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Na+
the sodium ion is coordinated by the main-chain carbonyl oxygen atoms of A461, G462, Y465 and three water molecules in an octahedral geometry
Ca2+
-
inhibits activity
Ca2+
-
weakly inhibits activity
Cd2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Cd2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Cd2+
-
the bimetallic enzyme contains either 2 Zn2+ or 2 Cd2+ or Zn2+ and Cd2+
Cd2+
-
can substitute for one or both of the Zn2+ ions
Co2+
-
enhances activity
Co2+
activates to 228% activity at 0.1 mM
Co2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Co2+
-
CoCl2 at 1mM increases the specific activity 18fold
Co2+
-
reactivates the apoenzyme
Co2+
-
highly activating, about 5fold at 1-10 mM
Co2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Co2+
-
580% relative activity in the presence of 2.0 mM Co2+
Co2+
-
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Co2+
-
65% of activity of zinc enzyme
Co2+
-
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than the other way round, which suggests two metal-binding sites with different functions
Co2+
-
spectroscopically distinct cobalt sites in heterodimetallic enzymes, implications for substrate binding
Co2+
2 Co2+ bound at the dinuclear active site, can be substituted by Zn2+, binding mode
Co2+
can substitute for Zn2+
Co2+
-
Co2+ can substitute for Cd2+ in the bimetallic enzyme
Co2+
-
can substitute for one or both of the Zn2+ ions
Co2+
-
can substitute for one or both Zn2+ ions
Co2+
-
Co2+ can substitute for Zn2+ at the the dinuclear active site of the enzyme
Co2+
-
the dinuclear active site of the enzyme contains Co2+ and/or Zn2+
Cu2+
-
weakly inhibits activity
Cu2+
-
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Cu2+
-
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than the other way round, which suggests two metal-binding sites with different functions
Mg2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+, binds at the active site
Mg2+
-
MgCl2 shows an optimal concentration at 10 mM that increases specific activity by 12fold
Mg2+
-
activates 2.9fold at 1 mM, 3.7fold at 10 mM
Mg2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Mg2+
-
258% relative activity in the presence of 2.0 mM Mg2+
Mn2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+, binds at the active site
Mn2+
-
recombinant LAP activity is progressively activated by MnCl2 (0.001-10 mM) with an optimum at 1 mM, yielding a 43fold increase
Mn2+
-
highly activating, 5.6fold at 1-10 mM
Mn2+
at pH 9.5, the active site contains two metal ions, one identified as Mn2+ or Zn2+ at site 1, and the other as Zn2+ at site 2. Mn2+ has a significant activation effect when bound to site 1 of ppLAP
Mn2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Mn2+
-
510% relative activity in the presence of 2.0 mM Mn2+
Mn2+
-
58% of activity of zinc enzyme
Ni2+
-
inhibits activity
Ni2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Ni2+
-
activates 3.5fold at 1 mM, 3.8fold at 10 mM
Ni2+
Mycobacterium tuberculosis LAP exhibits maximum activity in the presence of Ni2+, but it is active in the presence of a broad range of other metals
Ni2+
-
metallopeptidase, prefers Mn2+ or Mg2+, lower activity with Ni2+, Co2+, or Cd2+
Ni2+
-
can replace zinc, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of different metal ions, sequence of addition effects activity
Zn2+
-
-
Zn2+
-
dinuclear zinc active center
Zn2+
zinc-metalloaminopeptidase, 2 Zn2+ per enzyme molecule
Zn2+
-
2 ions bound per enzyme molecule, binding to Glu354
Zn2+
-
metallopeptidase, dimetal site structure, overview
Zn2+
-
ZnCl2 modestly affects the enzymatic activity
Zn2+
two active-site positively charged zinc ions are coordinated by negatively charged side-chain oxygen atoms of three aspartate residues (D263, D281, D340) and one glutamate residue (E342), the side-chain nitrogen atom of K258 and two water molecules in a distorted octahedral coordination geometry
Zn2+
-
0.05 mM, required for activity
Zn2+
LAP is zinc-dependent. At pH 9.5, the active site contains two metal ions, one identified as Mn2+ or Zn2+ at site 1, and the other as Zn2+ at site 2
Zn2+
-
