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Literature summary for 3.1.1.23 extracted from

  • Tyukhtenko, S.; Karageorgos, I.; Rajarshi, G.; Zvonok, N.; Pavlopoulos, S.; Janero, D.R.; Makriyannis, A.
    Specific inter-residue interactions as determinants of human monoacylglycerol lipase catalytic competency a role for global conformational chanages (2016), J. Biol. Chem., 291, 2556-2565 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.23

Protein Variants

Protein Variants Comment Organism
H103A site-directed mutagenesis, the mutant shows 20fold reduced catalytic efficiency compared to wild-type Homo sapiens
H269A site-directed mutagenesis, structural comparison to the wild-type enzyme by NMR spectrometry Homo sapiens
H272A site-directed mutagenesis, the mutant shows 13fold reduced catalytic efficiency compared to wild-type Homo sapiens
H272S site-directed mutagenesis, the mutant shows 58fold reduced catalytic efficiency compared to wild-type Homo sapiens
H272Y site-directed mutagenesis, the muant shows 12fold reduced catalytic efficiency compared to wild-type Homo sapiens
H49A site-directed mutagenesis, the mutant shows 5fold reduced catalytic efficiency compared to wild-type Homo sapiens
H54A site-directed mutagenesis, structural comparison to the wild-type enzyme by NMR spectrometry, the mutant shows a dramatic 25000fold loss in hMGL catalytic efficiency compared to wild-type Homo sapiens
L169S/L176S site-directed mutagenesis, hMGL function is not significantly compromised by the mutation, structural comparison to the wild-type enzyme by NMR spectrometry Homo sapiens
S122C site-directed mutagenesis, structural comparison to the wild-type enzyme by NMR spectrometry Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information structure-based MGL inhibitor design Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Homo sapiens
0.012
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H54A Homo sapiens
0.022
-
 2-arachidonoylglycerol pH 7.4, 22°C, soluble wild-type variant Homo sapiens
0.0222
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H272A Homo sapiens
0.0308
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H272S Homo sapiens
0.0362
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H272Y Homo sapiens
0.0366
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H49A Homo sapiens
0.122
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H103A Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q99685
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-arachidonoylglycerol + H2O
-
 Homo sapiens arachidonoate + glycerol
-
 ?
additional information direct NMR detection of a reversible equilibrium between active and inactive states of human MGL (hMGL) that is slow on the NMR time scale and can be modulated in a controlled manner by pH, temperature, and select point mutations Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
? x * 34100, SDS-PAGE Homo sapiens
More simultaneous NMR detection of both active and inactive hMGL states in solution Homo sapiens

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
11
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H54A Homo sapiens
13000
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H272S Homo sapiens
14000
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H103A Homo sapiens
45000
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H272A Homo sapiens
70000
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H272Y Homo sapiens
160000
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H49A Homo sapiens
570000
-
 2-arachidonoylglycerol pH 7.4, 22°C, soluble wild-type variant Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme is a member of the serine hydrolase superfamily Homo sapiens
additional information a network of aromatic interactions and hydrogen bonds regulates hMGL active-inactive state interconversion. Specific inter-residue interactions within hMGL modulate the enzymes function and implicate transitions between active (open) and inactive (closed) states of the hMGL lid domain in controlling substrate access to the enzymes active site. The residues Ser122, His269, and Asp239 form the catalytic triad, hMGL structure-function correlations, overview Homo sapiens
physiological function the serine hydrolase monoacylglycerol lipase (MGL) functions as the main metabolizing enzyme of 2-arachidonoyl glycerol, an endocannabinoid signaling lipid. Monoacylglycerol lipase is largely responsible for the catalytic inactivation of the endocannabinoid signaling lipid, 2-arachidonoylglycerol, and regulates a fatty acid network that promotes tumorigenesis Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
917
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H54A Homo sapiens
2027
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H272A Homo sapiens
4372
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H49A Homo sapiens
25909
-
 2-arachidonoylglycerol pH 7.4, 22°C, soluble wild-type variant Homo sapiens
114754
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H103A Homo sapiens
422078
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H272S Homo sapiens
1933700
-
 2-arachidonoylglycerol pH 7.4, 22°C, mutant H272Y Homo sapiens