Monoacylglycerol lipase

Source: Wikipedia, the free encyclopedia.
acylglycerol lipase
ExPASy
NiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
monoglyceride lipase
Identifiers
SymbolMGLL
Chr. 3 p13-q13.33
Search for
StructuresSwiss-model
DomainsInterPro

Monoacylglycerol lipase (EC 3.1.1.23; systematic name glycerol-ester acylhydrolase, also known as MAG lipase, acylglycerol lipase, MAGL, MGL or MGLL) is an enzyme that, in humans, is encoded by the MGLL gene.[1][2][3] MAGL is a 33-kDa, membrane-associated member of the serine hydrolase superfamily and contains the classical GXSXG consensus sequence common to most serine hydrolases. The catalytic triad has been identified as Ser122, His269, and Asp239.[2][4]

Human monoacylglycerol lipase

Function

Monoacylglycerol lipase catalyzes a reaction that uses water molecules to break the glycerol monoesters of long-chain fatty acids
:

hydrolyses glycerol monoesters of long-chain fatty acids

It functions together with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.[5]

Monoacylglycerol lipase is a key enzyme in the hydrolysis of the

downregulation of CB1 receptors in selective brain areas.[11]

Inhibitors

MAGL enzyme inhibitors (URB602, URB754, JZL184) produce cannabinoid behavioral effects in mice.[10]

Further examples include:[citation needed]

  1. KML-29
  2. JZL195
  3. JNJ-42165279
  4. JW 642

See also

References

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.