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Sn2+
-
10 mM, strong inhibitory effect
Ca2+
slight activation at 10 mM
Ca2+
-
0.5-1.0 mM, slight activation
Ca2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Ca2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Co2+
strong activation at 0.01-1.0 mM, inhibitory at 10 mM
Co2+
-
stimulatory at 0.01 mM, inhibitory above 0.1 mM
Co2+
-
0.03 mM, activates
Co2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Co2+
in a metal:protein ratio of 0.11:1, slightly activates the enzyme at 0.01-0.1 mM, 2.8fold activation at 1 mM in presence of 1 mM glutathione
Co2+
-
10 mM, moderate inhibitory effect
Co2+
-
metal ion required, Co2+ is the best activator
Co2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Co2+
or Mn2+, Zn2+, required. Maximal activity at 3 mM
Cu2+
-
0.1 mM, moderate inhibitory effect
Cu2+
-
10 mM, strong inhibitory effect
Fe2+
slight activation at 0.05 mM, complete inhibition at 1 mM
Fe2+
in a metal:protein ratio of 0.07:1
Mg2+
activates
Mg2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Mg2+
stimulation of the enzyme
Mn2+
required, best metal ion, the enzyme activity increases 27.6 times of the control level at 1 mM Mn2+, strong activation at 0.01-50 mM
Mn2+
-
0.25-1 mM activates
Mn2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM with substrates substance P and bradykinin
Mn2+
-
activates, sharp optimum at 0.37 mM
Mn2+
-
0.05 mM, 3-4fold activatiion
Mn2+
-
0.005 mM, 3fold activation
Mn2+
-
2 ions per enzyme molecule, ligand binding structure determination
Mn2+
-
may substitute for Co2+
Mn2+
-
wild-type and mutat R404A, binding of Mn2+ with a stoichiometry of 2 per monomer
Mn2+
2 mol of Mn2+ ions per mol of enzyme
Mn2+
required for activity
Mn2+
-
required, maximal activity at 0.05 mM
Mn2+
in a metal:protein ratio of 1:1, activates the enzyme 2.80fold at 0.1 mM with substrate substance P, maximal at 0.3 mM, 4.6fold activation at 1 mM in presence of 1 mM glutathione
Mn2+
-
the enzyme is double Mn2+-dependent for its activity
Mn2+
-
using the QM/MM method it is shown that XPNPEP1 employs two divalent manganese atoms (Mn(II)-Mn(II)) in the active site. The possibility of a single Mn(II) atom or other combination of divalent metal ions: Ca(II), Fe(II), Mg(II) is excluded
Mn2+
activates, required, Km values for Mn2+ are 0.0022 mM for the wild-type enzyme, 0.004 mM for mutant Y527F, and 0.0018 mM for mutant R535A. Kinetic analysis of MnCl2 activation of wild-type, Y527F and R535A hcAMPPs
Mn2+
-
1 mM, 6.8fold stimulates
Mn2+
-
the active site is internally located at the junction of the three domains and shows a di-metal coordination consistent with the presence of two catalytic manganese ions
Mn2+
activates at up to 5 mM, a trimetal manganese cluster is observed at the active site involving residues Asp260, Asp271, Glu384, Glu408, and His354, elucidating the binding structure and mechanism of inhibition by metal ions. Inhibitory at 8-15 mM. There is a Mn2+ ion concentration-dependent activity regulation pattern
Mn2+
-
0.3-0.4 mM, 4fold stimulation with Gly-Pro-Hyp as substrate
Mn2+
-
required, maximal activity at 0.05 mM
Mn2+
the activity of the enzyme depends critically on the presence of Mn2+. Reducing concentration of Mn2+ in reaction buffer from 1 mM to 0.006 mM reduces the activity of the enzyme by about 60%. Other divalent metal ions (Mg2+, Ca2+, Co2+, Ni2+ and Zn2+) fail to fully restore activity of the enzyme
Mn2+
stimulation of the enzyme, most effective at 4 mM
Mn2+
-
enhances activity, atomic absorption studies reveal the presence of Mn2+ in the protein as a co-factor
Mn2+
-
4-10 mM, activates hydrolysis of Gly-Pro-Hyp, beta-casomorphin or substance P
Mn2+
-
stimulates, optimal activity at 4 mM
Mn2+
activates 5fold at 0.01 mM, 2.5fold at 5 mM. The active site of PepP is involved in the binding of two Mn2+ ions
Mn2+
or Co2+, Zn2+, required. Maximal activity at 20 mM
Mn2+
-
required, activates
NaCl
increases the enzyme activity in the concentration range 0.5-3.0 M, suggesting that the enzyme is halophilic
NaCl
activates the wild-type enzyme at 160 mM, inhibits the enzyme mutant R353A at 160 mM
Ni2+
-
may substitute for Co2+
