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Cu2+
-
1 mM, increases aminoacylase activity to 107%
Na+
-
1 mM, increases aminoacylase activity to 136%
Ca2+
-
-
Ca2+
the enzyme contains 1.22 mol of Zn2+ and 0.17 mol of Ca2+ per mol of monomer enzyme protein
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
required, activity can be increased significantly by the addition of Co2+
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
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
inhibitory at concentration 1 mM
Co2+
when the enzyme is dialyzed against 50 mM EDTA (pH 7.5) for 10 h at 4°C and then against 50 mM sodium phosphate buffer (pH 7.5), the aminoacylase activity is decreased to less than 1.0%. The activity is restored by incubation in 50 mM sodium phosphate buffer (pH 7.5) containing ZnCl2, MnCl2, or CoCl2 at 4°C for 1 h. The restorative effect is dependent on the concentration of the metal ions. 88%, 23%, and 20% of activities are restored by adding 1.0 mM ZnCl2, 1.0 mM MnCl2, and 0.1 mM CoCl2, respectively
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
activates and stabilizes, 148% activity at 0.1 mM, tightly bound to the enzyme
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
activates free and immobilized enzyme
Co2+
-
0.01 mM, 1.1fold activation
Co2+
-
0.01 mM, 1.1fold activation. 0.1 mM, 1.3fold activation
CoCl2
-
relative activity of ACY is 286.2% when dipicolinic acid is removed
CoCl2
-
relative activity of ACY is 310% when EDTA is removed, 40.2% with EDTA
CoCl2
-
activates 2-3fold at 0.1 mM
CuCl2
-
relative activity of ACY is 22.9% when dipicolinic acid is removed
CuCl2
-
relative activity of ACY is 26.4% when EDTA is removed
Mg2+
-
1 mM, increases aminoacylase activity to 153%
Mn2+
-
-
Mn2+
-
1 mM, increases aminoacylase activity to 160%
Mn2+
-
activity can be increased by the addition of Mn2+
Mn2+
-
Mn2+ can substitute for zinc ions in AA1 without a substantial loss of activity
Mn2+
-
inhibitory at concentration 1 mM
Mn2+
-
Zn2+ substituted by Mn2+: increased activity (substrate: N-acetyl-L-methionine)
Mn2+
when the enzyme is dialyzed against 50 mM EDTA (pH 7.5) for 10 h at 4°C and then against 50 mM sodium phosphate buffer (pH 7.5), the aminoacylase activity is decreased to less than 1.0%. The activity is restored by incubation in 50 mM sodium phosphate buffer (pH 7.5) containing ZnCl2, MnCl2, or CoCl2 at 4°C for 1 h. The restorative effect is dependent on the concentration of the metal ions. 88%, 23%, and 20% of activities are restored by adding 1.0 mM ZnCl2, 1.0 mM MnCl2, and 0.1 mM CoCl2, respectively
MnCl2
-
relative activity of ACY is 125.3% when dipicolinic acid is removed
MnCl2
-
relative activity of ACY is 203.5% when EDTA is removed
Ni2+
-
AA3 is a metalloenzyme significantly activated by Co2+ and Ni2+
Ni2+
-
Zn2+ substituted by Ni2+: increased activity (substrate: N-acetyl-L-methionine)
Ni2+
110% relative activity at 0.005 mM
NiCl2
-
relative activity of ACY is 180.5% when dipicolinic acid is removed
NiCl2
-
relative activity of ACY is 200.1% when EDTA is removed
NiCl2
-
activates 2-3fold at 0.1 mM
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
restores activity after treatment with EDTA or phenanthroline
Zn2+
-
binding site structure, H206 and E146 are involved
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
Zn2+
the enzyme contains 1.22 mol of Zn2+ and 0.17 mol of Ca2+ per mol of monomer enzyme protein. When the enzyme is dialyzed against 50 mM EDTA (pH 7.5) for 10 h at 4°C and then against 50 mM sodium phosphate buffer (pH 7.5), the aminoacylase activity is decreased to less than 1.0%. The activity is restored by incubation in 50 mM sodium phosphate buffer (pH 7.5) containing ZnCl2, MnCl2, or CoCl2 at 4°C for 1 h. The restorative effect is dependent on the concentration of the metal ions. 88%, 23%, and 20% of activities are restored by adding 1.0 mM ZnCl2, 1.0 mM MnCl2, and 0.1 mM CoCl2, respectively
Zn2+
-
0.98 Zn2+ per enzyme molecule, tightly bound, involved in cataylsis
Zn2+
metalloenzyme, required for activity
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
120% relative activity at 0.0005 mM
Zn2+
activates 57% at 500 nM, 20% at 0.005 mM, but inhibits 61% at 2.5 mM
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
0.01 mM or 0.1 mM, 1.3fold activation
Zn2+
-
0.01 mM, 1.3fold activation
Zn2+
-
contains one Zn2+ per monomer, zinc-containing enzyme
ZnCl2
-
relative activity of ACY is 113.7% when EDTA is removed
ZnCl2
-
relative activity of ACY is 90.8% when dipicolinic acid is removed
additional information
-
metal removal completely inactivates AA3, whereas addition of Zn2+, Mn2+ or Fe2+ restores initial activity
additional information
-
metalloenzyme
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+
additional information
the enzyme activity is not affected by Ca2+ or Mg2+ at 0.5 mM
additional information
-
the enzyme activity is not affected by Ca2+ or Mg2+ at 0.5 mM