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Ag+
-
1 mM, stimulates activity up to 120%
Fe3+
-
1 mM, stimulates activity up to 348%
Hg2+
-
1 mM, can replace Ca2+ in activation
Se2+
activates 158% at 0.2 mM
Triton X-100
activates slightly at 0.5-1 mM
Tween-20
activates slightly at 1 mM
Ba2+
-
1 mM, 216% of initial activity
Ba2+
activates 181% at 0.2 mM
Ba2+
the enzyme is activated slightly in the presence of BaCl2
Ba2+
1 mM, 139% of initial activity
Ca2+
presence of Ca2+ increases thermostability
Ca2+
-
1 mM, 306% of initial activity. Presence of Ca2+ enhances thermoactivity and thermostability
Ca2+
Aspergillus luchuensis var. saitoi
-
activation, optimum concentration 0.3 mM
Ca2+
-
1 mM, activity is enhanced by 1209%
Ca2+
strong sigmoidal CaCl2 concentration dependent relation. Optimal catalysis at 0.5-1.0 mM Ca2+
Ca2+
-
optimum Ca2+ concentration at 0.6 mM
Ca2+
presence of Ca2+ enhances PelA stability in NaOH-glycine buffer, pH 9. About 60% activity is retained under incubation at 65°C with 0.3 mM CaCl2
Ca2+
activates 208% at 0.2 mM
Ca2+
absolute requirement
Ca2+
required for activity
Ca2+
-
restores activity of the EGTA-inactivated enzyme
Ca2+
-
optimal concentration: 0.4 mM
Ca2+
required for activity on pectic substrates, maximal activity at 0.5-0.75 mM CaCl2. Only 9% of maximal activity at 10 mM CaCl2
Ca2+
-
structurally essential
Ca2+
-
dependent on, binding structure, overview
Ca2+
Ca2+ is not required for activity on pectic substrates
Ca2+
-
optimum concentration at 0.6 mM
Ca2+
-
absolute requirement
Ca2+
-
maximal activity at 0.5-1 mM CaCl2
Ca2+
-
71% of maximal activity in absence of Ca2+
Ca2+
activity is not changed
Ca2+
-
optimum Ca2+ concentration at 2.0 mM
Ca2+
the enzyme in the absence of substrate binds a single calcium ion, two additional calcium ions bind between enzyme and substrate carboxylates occupying the +1 subsite in the Michaelis complex
Ca2+
activates 263% at 0.2 mM
Ca2+
required, activates the recombinant enzyme from Pichia pastoris by 26%
Ca2+
1 mM, 257% of initial activity
Ca2+
activity is lost at low pH because protonation of aspartates results in the loss of the two catalytic calcium-ions causing a profound failure to correctly organise the Michaelis complex
Ca2+
activity of wild-type peaks at 1 mM Ca2+, and declines with the increase in Ca2+concentration
Ca2+
presence of Ca2+ stimulates a change in tertiary structure. Binding of Ca2+ and polygalacturonic acid to the active site may occur independently
Ca2+
BxPEL1 shows full dependency
Ca2+
-
optimal activity in presence of 2.0-4.0 mM Ca2+. No activity when Ca2+ is replaced with Co2+, Cu2+, Ba2+, Mg2+, Mn2+, Ni2+, Sr2+ or Zn2+
Ca2+
-
optimum Ca2+ concentration at 2.0-4.0 mM
Ca2+
-
both pectate lyase I and II require 0.2 mM Ca2+ for maximal activity
Ca2+
-
optimal concentration: 0.2 mM
Ca2+
-
optimal concentration: 0.1 mM
Ca2+
-
the Ca2+ site consists primarily of beta-turns and beta-strands. The Ca2+ affinity for the enzyme is weak. Kd: 0.132 mM at pH 9.5, 1.09 mM at pH 11.2 and 5.84 mM at pH 4.5. Enzymatic activity at pH 4.5 is greatest at 30 mM Ca2+
Ca2+
-
the enzyme has a single high affinity calcium-binding site. A second Ca2+ binds between enzyme and substrate in the Michaelis complex
Ca2+
optimum Ca2+ concentration at 0.5 mM
Ca2+
optimum concentration at 0.6 mM
Ca2+
Erwinia aroidea
-
stimulates
Ca2+
-
optimum concentration at 1.0 mM, Ca2+ cannot be replaced by Ba2+, Be2+, Sr2+, Mg2+, and monovalent cations for Pel activity
Ca2+
-
optimum Ca2+ concentration at 0.6 mM
Ca2+
activates, active site binding structure, overview
Ca2+
enzyme activity is Ca2+-dependent
Ca2+
activates 208% at 0.2 mM
Ca2+
-
enzyme from Alpine strain A15 completely loses activity in absence of Ca2+
Ca2+
-
enzyme from Siberian strain AG25 completely loses activity in absence of Ca2+
Ca2+
-
required, can be replaced by Mn2+ or Mg2+. Optimal activity at 0.7 mM. Additive effect when any two metal ions (Mg2+, Ca2+, Mn2+) are present together
Ca2+
-
optimum Ca2+ concentration at 0.2 mM
Ca2+
activates optimally at 0-2.5 mM
Ca2+
-
enhances activity 5fold
Ca2+
required, 7.3fold activation at 0.5 mM, 4.4fold at 1 mM, Ca2+-binding residues are D151, D173, and D177 in PelN
Ca2+
residues D152, D174, and D178 form the Ca2+ ion binding sites
Ca2+
-
optimal concentration: 0.2 mM
Ca2+
-
0.5 mM, 7fold activation of pectate lyase I, 4fold activation of pectate lyase II
