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Literature summary for 3.1.1.23 extracted from
- The GxSxG motif of Arabidopsis monoacylglycerol lipase (MAGL6 and MAGL8) is essential for their enzyme activities (2016), Appl. Biol. Chem., 59, 833-840 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene MGLL, sequence comparisons and phylogenetic analysis and tree, recombinant expression of MBP-tagged wild-type and mutant enzymes in Escherichia coli | Homo sapiens |
| gene PLP16, sequence comparisons and phylogenetic analysis, recombinant expression of MBP-tagged wild-type and mutant enzymes in Escherichia coli | Arabidopsis thaliana |
| gene PLP6, sequence comparisons and phylogenetic analysis and tree, recombinant expression of MBP-tagged wild-type and mutant enzymes in Escherichia coli | Arabidopsis thaliana |
| gene PLP8, sequence comparisons and phylogenetic analysis and tree, recombinant expression of MBP-tagged wild-type and mutant enzymes in Escherichia coli | Arabidopsis thaliana |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G111S | site-directed mutagenesis by overlap extension PCR, inactive mutant | Homo sapiens |
| G111S | site-directed mutagenesis by overlap extension PCR, inactive mutant | Arabidopsis thaliana |
| G115S | site-directed mutagenesis by overlap extension PCR, inactive mutant | Homo sapiens |
| G115S | site-directed mutagenesis by overlap extension PCR, inactive mutant | Arabidopsis thaliana |
| G117S | site-directed mutagenesis by overlap extension PCR, inactive mutant | Arabidopsis thaliana |
| G121S | site-directed mutagenesis by overlap extension PCR, inactive mutant | Arabidopsis thaliana |
| additional information | computational modeling shows that amino acid changes of the GxSxG motif in AtMAGL6 alters the nucleophilic elbow structure, which is the active site of MAGLs. Mutating the GxSxG motif in the recombinant maltose binding protein (MBP):AtMAGL6 protein to SxSxG, GxAxG, and GxSxS motifs completely demolishes the activities of the mutant MAGL | Homo sapiens |
| additional information | computational modeling shows that amino acid changes of the GxSxG motif in AtMAGL6 alters the nucleophilic elbow structure, which is the active site of MAGLs. Mutating the GxSxG motif in the recombinant maltose binding protein (MBP):AtMAGL6 protein to SxSxG, GxAxG, and GxSxS motifs completely demolishes the activities of the mutant MAGL | Arabidopsis thaliana |
| S113A | site-directed mutagenesis by overlap extension PCR, inactive mutant | Homo sapiens |
| S113A | site-directed mutagenesis by overlap extension PCR, inactive mutant | Arabidopsis thaliana |
| S119A | site-directed mutagenesis by overlap extension PCR, inactive mutant | Arabidopsis thaliana |
| S139G | no significant differences are observed between the activities of AtMAGL16 wild-type form harboring the SxSxG (Ser139-Ser141-Gly143) motif, and mutant AtMAGL16 containing the GxSxG motif | Arabidopsis thaliana |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| phenylmethylsulfonyl fluoride | PMSF is able to produce an irreversible MAGL-PMSF adduct and hydrofluoric acid (HF), by specifically binding to the hydroxyl group of the serine residue in the active site of the serine protease, thereby inhibiting its enzymatic activity; PMSF is able to produce an irreversible MAGL-PMSF adduct and hydrofluoric acid (HF), by specifically binding to the hydroxyl group of the serine residue in the active site of the serine protease, thereby inhibiting its enzymatic activity | Arabidopsis thaliana |  |
| phenylmethylsulfonyl fluoride | PMSF is able to produce an irreversible MAGL-PMSF adduct and hydrofluoric acid (HF), by specifically binding to the hydroxyl group of the serine residue in the active site of the serine protease, thereby inhibiting its enzymatic activity | Homo sapiens | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | O49284 | - |
- |
| Arabidopsis thaliana | O80959 | - |
- |
| Arabidopsis thaliana | Q8H133 | - |
- |
| Homo sapiens | Q99685 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant MBP-tagged wild-type and mutant enzymes from Escherichia coli by amylose affinity chromatography | Homo sapiens |
| recombinant MBP-tagged wild-type and mutant enzymes from Escherichia coli by amylose affinity chromatography | Arabidopsis thaliana |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.13 | - |
purified recombinant MBP-tagged wild-type enzyme, pH 8.0-9.0, 37°C | Arabidopsis thaliana |
| 0.2 | - |
purified recombinant MBP-tagged mutant S139G enzyme, pH 8.0-9.0, 37°C | Arabidopsis thaliana |
| 19.3 | - |
purified recombinant MBP-tagged wild-type enzyme, pH 8.0-9.0, 37°C | Arabidopsis thaliana |
| 21.8 | - |
