Monoacylglycerol lipase

acylglycerol lipase
Reaction catalyzed by MGLL, in which a free fatty acid (FFA) is released from a monoacylglycerol (MAG)
Identifiers
EC no.3.1.1.23
CAS no.9040-75-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
monoglyceride lipase
Identifiers
SymbolMGLL
NCBI gene11343
HGNC17038
OMIM609699
RefSeqNM_007283
UniProtQ99685
Other data
EC number3.1.1.23
LocusChr. 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
  1. ^ Wall EM, Cao J, Chen N, Buller RM, Upton C (December 1997). "A novel poxvirus gene and its human homolog are similar to an E. coli lysophospholipase". Virus Research. 52 (2): 157–67. doi:10.1016/S0168-1702(97)00122-6. PMID 9495531.
  2. ^ a b Karlsson M, Contreras JA, Hellman U, Tornqvist H, Holm C (October 1997). "cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases, and haloperoxidases". The Journal of Biological Chemistry. 272 (43): 27218–23. doi:10.1074/jbc.272.43.27218. PMID 9341166.
  3. ^ "Entrez Gene: monoglyceride lipase".
  4. ^ Tornqvist H, Belfrage P (February 1976). "Purification and some properties of a monoacylglycerol-hydrolyzing enzyme of rat adipose tissue". The Journal of Biological Chemistry. 251 (3): 813–9. doi:10.1016/S0021-9258(17)33857-7. PMID 1249056.