Triacylglycerol lipase

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Triacylglycerol lipase
Identifiers
EC no.3.1.1.3
CAS no.9001-62-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
Lipase (class 3)
PDB 3tgl EBI.jpg
Structure of Triacyl-glycerol acylhydrolase.
Identifiers
SymbolLipase_3
PfamPF01764
InterProIPR002921
PROSITEPDOC00110
SCOP23tgl / SCOPe / SUPFAM
OPM superfamily127
OPM protein3tgl
CDDcd00519
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure 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.

Nomenclature[edit]

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[edit]

References[edit]

  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.

External links[edit]

This article incorporates text from the public domain Pfam and InterPro: IPR002921