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(NH4)2SO4
-
4fold activation
Ag3+
-
2.5 mM, activates to 115.94% of control
AgNO3
-
1 mM, 3% residual activity
CuCl2
-
1 mM, increases activity by 28.5%
H2O2
-
0.5 mM, 63% residual activity
HgCl2
-
1 mM, 1% residual activity
imidazole
-
about 2fold activation
K2SO4
-
3.2fold activation
KCl
activity is optimal at 200 mM salt, with 1.5fold greater activity in KCl than in NaCl, and the enzyme displays reduced activity after the removal of salt by dialysis
Manganese
-
1 gatom per mol
MgCl2
0.5 mM, 1.08fold activation
MnCl2
-
1 mM, increases activity by 11.7%
MnSO4
-
1 mM, 1.2fold activation
Na2SO4
-
3.5fold activation
Pb(NO3)2
-
1 mM, 24% residual activity
Sn2+
-
10 mM, 6.1fold activation
ZnSO4
-
1 mM, 59% residual activity
Al3+
-
1.25 mM, 1.2fold activation
Al3+
-
1 mM, 1.1fold activation
Al3+
-
2.5 mM, activates to 109.42% of control
Al3+
significantly enhances activity
Ba2+
-
1.25 mM, 1.2fold activation
Ba2+
-
1 mM, 1.15fold activation
Ba2+
-
10 mM, 1.6fold activation
Ba2+
-
about 15% loss of maximal activity at 10 mM, about 20% loss of activity at 50 mM
Ca2+
-
1.25 mM, 1.1fold activation
Ca2+
-
25 mM, 70% inhibition
Ca2+
-
activates laccase in a concentration-dependent manner (0.1-10 mM)
Ca2+
slightly stimulatory
Ca2+
-
1 mM, 1.24fold activation
Ca2+
-
10 mM, 1.2fold activation
Ca2+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
Ca2+
-
about 15% loss of maximal activity at 10 mM, about 25% loss of activity at 50 mM
Ca2+
-
1 mM, 1.3fold activation
Ca2+
-
1 mM, 1.14fold activation
Ca2+
-
1 mM, 1.6fold activation
Ca2+
-
10 mM, weak activation
Ca2+
10 mM, 5% inhibition
Ca2+
-
5 mM, 18% increase in activity
Cd2+
-
1.25 mM, 1.2fold activation
Cd2+
-
activates laccase in a concentration-dependent manner (0.1-10 mM)
Cd2+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
Cd2+
-
5 mM, 1.9fold activation
Co2+
-
25 mM, 61% inhibition
Co2+
-
5.0 mM, increased activity to 150%
Co2+
-
activates laccase in aconcentration-dependent manner up to 1 mM
Co2+
-
104.7% activity at 10 mM
Co2+
-
1 mM, activity is enhanced to 141%
Co2+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
Co2+
-
1 mM, 1.28fold activation
Co2+
10 mM, 48% inhibition
copper
-
4 gatom per mol
copper
-
1.8 gatom per mol
copper
-
multicopper oxidase
copper
-
multicopper enzyme
copper
-
multicopper enzyme
copper
copper-containing enzyme
copper
-
multicopper enzyme
copper
-
multicopper enzyme
copper
multicopper enzyme
copper
multicopper enzyme
copper
-
multicopper enzyme
copper
-
multicoopper oxidase
copper
-
copper content of recombinant CotA laccase from Bacillus subtilis produced by Escherichia coli cells is shown to be strongly dependent on the presence of copper and oxygen in the culture media. In copper-supplemented media, a switch from aerobic to microaerobic conditions leads to the synthesis of a recombinant holoenzyme, while the maintenance of aerobic conditions results in the synthesis of a copper-depleted population of proteins. Strikingly, cells grown under microaerobic conditions accumulate up to 80fold more copper than aerobically grown cells. In vitro copper incorporation into apoenzymes is monitored by optical and electron paramagnetic resonance spectroscopy. This analysis reveals that copper incorporation into CotA laccase is a sequential process, with the type 1 copper center being the first to be reconstituted, followed by the type 2 and the type 3 copper centers
copper
multicopper enzyme
copper
-
multicopper enzyme
copper
multicopper enzyme
copper
-
