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CaCl2
-
added to optimized fluorescence assay
Mg2+
-
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
Ca2+
-
a calcium-associated enzyme
Ca2+
required for activity
Ca2+
-
required, cannot be replaced by Mg2+, Ba2+, Cu2+, Ca2+, Mn2+, Co2+, Zn2+ or Hg2+
Ca2+
-
two calcium binding sites, the higher affinity site being essential for hydrolytic activity and its removal is irreversible, the lower affinity site being responsible for catalytic activity with reversible binding of Ca2+
Ca2+
dependent on, Ca2+ is required for activity and is involved in the catalytic mechanism via coordinating residues Asp54, Asn168, Asn224, and Asp269, structure, overview
Ca2+
involved in catalysis, active site structure, overview
Ca2+
Asp269 and Glu53 participate in the ligation of catalytic Ca2+
Ca2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+, two Ca2+ binding sites
Ca2+
required for enzyme stability and activity
Ca2+
-
is essential for activity and stability of PON1, modulates oligomeric state
Ca2+
-
required for the catalysis
Ca2+
-
2 mM used in assay conditions
Ca2+
-
the enzyme has two Ca2+ binding sites
Ca2+
-
required for catalysis, bound at the active site, coordinating residues are E21 and D229
Ca2+
-
two calcium binding sites, the higher affinity site being essential for hydrolytic activity and its removal is irreversible, the lower affinity site being responsible for catalytic activity with reversible binding of Ca2+
Ca2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+, two Ca2+ binding sites
Ca2+
dependent on, catalytic Ca2+ ion
Ca2+
dependent on, PON1 has a six-blade beta-propeller fold with two calcium ions in its central tunnel. The structural Ca2+ is completely embedded inside the protein, and the catalytic Ca2+ is located at the bottom of the active site cavity. PTE Ca2+ binding structure comparisons
Ca2+
-
required for maximal activity
Ca2+
-
optimal concentration is 2 mM
Ca2+
-
essential for maintaining enzyme activity
Ca2+
-
essential activator of rat plasma enzyme, nonessential activator of liver microsomal enzyme
Cd2+
-
2 microM, 180% of initial activity
Cd2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Cd2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Cd2+
0.2 mM, more than 8fold increase in activity
Cd2+
-
the Mn2+-containing enzyme is about 30-fold more efficient with paraoxon as substrate and more stable than the Cd2+ counterpart, even though the Mn2+ affinity for the binuclear metal centre is apparently lower
Cd2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Co2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
Co2+
-
2 Zn2+ or Co2+ ions per subunit
Co2+
binuclear metalloenzyme
Co2+
-
activates, preferred divalent metal ion by recombinant His6-OPH
Co2+
the Co2+ form of OPH is the most active of the metal-liganded enzyme forms
Co2+
Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. A single Co2+ in the active site already provides a significant enhancement of the catalytic efficiency compared to Zn-PTE
Co2+
-
2 Zn2+ or Co2+ ions per subunit
Co2+
-
activity is highest with Co2+ present in the active site
Co2+
activates by 14.2% at 1 mM
Co2+
-
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
Co2+
bound at the beta-site
Co2+
2.2 Co2+ per active site in the enzyme that is purified from recombinant Pseudomonas putida
Co2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Co2+
the enzyme possesses a bi-cobalt active site
Fe2+
the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme
Fe2+
the enzyme is a natively heterobinuclear ironzinc metalloprotein, binding structure, overview
Fe2+
bound at the alpha-site
Mn2+
-
activates
Mn2+
the enzyme is activated with 0.025 mM Mn2+ at 37°C for 1 h
Mn2+
-
the Mn2+-containing enzyme is about 30-fold more efficient with paraoxon as substrate and more stable than the Cd2+ counterpart, even though the Mn2+ affinity for the binuclear metal centre is apparently lower
Mn2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
NaCl
-
added to optimized fluorescence assay
NaCl
-
