Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cd2+
-
functional in the presence of, highest activity at pH 9
KCl
stimulates, optimal at 50 mM
Zinc
-
zinc-metallopeptidase, contains the HEXXH motif
Ba2+
-
slightly stimulated at 1 mM (111.6% activity)
Ba2+
-
shows slight activation at 0.1 mM
Ca2+
-
activation
Ca2+
-
shows slight activation at 0.1 mM
Ca2+
-
enzyme not functional in the presence of
Co2+
activates at 0.1-1.0 mM, inhibitory at 1.0-10 mM
Co2+
-
39% activation at 2 mM, 40% inhibition at 10 mM
Co2+
-
122% activity increase at 1 mM
Co2+
-
activates at 2 mM, inhibits at 10 mM and above
Co2+
activates moderately
Co2+
activates to 228% activity at 0.1 mM
Co2+
two ions per subunit, one exchangeable metal site can be occupied by Zn2+ or Mg2+, Co2+, or Mn2+, while the second, tight binding site can be occupied only by Zn2+ or Co2+, overview
Co2+
47.8fold activity increase at 1 mM
Co2+
597fold activation at 1 mM compared with non-metal ion-supplemented condition
Co2+
activates best at 1 mM
Co2+
addition of the ion prior to mixing with substrate increases activity up to 24fold
Co2+
-
binds at metal site 1
Co2+
optimally stimulates at 0.5-10 mM
Co2+
-
1 mM, 5.3fold activation
Co2+
-
stimulates by 100%
Co2+
-
enzyme not functional in the presence of
Cu2+
strong inhibitory effect
Cu2+
4fold activation at 0.1 mM compared with non-metal ion-supplemented condition
Fe2+
-
15% activation at 2 mM, 55% inhibition at 10 mM
Fe2+
12fold activation at 1 mM compared with non-metal ion-supplemented condition
K+
-
activates at 10-20 mM
Mg2+
activates at 0.1-10 mM
Mg2+
two ions per subunit, one exchangeable metal site can be occupied by Zn2+ or Mg2+, Co2+, or Mn2+, while the second, tight binding site can be occupied only by Zn2+ or Co2+, overview
Mg2+
10.9fold activity increase at 1 mM
Mg2+
maximum activity of the apoenzyme is observed in the presence of Mg2+, Mn2+, and Zn2+
Mg2+
-
slightly stimulated at 1 mM (122.7% activity)
Mg2+
120fold activation at 10 mM compared with non-metal ion-supplemented condition
Mg2+
activates at 1-10 mM
Mg2+
-
activity is increased at 0.05 mM, inhibition at 0.5 mM
Mg2+
-
slightly activates the enzymatic activity at concentrations from 0.1 to 1 mM
Mg2+
LAP activity is progressively enhanced by the addition of Mg2+ in the range of 0.001 mM to 1 mM
Mg2+
addition of the ion prior to mixing with substrate increases activity up to 8fold
Mg2+
-
binds at metal site 1
Mg2+
about 3.5fold activation at 0.5 mM, metallopeptidase
Mg2+
-
about 2fold activation at 0.5 mM for the recombinant enzyme and about 4fold for the wild-type enzyme in cell extract, metallopeptidase
Mg2+
-
1 mM, 4.7fold activation
Mg2+
-
enzyme not functional in the presence of
Mg2+
magnesium containing metallopeptidase
Mn2+
activates at 0.1-1.0 mM, inhibitory at 1.0-10 mM
Mn2+
activates, best divalent cation
Mn2+
absolutely dependent on
Mn2+
Km is 0.00056 mM with substrate Cys-Gly, two ions per subunit, one exchangeable metal site can be occupied by Zn2+ or Mg2+, Co2+, or Mn2+, while the second, tight binding site can be occupied only by Zn2+ or Co2+, overview
Mn2+
64.3fold activity increase at 1 mM
Mn2+
maximum activity of the apoenzyme is observed in the presence of Mg2+, Mn2+, and Zn2+
Mn2+
maximal activation at 5 mM. 1849fold activation at 10 mM compared with non-metal ion-supplemented condition
Mn2+
activates at 0.1-1 mM
Mn2+
-
activity is increased at 0.05 mM, inhibition at 0.5 mM
Mn2+
-
shows slight activation at 0.1 mM
Mn2+
LAP activity is progressively enhanced by the addition of Mn2+ in the range of 0.001 mM to 1 mM
