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Literature summary for 3.1.1.23 extracted from

  • Beladjila, K.A.; Berrehal, D.; De Tommasi, N.; Granchi, C.; Bononi, G.; Braca, A.; De Leo, M.
    New phenylethanoid glycosides from Cistanche phelypaea and their activity as inhibitors of monoacylglycerol lipase (MAGL) (2018), Planta Med., 84, 710-715 .
    View publication on PubMed
Search for more literature for 3.1.1.23

Application

Application Comment Organism
medicine enzyme MAGL represents a potential target to treat diverse pathological conditions, including cancer Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
(4-[4-chlorobenzoyl]piperidin-1-yl)(4-methoxyphenyl)-methanone
-
 Homo sapiens
2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-(4-coumaroyl)-beta-D-glucopyranoside
-
 Homo sapiens
2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-beta-D-glucopyranoside the inhibitor is selective for hMAGL over hLDH, modeling of the binding mode in the MAGL active site. The sugar moiety lies in the wide lipophilic cavity of the protein forming lipophilic interactions with L148, L213, L241, and V183, whereas the 4-hydroxyphenyl-ethyl ring lies into the small pocket of the binding site and forms lipophilic interactions with residues Y194 and V270. A high number of H-bonds stabilizes the binding disposition of the compound Homo sapiens
2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-beta-D-glucopyranoside
-
 Homo sapiens
brandioside
-
 Homo sapiens
additional information phenylethanoid glycosides isolated from the n-butanol extract of Cistanche phelypaea aerial parts (collected in March 2012 in the southwest of Algeria) show activity as inhibitors of monoacylglycerol lipase, structure determinations by spectroscopic analyses, including 1D and 2D NMR, and HRESIMS experiments, docking study, overview. No inhibition by galloflavin, apigenin 7-O-beta-D-glucuronopyranoside, and 2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-(4-coumaroyl)-beta-D-glucopyranoside Homo sapiens
pinoresinol 4-O-beta-D-glucopyranoside
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q99685
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O
-
 Homo sapiens 4-nitrophenol + acetate
-
 ?

Synonyms

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.088
-
 pH 7.4, temperature not specified in the publication Homo sapiens 2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-beta-D-glucopyranoside
0.1139
-
 pH 7.4, temperature not specified in the publication Homo sapiens 2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-(4-coumaroyl)-beta-D-glucopyranoside
0.1174
-
 pH 7.4, temperature not specified in the publication Homo sapiens 2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-beta-D-glucopyranoside

General Information

General Information Comment Organism
physiological function MAGL is a serine hydrolase that cleaves monoacyglycerols into fatty acids and glycerol. In particular, MAGL is the lipolytic enzyme that is mainly responsible for the degradation of the endocannabinoid 2-arachidonoylglycerol, which is a neurotransmitter and an important intermediate in lipid metabolism involved in many physiological processes. Moreover, the intensified production of fatty acids in cancer cells, generated by MAGL activity, increases the formation of protumorigenic signaling molecules Homo sapiens