| Entry |
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| Name |
triacylglycerol lipase;
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)
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| Class |
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
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| Sysname |
triacylglycerol acylhydrolase
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| Reaction(IUBMB) |
triacylglycerol + H2O = diacylglycerol + a carboxylate [RN: R01369]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
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.
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| History |
EC 3.1.1.3 created 1961
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| Pathway |
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| Orthology |
| K12298 | bile salt-stimulated lipase |
| K13534 | patatin-like phospholipase domain-containing protein 3 |
| K13616 | arylacetamide deacetylase |
| K14073 | pancreatic triacylglycerol lipase |
| K14074 | pancreatic lipase-related protein 1 |
| K14075 | pancreatic lipase-related protein 2 |
| K14076 | pancreatic lipase-related protein 3 |
| K14452 | gastric triacylglycerol lipase |
| K14674 | TAG lipase / steryl ester hydrolase / phospholipase A2 / LPA acyltransferase |
| K14675 | TAG lipase / lysophosphatidylethanolamine acyltransferase |
| K16816 | patatin-like phospholipase domain-containing protein 2 |
| K22283 | hepatic triacylglycerol lipase |
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| Genes |
» show all
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| Reference |
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| Authors |
SINGER TP, HOFSTEE BH |
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| Title |
Studies on wheat germ lipase; methods of estimation, purification, and general properties of the enzyme. |
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| Journal |
Arch Biochem 18:229-43 (1948) |
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| Reference |
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| Authors |
SINGER TP, HOFSTEE BH |
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| Title |
Studies on wheat germ lipase; kinetics. |
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| Journal |
Arch Biochem 18:245-59 (1948) |
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| Reference |
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| Authors |
SARDA L, DESNUELLE P. |
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| Title |
[Actions of pancreatic lipase on esters in emulsions.] |
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| Journal |
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| Reference |
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| Authors |
LYNN WS Jr, PERRYMAN NC. |
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| Title |
Properties and purification of adipose tissue lipase. |
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| Journal |
J Biol Chem 235:1912-6 (1960) |
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| Reference |
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| Authors |
Paznokas JL, Kaplan A |
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| Title |
Purification and properties of a triacylglycerol lipase from Mycobacterium phlei. |
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| Journal |
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| Reference |
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| Authors |
Tiruppathi C, Balasubramanian KA |
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| Title |
Purification and properties of an acid lipase from human gastric juice. |
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| Journal |
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| Reference |
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| Authors |
Hills MJ, Mukherjee KD |
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| Title |
Triacylglycerol lipase from rape (Brassica napus L.) suitable for biotechnological purposes. |
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| Journal |
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| Reference |
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| Authors |
Winkler FK, D'Arcy A, Hunziker W |
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| Title |
Structure of human pancreatic lipase. |
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| Journal |
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| Reference |
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| Authors |
Kim KK, Song HK, Shin DH, Hwang KY, Suh SW |
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| Title |
The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. |
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| Journal |
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| Reference |
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| Authors |
Kurat CF, Natter K, Petschnigg J, Wolinski H, Scheuringer K, Scholz H, Zimmermann R, Leber R, Zechner R, Kohlwein SD |
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| Title |
Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. |
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| Journal |
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| Reference |
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| Authors |
Ranaldi S, Belle V, Woudstra M, Bourgeas R, Guigliarelli B, Roche P, Vezin H, Carriere F, Fournel A |
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| Title |
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. |
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| Journal |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 3.1.1.3 |
| ExPASy - ENZYME nomenclature database: | 3.1.1.3 |
| BRENDA, the Enzyme Database: | 3.1.1.3 |
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