Ni2+
-
1 mM, 26% increase in activity
Zn2+
APP-1 is a dimer that uses dinuclear zinc at the active site
Zn2+
required, di-metal center, one metal ion (ZnA) is penta-coordinated and exhibits distorted trigonal bipyramidal geometry, whereas the other (ZnB) is tetra-coordinated and exhibits a tetrahedral geometry. Metal ZnA of Dr-smAPP is coordinated by O3 of phosphate ion, His285 Nepsilon2, and Glu328 Oepsilon1 in the equatorial plane and Asp221 Odelta2 and Glu314 Oepsilon2 in the axial sites. Metal ZnB of Dr-smAPP is coordinated by O3 of phosphate ion, Asp210 Odelta1, Asp221 Odelta1, and Glu328 Oepsilon2. Glu328 and Asp221 act as bidentate ligands and bind to both the metals
Zn2+
required, di-metal center, one metal ion (ZnA) is penta-coordinated and exhibits distorted trigonal bipyramidal geometry, whereas the other (ZnB) is tetra-coordinated and exhibits a tetrahedral geometry. Metal ZnA is coordinated by O1 of cacodylate ion, Glu335 Oepsilon2, Glu321 Oepsilon2, His292 Nepsilon2, and Asp223 Odelta2. Metal ZnB is coordinated by O1 of cacodylate ion, Glu335 Oepsilon1, Asp212 Odelta1, and Asp223 Odelta1. Glu335 and Asp223 act as bidentate ligands and bind to both the metals
Zn2+
in a metal:protein ratio of 0.11:1
Zn2+
-
1 mM, 2fold increase in activity
Zn2+
-
0.01 mM, moderate inhibitory effect
Zn2+
-
10 mM, strong inhibitory effect
Zn2+
-
mono-zinc-containing enzyme, lacks any of the typical metal binding motifs found in other zinc metalloproteases
Zn2+
or Mn2+, Co2+, required. Maximal activity at 0.4 mM
additional information
rXpmA is a metalloprotease
additional information
-
rXpmA is a metalloprotease
additional information
-
metalloenzyme, enzyme which is free of metals due to EDTA-treatment cannot be reactivated by addition of Co2+, Zn2+, or Mn2+
additional information
metalloprotease
additional information
-
metalloprotease
additional information
-
the active site contains a dinuclear metal binding site, the enzyme contains 12 metal atoms per molecule, 2 of which are Mn2+ ions
additional information
not activating: Mg2+, Zn2+, Na+, Ca2+
additional information
-
not activating: Mg2+, Zn2+, Na+, Ca2+
additional information
a metalloprotease
additional information
-
a metalloprotease
additional information
XPNPEP1 is a metallopeptidase
additional information
XPNPEP1 is a metallopeptidase
additional information
-
XPNPEP1 is a metallopeptidase
additional information
XPNPEP2 is a metallopeptidase
additional information
XPNPEP2 is a metallopeptidase
additional information
-
XPNPEP2 is a metallopeptidase
additional information
the enzyme activity is dependent on metal ions and influenced by different metal ions. This enzyme's pita-bread fold is commonly found in N-terminal amido-, imido-, and amidino-scissile bond-cleaving enzymes, and serves as a structural basis for the metal-dependent catalysis. Addition of Mn2+ significantly restores the Pa-PepP activity of the apoenzyme, while the limited enhancement of activity is observed upon addition of Ca2+ or Mg2+
additional information
structure modeling reveals that residues Thr273 and Thr383 do not directly interact with metal ions but may be important for their retention in the protein active site
additional information
-
activity of rTgAPP is enhanced by the addition of divalent cations
additional information
the active site of each subunit of puified recombinant TVMP50 contains two metals Ca2+ and Ni2+. The Ni2+ is likely also dragged from the IMAC resin purification. Additional Ca2+ atoms are detected bound in the structure, one on the N-terminal and two on the C-terminal domain. The conserved residues responsible for direct interaction with metallic ions are Glu407, Glu364, Asp232, Asp243, His328, and His335
additional information
-
the active site of each subunit of puified recombinant TVMP50 contains two metals Ca2+ and Ni2+. The Ni2+ is likely also dragged from the IMAC resin purification. Additional Ca2+ atoms are detected bound in the structure, one on the N-terminal and two on the C-terminal domain. The conserved residues responsible for direct interaction with metallic ions are Glu407, Glu364, Asp232, Asp243, His328, and His335