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Literature summary extracted from

  • Schalk-Hihi, C.; Schubert, C.; Alexander, R.; Bayoumy, S.; Clemente, J.C.; Deckman, I.; DesJarlais, R.L.; Dzordzorme, K.C.; Flores, C.M.; Grasberger, B.; Kranz, J.K.; Lewandowski, F.; Liu, L.; Ma, H.; Maguire, D.; Macielag, M.J.; McDonnell, M.E.; Mezzasalma Haarlander, T.; Miller, R.; Milligan, C.; R, R.e.
    Crystal structure of a soluble form of human monoglyceride lipase in complex with an inhibitor at 1.35 A resolution (2011), Protein Sci., 20, 670-683.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.23 expressed in Escherichia coli BL21 and Rosetta cells. Expression in the baculovirus expression system produced only insoluble, aggregated protein Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.23 in complex with methyl arachidonyl fluorophosphonate, hanging drop vapor diffusion method, using 6-10% (w/v) PEGMME 5000, 100 mM Na-MES pH 6.0, 0.2% (w/v) glucopyranoside, at 22°C Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.23 L167Q/L171Q the mutant shows increased catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme Homo sapiens
3.1.1.23 L167Q/L174Q the mutant shows increased catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme Homo sapiens
3.1.1.23 L169S/L176S the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate and increased catalytic efficiency with umbelliferyl arachidonate compared to the wild type enzyme Homo sapiens
3.1.1.23 L169S/L176S the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme Homo sapiens
3.1.1.23 L169S/L176S/K160A the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme Homo sapiens
3.1.1.23 L169S/L176S/K165A the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme Homo sapiens
3.1.1.23 L169S/L176S/K226A the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme Homo sapiens
3.1.1.23 L169S/L176S/K36A the mutant shows about wild type catalytic efficiency with 4-methylumbelliferyl butyrate Homo sapiens
3.1.1.23 L169S/L176S/K36A/K226A the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme Homo sapiens
3.1.1.23 L171Q the mutant shows about wild type catalytic efficiency with 4-methylumbelliferyl butyrate Homo sapiens
3.1.1.23 L171Q/L174Q the mutant shows increased catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.23 methyl arachidonyl fluorophosphonate irreversible active-site inhibitor of monoglyceride lipase Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.23 0.084
-
 4-Methylumbelliferyl butyrate mutant enzyme L167Q/L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.084
-
 4-Methylumbelliferyl butyrate mutant enzyme L167Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.089
-
 4-Methylumbelliferyl butyrate mutant enzyme L171Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.09
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K160A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.105
-
 4-Methylumbelliferyl butyrate mutant enzyme L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.11
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.123
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K36A/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.124
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K36A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.136
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.137
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K165A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.162
-
 4-Methylumbelliferyl butyrate wild type enzyme, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.23 membrane
-
 Homo sapiens 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.23 2-arachidonoylglycerol + H2O Homo sapiens
-
 glycerol + arachidonic acid
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.23 Homo sapiens Q99685
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.23 His-Trap column chromatography and Superdex 200 gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.23 2-arachidonoylglycerol + H2O
-
 Homo sapiens glycerol + arachidonic acid
-
 ?
3.1.1.23 4-methylumbelliferyl butyrate + H2O
-
 Homo sapiens 4-methylumbelliferol + butyrate
-
 ?
3.1.1.23 umbelliferyl arachidonate + H2O
-
 Homo sapiens umbelliferol + arachidonic acid
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.23 MGL
-
 Homo sapiens
3.1.1.23 monoglyceride lipase
-
 Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.23 58
-
 the midpoint of the melting transition is calculated to be 58°C for wild type enzyme Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.23 0.45
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K165A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.5
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K160A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.5
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K36A/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.63
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.78
-
 4-Methylumbelliferyl butyrate mutant enzyme L171Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.8
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.85
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K36A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.85
-
 4-Methylumbelliferyl butyrate mutant enzyme L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 0.98
-
 4-Methylumbelliferyl butyrate mutant enzyme L167Q/L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 1.13
-
 4-Methylumbelliferyl butyrate wild type enzyme, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 1.17
-
 4-Methylumbelliferyl butyrate mutant enzyme L167Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.23 1.5
-
 umbelliferyl arachidonate wild type enzyme, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 1.7
-
 umbelliferyl arachidonate mutant enzyme L169S/L176S, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 3.3
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K165A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 4.2
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K36A/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 5.5
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K160A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 5.8
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 5.8
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 6.8
-
 4-Methylumbelliferyl butyrate mutant enzyme L169S/L176S/K36A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 7
-
 4-Methylumbelliferyl butyrate wild type enzyme, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 8
-
 4-Methylumbelliferyl butyrate mutant enzyme L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 8.7
-
 4-Methylumbelliferyl butyrate mutant enzyme L171Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 11.8
-
 4-Methylumbelliferyl butyrate mutant enzyme L167Q/L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens
3.1.1.23 13.8
-
 4-Methylumbelliferyl butyrate mutant enzyme L167Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C Homo sapiens