EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.60 | recombinant expression of enzyme NAAA in Spodoptera frugiperda Sf9 insect cells via baculovirus transfection method, the enzyme is secreted. The endogenous signal peptide is replaced by the melittin signal peptide MKFLVNVALVFMVVYISYIYA followed by a His6-tag DRHHHHHHKL. Construct encompasses residues 31-359 of NAAA of mouse enzyme | Oryctolagus cuniculus |
3.5.1.60 | recombinant expression of wild-type and mutant enzymes NAAA in Spodoptera frugiperda Sf9 insect cells via baculovirus transfection method, the enzyme is secreted. The endogenous signal peptide comprising the first 28-33 residues is replaced by the melittin signal peptide MKFLVNVALVFMVVYISYIYA followed by a His6-tag DRHHHHHHKL. Constructs encompassed residues 29-359 of NAAA of human enzyme | Homo sapiens |
3.5.1.60 | recombinant expression of wild-type and mutant enzymes NAAA in Spodoptera frugiperda Sf9 insect cells via baculovirus transfection method, the enzyme is secreted. The endogenous signal peptide is replaced by the melittin signal peptide MKFLVNVALVFMVVYISYIYA followed by a His6-tag DRHHHHHHKL. Constructs encompass residues 29-355 of NAAA of mouse enzyme | Cavia porcellus |
3.5.1.60 | recombinant expression of wild-type and mutant enzymes NAAA in Spodoptera frugiperda Sf9 insect cells via baculovirus transfection method, the enzyme is secreted. The endogenous signal peptide is replaced by the melittin signal peptide MKFLVNVALVFMVVYISYIYA followed by a His6-tag DRHHHHHHKL. Constructs encompass residues 34-362 of NAAA of mouse enzyme | Mus musculus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.5.1.60 | purified recombinant enzyme C116A mutant in complex with inhibitors ARN726, ARN19702, and with substrate myristate, and in presence of Triton X-100, X-ray diffraction structure determination and analysis at 2.7 A resolution | Oryctolagus cuniculus |
3.5.1.60 | purified recombinant enzyme in complex with inhibitor ARN726, and in presence of Triton X-100, X-ray diffraction structure determination and analysis at 3.0. A resolution | Cavia porcellus |
3.5.1.60 | purified recombinnat enzyme C116A mutant in complex with ARN19702 and in presence of Triton X-100, X-ray diffraction structure determination and analysis at 3.0 A resolution | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.1.60 | A47V | site-directed mutagenesis | Mus musculus |
3.5.1.60 | A75R | site-directed mutagenesis | Cavia porcellus |
3.5.1.60 | C116A | site-directed mutagenesis, inhibition of disulfide bridge formation | Homo sapiens |
3.5.1.60 | H142R | site-directed mutagenesis | Mus musculus |
3.5.1.60 | K95E | site-directed mutagenesis | Cavia porcellus |
3.5.1.60 | N112S | site-directed mutagenesis, the mutation abolishes an N-linked glycosylation site | Homo sapiens |
3.5.1.60 | N163D | site-directed mutagenesis | Mus musculus |
3.5.1.60 | N338S | site-directed mutagenesis, the mutation abolishes an N-linked glycosylation site4 | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.60 | 4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate | ARN726, enzyme-binding structure analysis. Nucleophilic attack on the carbonyl carbon of the strained beta-lactam moiety by the Cys126 side chain | Cavia porcellus | |
3.5.1.60 | 4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate | ARN726, a beta-lactam that irreversibly reacts with Cys126 | Homo sapiens | |
3.5.1.60 | 4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate | ARN726 | Mus musculus | |
3.5.1.60 | 4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate | ARN726, enzyme-binding structure analysis. Nucleophilic attack on the carbonyl carbon of the strained beta-lactam moiety by the Cys126 side chain | Oryctolagus cuniculus | |