purified recombinant MBP-tagged wild-type enzyme, pH 8.0-9.0, 37°C | Arabidopsis thaliana |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl acetate + H2O | - |
Homo sapiens | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Arabidopsis thaliana | 4-nitrophenol + acetate | - |
? | |
| 7-hydroxycoumarinyl arachidonate + H2O | - |
Homo sapiens | 7-hydroxycoumarin + arachidonate | - |
? | |
| 7-hydroxycoumarinyl arachidonate + H2O | - |
Arabidopsis thaliana | 7-hydroxycoumarin + arachidonate | - |
? | |
| additional information | usage of a substrate with linoleic acid at the sn-1 position for enzyme activity assays | Homo sapiens | ? | - |
? | |
| additional information | usage of a substrate with linoleic acid at the sn-1 position for enzyme activity assays. The Arabidopsis thaliana isozyme MAGL16 (AtMAGL16) shows very weak lipase activity. AtMAGL16 may not be involved in the hydrolysis of lipid substrates | Arabidopsis thaliana | ? | - |
? | |
| additional information | usage of a substrate with linoleic acid at the sn-1 position for enzyme activity assays. The Arabidopsis thaliana isozyme MAGL6 (AtMAGL6) shows strong lipase activity | Arabidopsis thaliana | ? | - |
? | |
| additional information | usage of a substrate with linoleic acid at the sn-1 position for enzyme activity assays. The Arabidopsis thaliana isozyme MAGL8 (AtMAGL8) shows strong lipase activity | Arabidopsis thaliana | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 72000, about, recombinant MBP-tagged wild-type and mutant enzymes, SDS-PAGE | Arabidopsis thaliana |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MAGL16 | - |
Arabidopsis thaliana |
| MAGL6 | - |
Arabidopsis thaliana |
| MAGL8 | - |
Arabidopsis thaliana |
| MGL | - |
Homo sapiens |
| MGLL | - |
Homo sapiens |
| monoacylglycerol lipase | - |
Homo sapiens |
| monoacylglycerol lipase | - |
Arabidopsis thaliana |
| patatin-like protein 16 | UniProt | Arabidopsis thaliana |
| patatin-like protein 6 | UniProt | Arabidopsis thaliana |
| patatin-like protein 8 | UniProt | Arabidopsis thaliana |
| PLP16 | - |
Arabidopsis thaliana |
| PLP6 | - |
Arabidopsis thaliana |
| PLP8 | - |
Arabidopsis thaliana |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Homo sapiens |
| 30 | - |
assay at | Arabidopsis thaliana |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 9 | assay at | Homo sapiens |
| 8 | 9 | assay at | Arabidopsis thaliana |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.0023 | - |
pH 8.0-9.0, 37°C, recombinant enzyme | Arabidopsis thaliana | phenylmethylsulfonyl fluoride | |
| 0.00235 | - |
pH 8.0-9.0, 37°C, recombinant enzyme | Arabidopsis thaliana | phenylmethylsulfonyl fluoride | |
| 0.0032 | - |
versus 7-4-nitrophenylacetate, pH 8.0-9.0, 37°C, recombinant enzyme | Homo sapiens | phenylmethylsulfonyl fluoride | |
| 0.0033 | - |
versus 7-hydroxycoumarinyl arachidonate, pH 8.0-9.0, 37°C, recombinant enzyme | Homo sapiens | phenylmethylsulfonyl fluoride | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the GxSxS motif is conserved in monoacylglycerol lipases (MAGLs) | Homo sapiens |
| evolution | the GxSxS motif is conserved in monoacylglycerol lipases (MAGLs) | Arabidopsis thaliana |
| malfunction | amino acid changes of the GxSxG motif in AtMAGL6 alters the nucleophilic elbow structure, which is the active site of MAGLs. Mutating the GxSxG motif in the recombinant maltose binding protein (MBP):AtMAGL6 protein to SxSxG, GxAxG, and GxSxS motifs completely demolishes the activities of the mutant MAGL | Arabidopsis thaliana |
| malfunction | computational modeling shows that amino acid changes of the GxSxG motif in AtMAGL8 alters the nucleophilic elbow structure, which is the active site of MAGLs. Mutating the GxSxG motif in the recombinant maltose binding protein (MBP):AtMAGL8 protein to SxSxG, GxAxG, and GxSxS motifs completely demolishes the activities of the mutant MAGL | Arabidopsis thaliana |
| additional information | no significant differences are observed between the activities of AtMAGL16 wild-type form harboring the SxSxG motif, and mutant AtMAGL16 containing the GxSxG motif. Enzyme structure modelling using the crystal structure of human MAGL, PDB ID 3HJU | Arabidopsis thaliana |
| additional information | the glycine and serine residues of the GxSxG motif are essential for AtMAGL6 enzyme activity. Enzyme structure modelling using the crystal structure of human MAGL, PDB ID 3HJU | Arabidopsis thaliana |
| additional information | the glycine and serine residues of the GxSxG motif are essential for AtMAGL8 enzyme activity. Enzyme structure modelling using the crystal structure of human MAGL, PDB ID 3HJU | Arabidopsis thaliana |
| physiological function | AtMAGL16 may not be involved in the hydrolysis of lipid substrates | Arabidopsis thaliana |
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