Triacylglycerol lipase

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
Search PMC articles PubMed articles NCBI proteins

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   PDB RCSB PDB; PDBe; PDBj PDBsum structure 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

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

• Pancreatic lipase
• Gastric lipase
• Lingual lipase

References

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

• Triacylglycerol+lipase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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