bound zinc ion interacts directly with substrate during catalysis but not during substrate binding, contains 2 mol zinc per mol enzyme but only one site has to be occupied in order to faciliate catalysis
Zn2+
-
if copper or cobalt are added prior to zinc in sequential substitution experiments, activation is two orders of magnitude higher than in the opposite sequence, which suggests two metal-binding sites with different functions
Zn2+
-
2 mol zinc per mol enzyme
Zn2+
-
no loss of zinc upon photoinactivation
Zn2+
-
zinc can be replaced by other metals, nonidentical, interacting metal-binding sites, magnetic circular dichroism study, hyperactivation by sequential addition of metal ions, sequence of addition effects activity
Zn2+
2 Zn2+ bound at the dinuclear active site, can be substituted by Co2+, binding mode
Zn2+
bound in the active site, binding structure, bridged bimetallic enzyme
Zn2+
-
the bimetallic enzyme contains either 2 Zn2+ or 2 Cd2+ or Zn2+ and Cd2+
Zn2+
AAP is a metalloenzyme containing two Zn2+ per enzyme molecule
Zn2+
-
dinuclear Zn2+ metal center
Zn2+
dinuclear Zn2+ metal center, the binding of Zn2+ to the E151H mutant is much more weak than to the wild-type enzyme
Zn2+
-
the dinuclear active site of the enzyme contains Co2+ and/or Zn2+
Zn2+
-
the enzyme is a two-zinc metallopeptidase, zinc-binding involved residues His97, Asp117, Glu152, Asp179, and His256
Zn2+
the enzyme is bridged bimetallic, the metal ions are involved in the reaction, overview
Zn2+
the metallopeptidase requires two divalent metal ions per enzyme molecule for full activity, binuclear metal center activation and reaction mechanism
Zn2+
-
zinc-dependent metallopeptidase, Co2+ can substitute for Zn2+ at the the dinuclear active site of the enzyme
Zn2+
-
zinc-metallopeptidase, 2 ions per enzyme molecule
Zn2+
AAP is a binuclear zinc enzyme, Zn2+ is essential for its enzymatic activity
Zn2+
two zinc ions in close proximity have been identified to form the metal component of the active site
Zn2+
required, 2 Zn2+ per active site
additional information
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API and APII are metallopeptidases
additional information
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metallopeptidase, the kind of bound metal ion determines the substrate specificity
additional information
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no relevant stimulatory effect with NiCl2, FeSO4 and CuSO4
additional information
the enzyme is a metallopeptidase, most active with Mn2+, no activation by Zn2+
additional information
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the enzyme is a metallopeptidase, most active with Mn2+, no activation by Zn2+
additional information
ppLAP requires the presence of divalent metal ions for its activity, in particular Zn2+ and/or Mn2+. At pH 5.2, the active site of ppLAP is highly disordered and metal ions are absent, most probably due to full protonation of one of the metal-interacting residues, Lys267
additional information
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metallopeptidase, the kind of bound metal ion determines the substrate specificity
additional information
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not stimulated by Zn2+ or Ca2+
additional information
-
metal ion interacts directly with the substrate atoms, as shown by multiple inhibitor studies
additional information
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bimetallic enzyme, binding conformations, overview
additional information
detailed metal binding structure analysis, overview, the first metal ion in the dinuclear metal center is in a hexacoordinate/pentacoordinate equilibrium, while the second metal ion is six-coordinate
additional information
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detailed metal binding structure and kinetic analysis with recombinant wild-type and mutant enzymes, overview
additional information
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metallopeptidase, the kind of bound metal ion determines the substrate specificity
additional information
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metalloprotein active site, structure and mechanism overview