B-type esterase has relatively higher paraoxonase activity and is stimulated to a greater degree by 1 M NaCl than the A allozyme
NaCl
-
paraoxonase activity of the B type isozyme is considerably higher and stimulated more by 1 M NaCl than A-type paraoxonase
NaCl
-
salt-stimulated activity
NaCl
activation effects of NaCl on PON1 activity and serum arylesterase activity, kinetics, overview
Ni2+
-
activates
Ni2+
activates by 23.5% at 1 mM
Ni2+
-
the enzyme depends on divalent metal ions with Co2+, Mg2+, and Ni2+ being the most effective
Ni2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Zn2+
the enzyme is a natively heterobinuclear iron-zinc metalloprotein, binding structure, overview
Zn2+
the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview
Zn2+
-
2 Zn2+ or Co2+ ions per subunit
Zn2+
the enzyme is a zinc metalloenzyme
Zn2+
the Zn2+ form of OPH is one of the most stable dimeric proteins ever identified
Zn2+
recombinant Zn-PTE contains only Zn2+ whereas Co-PTE has Zn2+ and Co2+ in equimolar amount, the later being located most likely in the labile beta-site. 0.05 mM ZnCl2 has a modest stabilizing effect, as Zn-PTE and Co-PTE retain respectively 38% and 27% of their activity 2 min after dilution. There are neither additives nor synergistic effect of ZnCl2 and beta-lactoglobulin
Zn2+
required, a metalloenzyme, the active site contains two divalent metal ions essential for its catalytic activity and also 6 amino acids, including four histidine, one aspartic acid and one lysine
Zn2+
-
2 Zn2+ or Co2+ ions per subunit
Zn2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Zn2+
-
the native enzyme contains two Zn2+ ions, and these metal ions can be substituted with Cd2+, Co2+, Ni2+, or Mn2+ without a loss of catalytic activity
Zn2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Zn2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
additional information
metal analysis of wild-type and recombinant enzymes, overview
additional information
-
metal analysis of wild-type and recombinant enzymes, overview
additional information
the my-hydroxo bridge between the metal ions initiates the hydrolytic reaction, roles of alpha- and beta-metal ions in catalysis, overview
additional information
-
the my-hydroxo bridge between the metal ions initiates the hydrolytic reaction, roles of alpha- and beta-metal ions in catalysis, overview
additional information
-
requirement for divalent metal ions, the activity of recombinant His6-OPH decreases in the series: Co2+, Ni2+, Mn2+, Cu2+, Zn2+
additional information
-
contains a binuclear metal center with two metals interactively involved in catalysis and/or structural functions
additional information
divalent cations are essential for activity
additional information
-
the enzyme is not affected by phosphotungstic acid/MgCl2
additional information
-
at 37°C, 1 mM Mg2+ and Mn2+ have no stimulatory effect on activity
additional information
architecture of active pocket of enzyme mPHP coordinates with two metal ions
additional information
no effect by Ca2+, Cr3+, Mg2+, Li+, and EDTA at 1 mM
additional information
no binding of Zn2+, Cl- and Ca2+ ions
additional information
-
no binding of Zn2+, Cl- and Ca2+ ions
additional information
the enzyme has a binuclear metal-centre. The activity depends on the presence of divalent metal cations, the highest activity is observed with Co2+. The binuclear centre is used to activate a bridging water molecule to a hydroxide ion and the substrate for nucleophilic attack by polarizing the phosphoryl-oxygen bond. The nucleophilic bridging hydroxide ion attacks the electrophilic centre (phosphorus or carbon) via a SN2 mechanism, forming transition states that bridge the two metals
additional information
the enzyme contains a binuclear metal centre with two divalent cations
additional information
-
the enzyme contains a binuclear metal centre with two divalent cations
additional information
enzyme Sb-PTE uses a binuclear metal center
additional information
structure of the binuclear metal center in Sb-PTE with coordinating nitrogens from the four histidine ligands, overview