3.5.1.60 | additional information | NAAA inhibitors block the substrate-binding site | Cavia porcellus | |
3.5.1.60 | additional information | NAAA inhibitors block the substrate-binding site | Homo sapiens | |
3.5.1.60 | additional information | NAAA inhibitors block the substrate-binding site | Mus musculus | |
3.5.1.60 | additional information | NAAA inhibitors block the substrate-binding site | Oryctolagus cuniculus | |
3.5.1.60 | [2-(ethylsulfonyl)phenyl][(2S)-4-(6-fluoro-1,3-benzothiazol-2-yl)-2-methylpiperazin-1-yl]methanone | ARN19702, a noncovalent benzothiazole-piperazine derivative | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.5.1.60 | lysosome | - |
Homo sapiens | 5764 | - |
3.5.1.60 | lysosome | - |
Mus musculus | 5764 | - |
3.5.1.60 | lysosome | - |
Oryctolagus cuniculus | 5764 | - |
3.5.1.60 | lysosome | - |
Cavia porcellus | 5764 | - |
3.5.1.60 | membrane | proposed membrane interactions via hydrophobic helices alpha3 and alpha6 | Homo sapiens | 16020 | - |
3.5.1.60 | membrane | proposed membrane interactions via hydrophobic helices alpha3 and alpha6 | Mus musculus | 16020 | - |
3.5.1.60 | membrane | proposed membrane interactions via hydrophobic helices alpha3 and alpha6 | Oryctolagus cuniculus | 16020 | - |
3.5.1.60 | membrane | proposed membrane interactions via hydrophobic helices alpha3 and alpha6 | Cavia porcellus | 16020 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.60 | N-palmitoylethanolamide + H2O | Homo sapiens | - |
palmitate + ethanolamine | - |
? | |
3.5.1.60 | N-palmitoylethanolamide + H2O | Mus musculus | - |
palmitate + ethanolamine | - |
? | |
3.5.1.60 | N-palmitoylethanolamide + H2O | Oryctolagus cuniculus | - |
palmitate + ethanolamine | - |
? | |
3.5.1.60 | N-palmitoylethanolamide + H2O | Cavia porcellus | - |
palmitate + ethanolamine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.60 | Cavia porcellus | H0VCJ6 | - |
- |
3.5.1.60 | Homo sapiens | Q02083 | - |
- |
3.5.1.60 | Mus musculus | Q9D7V9 | - |
- |
3.5.1.60 | Oryctolagus cuniculus | G1T7U7 | - |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.5.1.60 | glycoprotein | - |
Homo sapiens |
3.5.1.60 | glycoprotein | - |
Mus musculus |
3.5.1.60 | glycoprotein | - |
Oryctolagus cuniculus |
3.5.1.60 | glycoprotein | - |
Cavia porcellus |
3.5.1.60 | proteolytic modification | self-proteolysis exposes the NAAA active site | Homo sapiens |
3.5.1.60 | proteolytic modification | self-proteolysis exposes the NAAA active site | Mus musculus |
3.5.1.60 | proteolytic modification | self-proteolysis exposes the NAAA active site | Oryctolagus cuniculus |
3.5.1.60 | proteolytic modification | self-proteolysis exposes the NAAA active site | Cavia porcellus |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.1.60 | recombinant His-tagged enzyme from Spodoptera frugiperda Sf9 insect cells by nickel affinity chromatography, gel filtration, and anion exchange chromatography | Oryctolagus cuniculus |
3.5.1.60 | recombinant His-tagged wild-type and mutant enzymes from Spodoptera frugiperda Sf9 insect cells by nickel affinity chromatography, gel filtration, and anion exchange chromatography | Cavia porcellus |
3.5.1.60 | recombinant His6-tagged wild-type and mutant enzymes from Spodoptera frugiperda Sf9 insect cells by nickel affinity chromatography, gel filtration, and anion exchange chromatography | Homo sapiens |
3.5.1.60 | recombinant His6-tagged wild-type and mutant enzymes from Spodoptera frugiperda Sf9 insect cells by nickel affinity chromatography, gel filtration, and anion exchange chromatography | Mus musculus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.5.1.60 | additional information | N-acylethanolamine acid amidase is expressed at high levels in immune cells | Homo sapiens | - |