4 atoms per protein molecule, a type I CuII, a type II CuII and a type III binuclear CuII
copper
copper-containing enzyme
copper
-
3-4 gatom Cu per mol
copper
-
multicopper enzyme
copper
the enzyme is denatured in the presence of a number of denaturing agents and refolded back to functional state with copper. In the folding experiments under alkaline conditions, zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase
copper
-
10 mM increase activity by 17%, 0.1 mM increase activity by 100%
copper
-
low copper occupancy in apo-CueO and slow copper reconstitution process in CueO with exogenous copper are demonstrated. These observations well explain the copper dependence of CueO oxidase activity
copper
contains six copper atoms per polypeptide chain and displays optical and electron paramagnetic resonance spectra consistent with the presence of type 1, type 2, and type 3 copper centers. The addition of copper leads to immediate and reversible changes in the optical and electron paramagnetic resonance spectra of the protein, as well as decreased thermal stability of the enzyme and stimulates both the phenoloxidase and ferroxidase activities
copper
four copper atoms per molecule, spectroscopic properties are typical of blue copper oxidase. Presence of copper is essential for CueO-dependent oxidation of 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) and p-phenylenediamine
copper
mechanism of copper incorporation in CueO is sequential, with type 1 copper being the first to be reconstituted, followed by type 2 and type 3 sites. The copper content of the purified protein is routinely 0.5-0.6 Cu atoms/protein molecule
copper
the affinity of site T4 for CuII shows a KD of 0.0055 microM
copper
-
multi-copper oxidase
copper
multicopper oxidase. The apoenzyme is inactive. Incubation with CuSO4 allows a 43fold increase of the specific activity yielding a metallo-enzyme
copper
Halalkalibacterium halodurans
-
multicopper enzyme
copper
the enzyme is modified posttranslationally, including removal of 31 amino acid residues from its N terminus, addition of glycan residues (glycosylation), and apparent coordination of four copper atoms into three types of copper-binding sites
copper
-
multicopper enzyme
copper
multicopper oxidase
copper
-
multicopper enzyme
copper
-
1.8 gatom per mol
copper
-
50% of copper is paramagnetic, type 1 Cu2+ and type 2 Cu2+
copper
-
one gatom per mol
copper
Phlebia fascicularia
-
contains 4 copper atoms per protein molecule
copper
a blue copper-containing oxidoreductase
copper
-
3-4 gatom Cu per mol
copper
-
3.3 mol copper per mol of protein, type I copper
copper
-
Type I and type II copper center
copper
-
16 gatom per mol, laccase I, 4 gatom per mol, laccases II, III, study of copper centers
copper
-
18 gatom per mol
copper
Polyporus versicolor
-
preparation of type II-depleted enzyme
copper
Polyporus versicolor
-
temperature dependence of reduction potential
copper
-
3-4 gatom Cu per mol
copper
-
3-4 gatom Cu per mol
copper
-
copper-containing enzyme
copper
-
multicopper enzyme
copper
-
multicopper enzyme
copper
multicopper enzyme
copper
multicopper enzyme
copper
-
four ions per subunit
copper
-
multicopper enzyme
copper
multicopper enzyme
copper
multicopper enzyme
copper
-
multicopper enzyme
copper
-
multicopper enzyme
copper
-
multicopper enzyme
copper
multicopper enzyme
copper
-
copper multi-copper oxidase
copper
Thermochaetoides thermophila
-
-
copper
multicopper oxidase
copper
-
preparation of Cu-depleted enzyme
copper
-
temperature dependence of reduction potential
copper
-
chemical and spectral studies of binuclear copper site
