Literature summary for 3.1.1.23 extracted from

Karageorgos, I.; Tyukhtenko, S.; Zvonok, N.; Janero, D.R.; Sallum, C.; Makriyannis, A.
Identification by nuclear magnetic resonance spectroscopy of an active-site hydrogen-bond network in human monoacylglycerol lipase (hMGL): implications for hMGL dynamics, pharmacological inhibition, and catalytic mechanism (2010), Mol. Biosyst., 6, 1381-1388.

Search for more literature for 3.1.1.23

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C208A	the mutation does not affect enzyme catalytic activity	Homo sapiens
C242A	the mutation does not affect enzyme catalytic activity	Homo sapiens
D239T	the mutation substantially compromises enzyme activity	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
AM6701	MGL inhibition by AM6701 involves a covalent interaction resulting in the enzyme's rapid, selective carbamoylation at its catalytic serine nucleophile (Ser122)	Homo sapiens
JZL184	-	Homo sapiens
N-arachidonoylmaleimide	inhibits MGL through partial enzyme alkylation at Cys208 and/or Cys242 (Cys242 being favored)	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
immobilized metal affinity column chromatography	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-arachidonoylglycerol + H2O	-	Homo sapiens	glycerol + arachidonic acid	-	?
arachidonoyl-7-hydroxy-6-methoxy-4-methylcoumarin ester + H2O	-	Homo sapiens	arachidonic acid + 7-hydroxy-6-methoxy-4-methylcoumarin	-	?

Synonyms

Synonyms	Comment	Organism
MGL	-	Homo sapiens
monoacylglycerol lipase	-	Homo sapiens

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Release 2023.1 (January 2023)