Mn2+
addition of the ion prior to mixing with substrate increases activity up to 24fold
Mn2+
-
binds at metal site 1
Mn2+
about 4fold activation at 0.05 mM, metallopeptidase
Mn2+
-
about 2fold activation at 0.05 mM for the recombinant enzyme and about 4fold for the wild-type enzyme in cell extract, metallopeptidase
Mn2+
maximal (5fold) activation at 0.5 mM or higher
Mn2+
-
1 mM, 3.9fold activation
Mn2+
-
0.2 mM, increases activity by 7fold
Mn2+
-
activates, best metal ion
Mn2+
PepA requires Mn2+ for full activity, 2 Mn2+ ions occupy the metal binding site
Na+
-
activates at 10-20 mM
Ni2+
activates at 0.1-1.0 mM, inhibitory at 1.0-10 mM
Ni2+
493fold activation at 10 mM compared with non-metal ion-supplemented condition
Ni2+
activates at 1-10 mM
Ni2+
addition of the ion prior to mixing with substrate increases activity up to 10fold
Ni2+
-
functional in the presence of, highest activity at pH 7
Zn2+
activates at 0.1-1.0 mM, inhibitory at 1.0-10 mM
Zn2+
-
2 mM: 184.3% activity in crude enzyme solution
Zn2+
-
258% activity increase at 1 mM
Zn2+
-
6-12 gatom per mol
Zn2+
-
active site bound, coordination is mainly due to steric effects not electrostatic and/or electronic interactions, bimetallic complex, modeling, Ala333 is involved, functional study
Zn2+
bizinc hydrolase, zinc coordination and binding structure
Zn2+
two ions per subunit, one exchangeable metal site can be occupied by Zn2+ or Mg2+, Co2+, or Mn2+, while the second, tight binding site can be occupied only by Zn2+ or Co2+, overview
Zn2+
-
zinc-metallopeptidase, two Zn2+ per protomer, the zinc bound at residue 488 can be exchanged for the less preferable Mn2+, Co2+, or Mg2+, dimetal site structure involving Asp332, Asp255, Asp273, Lys250, and Glu334 for binding of the two catalytic zinc ions, overview
Zn2+
strong inhibitory effect
Zn2+
12.1fold activity increase at 1 mM
Zn2+
-
a zinc metallopeptidase
Zn2+
maximum activity of the apoenzyme is observed in the presence of Mg2+, Mn2+, and Zn2+
Zn2+
LAP contains two Zn2+ ions in the active site
Zn2+
-
A-LAP ia a zinc-metallopeptidase
Zn2+
-
a zinc metallopeptidase
Zn2+
leucine aminopeptidases (LAPs) are zinc-containing metalloproteinases
Zn2+
-
contains 4 mol of tightly bound Zn2+
Zn2+
bound to the enzyme as native cofactor
Zn2+
inhibitory at 10 mM, slightly activating at 1 mM
Zn2+
-
10 nM activates over 30%, inhibits above 0.005 mM
Zn2+
-
metallopeptidase, contains the conserved motif HEXXH(18X)E
Zn2+
-
Zn2+ seem to be its metal cofactor
Zn2+
LAP enzyme activity is increased in the presence of 0.01 mM Zn2+
Zn2+
addition of the ion prior to mixing with substrate increases activity up to 4fold
Zn2+
-
binds at metal sites 1 and 2
Zn2+
-
zinc-metallopeptidase
Zn2+
-
putative binding residues are Asp347 and Glu429
Zn2+
-
metallopeptidase, bound by residues Asp347 and Glu429
Zn2+
-
enzyme not functional in the presence of
Zn2+
-
2 mol of Zn2+ per mol of enzyme
Zn2+
-
11.4 gatom per mol
Zn2+
-
zinc-containing metallopeptidase
Zn2+
-
zinc-metallopeptidase, two Zn2+ per protomer
additional information
AcLAPr activity is progressively enhanced by Ni2+, Mn2+, Mg2+, Zn2+, and Co2+ but not by Ca2+. Among the divalent metal ions tested, Ni2+ (0.1-1.0 mM) increases AcLAPr activity the most by 5.5fold. Higher concentrations of all metal ions of 10 mM, except of Mg2+, inhibit AcLAPr activity
additional information
-
AcLAPr activity is progressively enhanced by Ni2+, Mn2+, Mg2+, Zn2+, and Co2+ but not by Ca2+. Among the divalent metal ions tested, Ni2+ (0.1-1.0 mM) increases AcLAPr activity the most by 5.5fold. Higher concentrations of all metal ions of 10 mM, except of Mg2+, inhibit AcLAPr activity