copper
-
ENDOR (i.e. electron nuclear double resonance) studies
copper
-
X-ray absorption edge study of type I, type II and binuclear type III copper center
copper
-
X-ray absorption spectra, possible copper-copper interaction
copper
-
3-4 gatom Cu per mol
copper
two paramagnetic copper centers per protein molecule
copper
-
multicopper enzyme
copper
-
multicopper enzyme
copper
-
multi-copper containing oxidase
copper
-
four ions per molecule
copper
-
electron paramagnetic resonance studies
copper
-
trinuclear and mononuclear copper center
copper
-
multicopper enzyme
copper
-
multicopper enzyme
copper
copper-containing enzyme
copper
-
multicopper enzyme
Cr2+
-
1.25 mM, 1.2fold activation
Cr2+
10 mM, 5% inhibition
Cu2+
-
1.25 mM, 1.3fold activation
Cu2+
activity is low in the absence of Cu2+, so 1 mM Cu2+ is added into the assay buffer
Cu2+
-
1 mM, enhances activity to 137% of control
Cu2+
-
the CotA-type laccase is associated with 4 Cu2+ ions, content determined by inductive coupled plasma optical emission spectroscopy
Cu2+
-
purified laccase contains 2.7 mol/mol of copper
Cu2+
-
required for LacZ1 enzyme activity
Cu2+
-
multicopper enzyme, the T1 copper centre clearly plays a key role
Cu2+
-
a copper enzyme, the wild-type enzyme contains 3.7 mol Cu2+ per mol of enzyme, mutants I494A and L386A contain 4.0 mol copper per mol of enzyme. Binding structures in wild-type and mutant enzymes I494A and L386A, analysis of crystal structures and simulation, overview
Cu2+
-
5.0 mM, increased activity to 126%
Cu2+
-
multi-copper enzyme
Cu2+
-
activates laccase in aconcentration-dependent manner up to 1 mM
Cu2+
-
required, stimulates up to 0.2 mM, contains type I Cu+ and type III Cu+
Cu2+
-
copper-containing enzyme
Cu2+
-
contains a type III binuclear Cu2+ center and a type I Cu2+ center
Cu2+
the gene sequence encodes copper-binding domains I and II
Cu2+
zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase
Cu2+
-
activates 40% at 1 mM
Cu2+
-
153.4% activity at 10 mM
Cu2+
-
1 mM, 1.38fold activation
Cu2+
-
10 mM, 8.0fold activation
Cu2+
multicopper enzyme, copper is not fully incorporated into the type-I Cu center of Escherichia coli purified enzyme. Typical metal content of laccases includes a type-1 Cu site (T1), a type-2 Cu site (T2), and a dinuclear type-3 Cu site (T3), with T2 and T3 arranged in a trinuclear cluster. The T1 Cu site contains the blue copper, whose tight coordination to a cysteine is responsible for an intense SCys -> Cu(II) charge transfer transition at around 600 nm, giving the typical blue color to the enzyme. T2 shows a characteristic electron paramagnetic resonance (EPR) spectrum, clearly distinct from that of T1, whereas the T3 copper dimer is anti-ferromagnetically coupled and EPR-silent
Cu2+
-
activates, 148% at 2 mM
Cu2+
-
multicopper enzyme
Cu2+
-
multicopper enzyme
Cu2+
-
copper-containing enzyme, type 1 and type 3 copper
Cu2+
-
presence of type-1 site and type-3 binuclear copper in the bright blue colored purified enzyme
Cu2+
-
1 mM, 1.3fold activation
Cu2+
-
the enzyme is strongly stimulated by Cu2+
Cu2+
a multicopper oxidase
Cu2+
a multi-copper laccase
Cu2+
four coppers involved in dioxygen binding, a copper T1 forming a mononuclear site and a cluster of three coppers T2, T3, and T3' forming a trinuclear site, binding and coordination structure analysis, overview
Cu2+
a copper-containing metalloenzyme
Cu2+
-
the enzyme contains 1 mol of Fe and Zn and 2 mol of Cu per mol of protein
Cu2+
Opuntia vulgaris
-
activates 40% at 1 mM
Cu2+
