Hills, M.J. and Mukherjee, K.D. Triacylglycerol lipase from rape (Brassica napus L.) suitable for biotechnological purposes. Appl. Biochem. Biotechnol. 26 (1990) 1–10. [PMID: 2268143]
8.	Winkler, F.K., D'Arcy, A. and Hunziker, W. Structure of human pancreatic lipase. Nature 343 (1990) 771–774. [PMID: 2106079]
9.	Kim, K.K., Song, H.K., Shin, D.H., Hwang, K.Y. and Suh, S.W. The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. Structure 5 (1997) 173–185. [PMID: 9032073]
10.	Kurat, C.F., Natter, K., Petschnigg, J., Wolinski, H., Scheuringer, K., Scholz, H., Zimmermann, R., Leber, R., Zechner, R. and Kohlwein, S.D. Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J. Biol. Chem. 281 (2006) 491–500. [PMID: 16267052]
11.	Ranaldi, S., Belle, V., Woudstra, M., Bourgeas, R., Guigliarelli, B., Roche, P., Vezin, H., Carriere, F. and Fournel, A. Amplitude of pancreatic lipase lid opening in solution and identification of spin label conformational subensembles by combining continuous wave and pulsed EPR spectroscopy and molecular dynamics. Biochemistry 49 (2010) 2140–2149. [PMID: 20136147]

[EC 3.1.1.3 created 1961]