Biology:Triacylglycerol lipase

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Triacylglycerol lipase
Identifiers
EC number3.1.1.3
CAS number9001-62-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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

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

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

Nomenclature

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

References

  1. "Minireview on pancreatic lipase and colipase". Biochimie 70 (9): 1223–1234. 1988. doi:10.1016/0300-9084(88)90188-5. PMID 3147715. 
  2. "Lipoprotein lipase of chicken adipose tissue". The Journal of Biological Chemistry 226 (2): 833–9. June 1957. doi:10.1016/S0021-9258(18)70867-3. PMID 13438870. 
  3. "Properties and purification of adipose tissue lipase". The Journal of Biological Chemistry 235 (7): 1912–6. July 1960. doi:10.1016/S0021-9258(18)69335-4. PMID 14419169. 
  4. "[Actions of pancreatic lipase on esters in emulsions]". Biochimica et Biophysica Acta 30 (3): 513–21. December 1958. 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

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