3.5.1.60 | additional information | N-acylethanolamine acid amidase is expressed at high levels in immune cells | Mus musculus | - |
3.5.1.60 | additional information | N-acylethanolamine acid amidase is expressed at high levels in immune cells | Oryctolagus cuniculus | - |
3.5.1.60 | additional information | N-acylethanolamine acid amidase is expressed at high levels in immune cells | Cavia porcellus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.60 | N-palmitoylethanolamide + H2O | - |
Homo sapiens | palmitate + ethanolamine | - |
? | |
3.5.1.60 | N-palmitoylethanolamide + H2O | - |
Mus musculus | palmitate + ethanolamine | - |
? | |
3.5.1.60 | N-palmitoylethanolamide + H2O | - |
Oryctolagus cuniculus | palmitate + ethanolamine | - |
? | |
3.5.1.60 | N-palmitoylethanolamide + H2O | - |
Cavia porcellus | palmitate + ethanolamine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.60 | heterotetramer | enzyme NAAA adopts an alphabetabetaalpha-fold with a helical alpha-subunit | Homo sapiens |
3.5.1.60 | heterotetramer | enzyme NAAA adopts an alphabetabetaalpha-fold with a helical alpha-subunit | Mus musculus |
3.5.1.60 | heterotetramer | enzyme NAAA adopts an alphabetabetaalpha-fold with a helical alpha-subunit | Oryctolagus cuniculus |
3.5.1.60 | heterotetramer | enzyme NAAA adopts an alphabetabetaalpha-fold with a helical alpha-subunit | Cavia porcellus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.60 | N-acylethanolamine acid amidase | - |
Homo sapiens |
3.5.1.60 | N-acylethanolamine acid amidase | - |
Mus musculus |
3.5.1.60 | N-acylethanolamine acid amidase | - |
Oryctolagus cuniculus |
3.5.1.60 | NAAA | - |
Homo sapiens |
3.5.1.60 | NAAA | - |
Mus musculus |
3.5.1.60 | NAAA | - |
Oryctolagus cuniculus |
3.5.1.60 | NAAA | - |
Cavia porcellus |
3.5.1.60 | Nacylethanolamine acid amidase | - |
Cavia porcellus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.60 | 37 | - |
assay at | Homo sapiens |
3.5.1.60 | 37 | - |
assay at | Mus musculus |
3.5.1.60 | 37 | - |
assay at | Oryctolagus cuniculus |
3.5.1.60 | 37 | - |
assay at | Cavia porcellus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.60 | 4.5 | - |
assay at | Homo sapiens |
3.5.1.60 | 4.5 | - |
assay at | Mus musculus |
3.5.1.60 | 4.5 | - |
assay at | Oryctolagus cuniculus |
3.5.1.60 | 4.5 | - |
assay at | Cavia porcellus |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
3.5.1.60 | 0.00023 | - |
pH 4.5, 37°C, recombinant enzyme | Homo sapiens | [2-(ethylsulfonyl)phenyl][(2S)-4-(6-fluoro-1,3-benzothiazol-2-yl)-2-methylpiperazin-1-yl]methanone |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.60 | malfunction | pharmacological inhibitors of NAAA activity exert profound analgesic and antiinflammatory effects | Mus musculus |
3.5.1.60 | additional information | structure analysis of the enzme in complex with myristate, substrate binding structure, overview. The enzyme must disrupt the membrane to reach its embedded substrate, and helices alpha3 and alpha6 are likely candidates for this function | Oryctolagus cuniculus |
3.5.1.60 | additional information | the enzyme must disrupt the membrane to reach its embedded substrate, and helices alpha3 and alpha6 are likely candidates for this function | Homo sapiens |
3.5.1.60 | additional information | the enzyme must disrupt the membrane to reach its embedded substrate, and helices alpha3 and alpha6 are likely candidates for this function | Cavia porcellus |
3.5.1.60 | additional information | the enzyme must disrupt the membrane to reach its embedded substrate, and helices alpha3 and alpha6 are likely candidates for this function. Detergent-induced rearrangement generates the NAAA substrate-binding site | Mus musculus |