EC - Triacylglycerol lipase

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IntEnz Enzyme Nomenclature


Accepted name:
triacylglycerol lipase
Other names:
GA 56
Meito MY 30
Takedo 1969-4-9
Tween hydrolase
amano AP
amano B
amano CE
amano CES
amano P
amno N-AP
capalase L
glycerol ester hydrolase
glycerol-ester hydrolase
heparin releasable hepatic lipase
hepatic lipase
hepatic monoacylglycerol acyltransferase
liver lipase
meito Sangyo OF lipase
post-heparin plasma protamine-resistant lipase
salt-resistant post-heparin lipase
triacylglycerol ester hydrolase
tributyrin esterase
triglyceride hydrolase
triglyceride lipase
triolein hydrolase
tween-hydrolyzing esterase
Systematic name:
triacylglycerol acylhydrolase



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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00110 , PROSITE:PDOC00112
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004806
CAS Registry Number: 9001-62-1
UniProtKB/Swiss-Prot: (206) [show] [UniProt]


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

[EC created 1961]