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3.1.1.23: acylglycerol lipase

This is an abbreviated version!
For detailed information about acylglycerol lipase, go to the full flat file.

Word Map on EC 3.1.1.23

Reaction

CnHmCO-C3O3H7
+
H2O
=
CnHmCO2H
 +
glycerol

Synonyms

AtMAGL, AtMAGL1, AtMAGL10, AtMAGL11, AtMAGL14, AtMAGL15, AtMAGL16, AtMAGL2, AtMAGL3, AtMAGL4, AtMAGL5, AtMAGL6, AtMAGL7, AtMAGL8, AtMAGL9, fatty acyl monoester lipase, glycerol-monoester acylhydrolase, HMGL, LH57_01015, lipase, lipase G, LipB, lipozyme IM, MAG hydrolase, MAG lipase, MAGL, MAGL-cy, MAGL-m, MAGL16, MAGL6, MAGL8, MGH, MGL, MGL Rv0183, MGL-like activity, MGLL, MGLP, monoacylglycerol hydrolase, monoacylglycerol lipase, monoglycerid lipase, monoglyceridase, monoglyceride hydrolase, monoglyceride lipase, monoglyceride lipase-like activity, monoglyceridyllipase, MSMEG_0220, mtbMGL, patatin-like protein 1, patatin-like protein 16, patatin-like protein 2, patatin-like protein 3, patatin-like protein 4, patatin-like protein 5, patatin-like protein 6, patatin-like protein 7, patatin-like protein 8, patatin-like protein 9, PLP1, PLP16, PLP2, PLP3, PLP4, PLP5, PLP6, PLP7, PLP8, PLP9, Rv0183, Rv0183 protein, Yju3p

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.23 acylglycerol lipase

Crystallization

Crystallization on EC 3.1.1.23 - acylglycerol lipase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1.5 M ammonium sulfate, 100 mM citrate (pH 5.8) and 100 mM tartrate
sitting drop vapor diffusion method, using 0.1 M MES/imidazole pH 6.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (w/v) MPD
sitting drop vapor diffusion method, using 0.1 M MES/imidazole, pH 6.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (w/v) 2-methyl-2,4-pentanediol or hanging drop vapor diffusion method using 0.1 M citric acid, pH 5.2, and 18% (w/v) PEG3350
hanging drop vapor diffusion method, benzamidine is essential for crystallization
-
apoenzyme alone or in complex with inhibitor SAR629, in 50 mM MES (pH 6.0) and 40% (v/v) 2-methyl-pentane-2,4-diol, at 4°C
-
by the hanging drop method and under oil crystallization, native enzyme or selenomethionyl derivative, at 2.2 A resolution. Belongs to I222 space group, with two molecules per asymmetric unit. Docking of 2-arachidonoylglycerol highlights a hydrophobic and a hydrophilic cavity that accommodate the lipid into the catalytic site
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
enzyme mtbMGL in open conformation, sitting drop vapor diffusion method and microseeding, mixing 500 nl of 10 mg/ml protein solution with 500 nl of crystallization solution containing 0.1 M carboxylic acids, 0.1 M sodium HEPES/MOPS, pH 7.5, 20% ethylene glycol, and 10% PEG 8000, 4 months, 20°C, microseeding by mixing of 400 nl protein solution with 400 nl crystallization solution and 200 nl seeding stock, containing 0.03 M NaNO3, 0.03 M Na2HPO4, 0.03 M (NH4)2SO4, 0.1 M Na HEPES/MOPS, pH 7.8, 12% MPD, 12% PEG 1000 and 12% PEG 3350, 2 weeks, 20°C, X-ray diffraction structure determination and analysis at 1.80 A resolution, molecular replacement using the PDB IDs 3PE6 and 1W53 as search templates