Ca2+
-
stabilizes, best activating metal ion, optimally at 2 mM
Ca2+
-
absolute requirement for Ca2+for pectin degradation, no other divalent cation (Mg2+, Mn2+, Ba2+, Cu2+, Zn2+ or Co2+) can substitute for Ca2+, pectate lyase activity is undetectable without Ca2+ and the maximum activity is at 0.75 mm CaCl2, while enzymatic activity decreases at higher concentrations of Ca2+
Ca2+
-
activates, optimal at 1 mM
Ca2+
-
optimum Ca2+ concentration at 0.5 mM
Ca2+
-
optimum concentration at 1.0 mM
Ca2+
-
optimum concentration at 0.5 mM
Ca2+
-
maximal activity at 0.2 mM Ca2+
Ca2+
-
optimum Ca2+ concentration at 0.2 mM
Ca2+
Ca2+-dependent activity
Ca2+
-
required, optimal concentration varies with levels of the substrate
Ca2+
-
cation required, Ca2+ is most effective
Ca2+
-
required, optimal at about 0.05 mM
Ca2+
-
maximal activity at 0.6 mM
Ca2+
absolute requirement, maximal activity of recombinantly expressed full-length enzyme at 0.05 mM, maximal activity of recombinantly expressed catalytic module CM9-1 at 0.02 mM, maximal activity of recombinantly expressed catalytic module CM9-2 at 0.1 mM
Ca2+
strong activation, optimal activity at 0.05 mM CaCl2
Ca2+
-
PelC is dependent on Ca2+ for activity and stability
Ca2+
requires Ca2+, optimal activity with 0.25 mM
Ca2+
required, activates 5.8fold at 0.5 mM
Ca2+
0.1 mM, 180% of initial activity. Presence of Ca2+ enhances thermal stability
Ca2+
-
up to 1 mM, stimulation
Ca2+
Ca2+-dependent activity
Ca2+
-
required, best at 0.05 mM
Co2+
-
1 mM, 180% of initial activity
Co2+
5 mM, 138% of initial activity
Cu2+
5 mM, 122% of initial activity
Cu2+
activates 193% at 0.2 mM
Cu2+
activates 19% at 0.2 mM
Cu2+
activates slightly at 0.5 mM
Fe2+
-
1 mM, 126% of initial activity
Fe2+
-
1 mM, stimulates activity up to 592%
Fe2+
activates 213% at 0.2 mM
Fe2+
activates 231% at 0.2 mM
Fe2+
completely inactivates activity after incubation for 15 min
Fe2+
-
required for activity, optimal at 0.1 to 0.3mM
K+
19% activation at 0.5 mM
K+
-
9% activation at 1 mM
K+
activates slightly at 0.5-1 mM
Mg2+
-
1 mM, 226% of initial activity
Mg2+
-
1 mM, stimulates activity up to 368%
Mg2+
5 mM, 133% of initial activity
Mg2+
-
slightly enhances enzyme activity
Mg2+
activates 190% at 0.2 mM
Mg2+
the enzyme is activated 40% in the presence of MgCl2
Mg2+
slightly increases activity
Mg2+
1 mM, 144% of initial activity
Mg2+
-
can substitute for Ca2+ in activation. Optimal activity at 0.7 mM. Additive effect when any two metal ions (Mg2+, Ca2+, Mn2+) are present together
Mg2+
25% activation at 0.5 mM
Mg2+
-
41% of the activation with Ca2+
Mg2+
-
26% of the activation with Ca2+
Mg2+
activates slightly at 0.5 mM
Mn2+
-
1 mM, 268% of initial activity
Mn2+
-
1 mM, activity is enhanced by 1221%
Mn2+
5 mM, 116% of initial activity
Mn2+
activates 136% at 0.2 mM
Mn2+
-
restores activity of the EGTA-inactivated enzyme
Mn2+
1 mM, 143% of initial activity
Mn2+
-
optimal concentration: 0.1 mM
Mn2+
-
11% of the activation with Ca2+
Mn2+
-
can substitute for Ca2+ in activation. Optimal activity at 0.7 mM. Additive effect when any two metal ions (Mg2+, Ca2+, Mn2+) are present together
Mn2+
-
1 mM, enhances activity 6fold
Mn2+
-
27% of the activity with Ca2+
Mn2+
-
29% activation at 1 mM, 7.5% activation at 5 mM
Na+
decreases activity
Na+
-
10% activation at 1 mM
Ni2+
5 mM, 120% of initial activity
Ni2+
activates 191% at 0.2 mM
Sr2+
-
restores activity of the EGTA-inactivated enzyme
Sr2+
-
21% of the activation with Ca2+
Zn2+
-
1 mM, 202% of initial activity
Zn2+
5 mM, 145% of initial activity
Zn2+
activates 132% at 0.2 mM
Zn2+
16% activation at 0.5 mM
Zn2+
activates slightly at 0.5-1 mM
additional information
-
enzyme does not require Ca2+
additional information
-
no requirement of Ca2+
additional information
Fe2+ and Cu2+ do not significantly affect the activity of Pel-66
additional information
no or poor effect on the recombinant enzyme from Pichia pastoris by Sr2+, K+, and Li+
additional information
-
no or poor effect on the recombinant enzyme from Pichia pastoris by Sr2+, K+, and Li+
additional information
-
no activation by Ca2+, Co2+, Cu2+, Mg2+, Mn2+, Ni2+, Zn2+, or Ba2+,
additional information
Fe2+ and Ni2+ do not significantly affect the activity of Pel-90
additional information
-
Fe2+ and Ni2+ do not significantly affect the activity of Pel-90
additional information
-
divalent cations are required for maximum activity