additional information
-
metallopeptidase
additional information
-
no effect by K+ and Na+
additional information
the enzyme is strongly dependent on metal divalent cations
additional information
-
the enzyme is strongly dependent on metal divalent cations
additional information
metallopeptidase
additional information
-
metallopeptidase
additional information
unaffected by Zn2+ after removal of bound metal ions, while Mn2+ can restore activity
additional information
-
unaffected by Zn2+ after removal of bound metal ions, while Mn2+ can restore activity
additional information
-
the enzyme contains no disulfide bonds
additional information
-
metallopeptidase
additional information
-
metallopeptidase
additional information
-
metallopeptidase
additional information
-
metallopeptidase
additional information
-
metallopeptidase
additional information
metalloprotease, metal coordination in the active site and apo LAP-A, overview
additional information
-
metallopeptidase
additional information
-
the exopeptidase contains two metal-binding sites, a readily exchangeable site and a tight binding site. The enzyme retains activity when the metal ion is removed from site 1, while removal of metal ions from both sites results in an inactive apoenzyme that cannot be reactivated by the addition of divalent metal cations. The metal ion at site 1 is readily exchangeable with several divalent metal ions and displays a preference in the order of preference Zn2+, Mn2+, Co2+, Mg2+. While it is likely that native PfLAP contains a Zn2+ in site 2. the type of metal ion present at site 1 influences not only the catalytic efficiency of the enzyme for peptide substrates but also the mode of binding by bestatin, a metal-chelating inhibitor of M17 aminopeptidases with antimalarial activity
additional information
metallo-exopeptidase, enzyme activity is dependent on divalent metal ions best activation at 0.1-1 mM metal ion. M17 family of metalloproteinase contains two metal-binding sites having different affinities for metal ions
additional information
-
metallo-exopeptidase, enzyme activity is dependent on divalent metal ions best activation at 0.1-1 mM metal ion. M17 family of metalloproteinase contains two metal-binding sites having different affinities for metal ions
additional information
the enzyme is relatively tolerant to Mn2+ which is enriched in hydrothermal vent fluids
additional information
enzyme is a metallopeptidase
additional information
-
metallopeptidase
additional information
-
metallopeptidase
additional information
a metalloexopeptidase, TpLAP activity is metal-ion dependent and strongly enhanced by the addition of Mn2+ and Co2+. In contrast, Mg2+, Zn2+, Ca2+, and Ba2+ do not influence enzymatic activities
additional information
-
a metalloexopeptidase, TpLAP activity is metal-ion dependent and strongly enhanced by the addition of Mn2+ and Co2+. In contrast, Mg2+, Zn2+, Ca2+, and Ba2+ do not influence enzymatic activities
additional information
-
the enzyme activity strongly depends on metal ions, only slight activition by Fe2+, Mg2+, Ca2+, Cu2+, and Zn2+
additional information
LAP1 is a metallopeptidase
additional information
metalloprotease, metal coordination in the active site and apo LAP-A, overview. The metal-free apo TbLAP-A form shows a disordered active-site loop (aa 293 to 305)
additional information
metalloprotease, metal coordination in the active site and apo LAP-A, overview