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Cobalt
-
2 atoms per subunit are required for optimum activity
Na+
-
the enzyme contains five Na+ ions, four organized in two dinuclear centres and one located in an external position of the homodimer, each subunit contains two ions Na+, binding structure, overview
Ca2+
-
can substitute for Mn2+ by less than 30%
Co2+
-
activates
Co2+
-
can substitute for Mn2+ by less than 30%
Co2+
-
activates, preferred metal ion
Co2+
-
requires Co2+ in addition to one cobalt atom bound per subunit
Co2+
dinuclear metal cluster in the active site, binding of 2 Co2+ per subunit
Co2+
-
one Co-bound dinuclear metal cluster per monomer, Co1 is the tight binding, Co2 the loose binding metal center. Wild-type exhibits maximal activity in presence of 0.5 mM Co2+, less than 20% residual activity with 10 mM Co2+
Co2+
-
metalloenzyme, required for activity, a homodimer having one Co-bound dinuclear metal cluster per monomer with one tightly bound Co1 and one loosely bound Co2 cobalt site, 5 amino acids that function as metal-binding residues: His284 and Glu313 solely bind to the first cobalt centre, Co1, Asp209 to the second cobalt centre, Co2, and Asp220 and Glu327 to both Co2+ ions
Co2+
-
highly activating, one Co2+ per enzyme subunit
Fe2+
-
best activating divalent ion
Mg2+
-
can substitute for Mn2+ by less than 30%
Mn2+
-
requires divalent cations for activity, most active with manganese
Mn2+
-
the enzyme harbors binuclear Mn2+ ions within the active site
Mn2+
-
stabilization of enzyme against inhibition by Ni2+
Mn2+
-
presence of 1 mM in the assay
Mn2+
-
required for activity
Mn2+
-
dependent on, metallopeptidase, complex formation with anthracyclines
Mn2+
-
required for enzyme activation
Mn2+
-
dependent on, best divalent cation
Mn2+
-
metalloenzyme, required for activity, each subunit contains two ions Mn2+, binding structure, overview
Mn2+
-
metalloenzyme, required for activity, the active site Mn2+ cation is simultaneously ligated to the prolyl carboxyl group and the amido oxygen of the preceding residue of the trans X-Pro dipeptides
Mn2+
-
required, plays an important role in the activation and functional regulation of the enzyme
Mn2+
-
40 mM, dependent on
Mn2+
-
activation of prolidase requires preincubation with 2 mM Mn2+
Mn2+
-
requires divalent cations for activity, most active with manganese
Mn2+
the protein can host two metal ions in the active site of each constituent monomer, two different kinds of metals, Mn and Zn can be simultaneously present in the protein active sites with the protein partially maintaining its enzymatic activity. Dimeric metalloenzyme, one of the two active sites is occupied by two Zn ions and the second one by one Zn and one Mn ion, in both dinuclear units a histidine residue is bound to a Zn ion, binding structure, overview
Mn2+
-
requires divalent cations for activity, most active with manganese
Mn2+
two preferred metal cations: zinc and manganese, the substrate Leu-Pro is preferred with zinc, whereas Arg-Pro is preferred with manganese
Mn2+
maximum activity in presence of Mn2+ ions, addition of 1 mM to the assay
Mn2+
-
Co2+ can be replaced by Mn2+
Mn2+
-
requires divalent cations for activity, most active with manganese
Mn2+
-
activation of prolidase requires preincubation with 2 mM Mn2+
Mn2+
maximum activity in presence of Mn2+ ions, addition of 1 mM to the assay
Zn2+
-
can substitute for Mn2+ by less than 30%
Zn2+
the protein can host two metal ions in the active site of each constituent monomer, two different kinds of metals, Mn and Zn can be simultaneously present in the protein active sites with the protein partially maintaining its enzymatic activity. Dimeric metalloenzyme, one of the two active sites is occupied by two Zn ions and the second one by one Zn and one Mn ion, in both dinuclear units a histidine residue is bound to a Zn ion, binding structure, overview
Zn2+
-
requires divalent cations for activity, most active with zinc
Zn2+
-
required for optimum activity
Zn2+
two preferred metal cations: zinc and manganese, the substrate Leu-Pro is preferred with zinc, whereas Arg-Pro is preferred with manganese
Zn2+
2 Zn2+ bound to the subunit in the crystallized enzyme only replacing the Co2+ ions, binding structure via 5 coordinates
Zn2+
-
interaction with amino acid residues D209, D220, H284, E313 and E327, overview
additional information
-
OPAA-2 has a conserved binuclear metal center
additional information
determination of enzyme samples metal contents, overview
additional information
-
determination of enzyme samples metal contents, overview
additional information
-
no significant effect by Ca2+ at 1 mM
additional information
the substrate specificity is dependent on the catalytic metal cation, molecular modeling, overview
additional information
-
the enzyme requires divalent cations for activity
additional information
-
PepQ shows increased activity under high salt conditions
additional information
-
the enzyme contains a dinuclear metal center bridged by a water molecule or hydroxide ion. The metal cluster is essential for the activation of catalysis. It functions to activate a nucleophile for the reaction, as well as participating in substrate binding and stabilizing the transition state. The dipeptidase is maximally active with the addition of the divalent cations Co2+ and Mn2+ and it cannot be substituted with other divalent cations, i.e Mg2+, Ca2+, Fe2+, Ni2+, Cu2+, or Zn2+, under aerobic conditions