EC Number   |
Metals/Ions |
Reference |
|---|
   3.5.1.114 | Co2+ |
Co2+ and to a lesser extent Ni2+ increases activity several times in comparison with intact wild type AA3. Co2+ drastically increases the rate of deacetylation of N-acetyl-1,2-dichlorovinyl-L-cysteine and significantly increased the toxicity of Ac-DCVC in the HEK293T cells expressing wt-AA3. Aminoacylase 3 is a metalloenzyme significantly activated by Co2+ and Ni2+. The Co2+ -activated enzyme contains about 1 cobalt atom per monomer and trace amounts of zinc and other metals indicating that cobalt completely replaces them from the enzyme |
711284 |
| 3.5.1.114 | Co2+ |
metalloenzyme, highly activating |
723787 |
| 3.5.1.114 | Co2+ |
required |
733862 |
| 3.5.1.114 | more |
enzyme does not require metal ions |
679474 |
| 3.5.1.114 | more |
Mn2+, Fe2+, Cd2+, Mg2+, Ca2+, K+ and Na+ do not significantly alter activity |
711284 |
| 3.5.1.114 | Ni2+ |
Co2+ and to a lesser extent Ni2+ increases activity several times in comparison with intact wild type AA3. Co2+ drastically increases the rate of deacetylation of N-acetyl-1,2-dichlorovinyl-L-cysteine and significantly increased the toxicity of Ac-DCVC in the HEK293T cells expressing wt-AA3. Aminoacylase 3 is a metalloenzyme significantly activated by Co2+ and Ni2+ |
711284 |
| 3.5.1.114 | Zn2+ |
Wild type mouse aminoacylase 3 expressed in Escherichia coli contains 0.35 zinc atoms per monomer |
711284 |
