Triacylglycerol lipase (original) (raw)

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Enzyme catalyst

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
SearchPMCarticlesPubMedarticlesNCBIproteins

Protein family

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
Available protein structures:Pfam structures / ECOD PDBRCSB PDB; PDBe; PDBjPDBsumstructure summary

The enzyme triacylglycerol lipase (also triglyceride lipase, EC 3.1.1.3;systematic name triacylglycerol acylhydrolase) catalyses the hydrolysis of ester linkages of triglycerides:[1]

triacylglycerol + H2O ⇌ 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.[2][3][4][5][6]

Human proteins containing this domain

[edit]

DAGLA; DAGLB; LOC221955; The pancreatic enzyme acts only on an ester-water interface.

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).

  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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.
  5. ^ 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.
  6. ^ Singer, T.P.; Hofstee, B.H.J. (1948). "Studies on wheat germ lipase. II. Kinetics". Arch. Biochem. 18 (2): 245–259. PMID 18875046.