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Literature summary for 3.5.1.14 extracted from
- Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel (2009), Biochim. Biophys. Acta, 1794, 1049-1057.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Mus musculus |
| expression of His6-tagged AA3 in HEK-293 cells | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D68A | site-directed mutagenesis of AA3, the mutant is inactive | Mus musculus |
| E177A | site-directed mutagenesis of AA3, the mutant is inactive | Mus musculus |
| E24A | site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview | Mus musculus |
| H116A | site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview | Mus musculus |
| H21A | site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview | Mus musculus |
| H21D | site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview | Mus musculus |
| N70A | site-directed mutagenesis of AA3, the mutant is active | Mus musculus |
| R63A | site-directed mutagenesis of AA3, the mutant is inactive | Mus musculus |
| R71A | site-directed mutagenesis of AA3, the mutant is active | Mus musculus |
| Y287A | site-directed mutagenesis of AA3, the mutant is inactive | Mus musculus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics of wild-type AA3 in presnece of different metal ions, overview | Mus musculus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | three-dimensional modelling of Co2+ binding structure. AA3 is a metalloenzyme significantly activated by Co2+ and Ni2+. Cobalt increases the Vmax several times and decreases the Km of wild-type AA3. Co2+ can substitute for zinc ions in AA1 without a substantial loss of activity. Wild-type mouse AA3 expressed in Escherichia coli does not contain cobalt | Mus musculus |  |
| Mn2+ | Mn2+ can substitute for zinc ions in AA1 without a substantial loss of activity | Mus musculus | |
| additional information | determination of metal contents, overview. Metal removal completely inactivates AA3, whereas addition of Zn2+, Mn2+ or Fe2+ restores initial activity. A putative metal binding site is formed by His21, Glu24 and His116. No effect on AA3 activity by Zn2+, Mn2+, Fe2+, Cd2+, Mg2+, Ca2+, K+ and Na+ | Mus musculus | |
| additional information | metal removal completely inactivates AA3, whereas addition of Zn2+, Mn2+ or Fe2+ restores initial activity | Homo sapiens | |
| Ni2+ | AA3 is a metalloenzyme significantly activated by Co2+ and Ni2+ | Mus musculus | |
| Zn2+ | required | Homo sapiens | |
| Zn2+ | AA1 is a Zn2+ -metalloprotein containing stoichiometric amounts of this metal per monomer. Recombinant AA3 expressed in Escherichia coli contains 0.35 zinc atoms per monomer, but Zn2+ does not affect AA3 activity | Mus musculus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Mus musculus | AA1 similar to AA3 is involved in deacetylation of N-acetyl-aromatic amino acids and mercapturic acids | ? | - |
? | |
| N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O | Mus musculus | a metabolite of a xenobiotic trichloroethylene, substrate of AA3 | acetate + 1,2-dichlorovinyl-L-cysteine | - |
? | |
| N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O | Homo sapiens | a metabolite of a xenobiotic trichloroethylene, substrate of AA3 | acetate + 1,2-dichlorovinyl-L-cysteine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | no AA3 in wild-type HEK-293 cells | Homo sapiens | - |
| renal proximal tubule | high expression level of AA1 and AA3 | Mus musculus | - |
| renal proximal tubule | high expression level of AA3 | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | AA1 similar to AA3 is involved in deacetylation of N-acetyl-aromatic amino acids and mercapturic acids | Mus musculus | ? | - |
? | |
| additional information | AA3 residues Arg63, Asp68, Asn70, Arg71, Glu177 and Tyr287 are potentially involved in catalysis/substrate binding | Mus musculus | ? | - |
? | |
| N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O | a metabolite of a xenobiotic trichloroethylene, substrate of AA3 | Mus musculus | acetate + 1,2-dichlorovinyl-L-cysteine | - |
? | |
| N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O | a metabolite of a xenobiotic trichloroethylene, substrate of AA3 | Homo sapiens | acetate + 1,2-dichlorovinyl-L-cysteine | - |
? | |
| N-acetyl-L-tyrosine + H2O | - |
Mus musculus | acetate + L-tyrosine | - |
? | |
| N-acetyl-L-tyrosine + H2O | - |
Homo sapiens | acetate + L-tyrosine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AA1 | - |
Mus musculus |
| AA3 | - |
Mus musculus |
| AA3 | - |
Homo sapiens |
| aminoacylase 1 | - |
Mus musculus |
| aminoacylase 3 | - |
Mus musculus |
| aminoacylase 3 | - |
Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Mus musculus |
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Release 2023.1 (January 2023)
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