His64 and His399 coordinate with T2 Cu and the other six histidines at positions 66, 109, 111, 401, 451 and 453 coordinate with the T3 Cu pair, a hydrogen bond between Glu460 and Ser113 causes a longer Cu1-N-His458 bond at T1 site, Cu2+ binding structure, overview
Cu2+
-
activates, increases the enzyme activity best at 0.25 mM in the culture medium
Cu2+
-
copper-containing enzyme, type I copper atoms
Cu2+
laccases contain four copper ions distributed into three sites that, according to their spectroscopic properties, are classified as type 1 Cu, or blue copper centre, type 2 or normal copper centres, and type 3 or coupled binuclear copper centres, overview
Cu2+
-
the enzyme is a multi-copper enzyme
Cu2+
-
the enzyme contains four copper ions per enzyme molecule
Cu2+
138% activity at 10 mM
Cu2+
-
copper-containing enzyme
Cu2+
-
activates 1.8fold at 2.0 mM
Cu2+
-
copper-containing enzyme
Cu2+
-
stimulates the wild-type enzyme by 6% at 10 mM, 14.5% at 100 mM, required for activity
Cu2+
-
1 mM, 1.36fold activation
Cu2+
Sporothrix carnis
-
10 mM, 1.3fold activation
Cu2+
-
a copper enzyme with type I Cu2+
Cu2+
-
laccase activity is increased 2.6-fold by the addition of 10 mM copper sulfate
Cu2+
-
a copper-containing enzyme
Cu2+
copper-containing enzyme. Contains 4 atoms per molecule of the enzyme
Cu2+
-
copper-containing enzyme
Cu2+
-
a multicopper protein
Cu2+
the enzyme requires copper ions for activity. The dependence of the activity on Cu2+ concentration is sigmoidal with the midpoint at 0.00304 mM. Other metal ions (Mg2+, Mn2+, Ca2+, Ni2+, or Zn2+ each at 1 mM) fail to support the activity. The methionine-rich region from Met271 to Met283 may be involved in copper binding
Cu2+
-
copper-containing enzyme, trinuclear Cu cluster upon interaction with o-fluorophenol, overview
Cu2+
-
type 1 copper ion, Redox potential: 790 mV, 4 ions per enzyme molecule
Cu2+
-
the structure of laccase active sites including all copper centers of types T1, T2, and T3 changes during the phase transition, overview
Cu2+
-
2.5 mM, activates to 237.68% of control
Cu2+
-
a multicopper enzyme, redox potential determination of the different copper ions of the different isozymes, overview
Cu2+
-
activates slightly at 1 mM
Cu2+
-
a multicopper oxidase
Cu2+
the enzyme contains 4 copper molecules per enzyme molecule, structure overview
Cu2+
significantly enhances activity
Cu2+
a multicopper enzyme
Cu2+
coordination of Cu1 with His458
Cu2+
-
multi-copper-containing enzyme
Cu2+
-
opper-containing enzyme
Cu2+
-
blue multi-copper oxidase
Cu2+
-
5 mM, 85% increase in activity
CuSO4
-
1 mM, 1.1fold activation
CuSO4
oxidation of dimethoxyphenol requires the addition of CuSO4
Fe2+
-
5 mM, 3-11% inhibition (depending on purification method)
Fe2+
-
activates laccase in aconcentration-dependent manner up to 1 mM
Fe2+
-
10 mM, 2.6fold activation
Fe2+
-
activates, 204% at 2 mM
Fe2+
-
1 mM, 1.9fold activation
Fe2+
-
the enzyme contains 1 mol of Fe and Zn and 2 mol of Cu per mol of protein
Fe2+
-
1 mM, 1.57fold activation
Fe2+
10 mM, 96% inhibition
Fe3+
-
1.25 mM, 1.3,fold activation
Fe3+
-
2.5 mM, activates to 114.49% of control
Hg2+
-
130.7% relative activity in the presence of 20 mM Hg2+
Hg2+
10 mM, 94% inhibition
K+
-
1.25 mM, 1.2fold activation
K+
-
5 mM, 6-12% inhibition (depending on purification method)
K+
-
1.25 mM, 1.08fold activation
K+
-
1 mM, 1.3fold activation
K+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
K+
-
1 mM, 1.2fold activation
K+
-
2.5 mM, activates to 117.39% of control
Li+
-
activates
Li+
10 mM, 47% inhibition
Mg2+
-
1.25 mM, 1.2fold activation
Mg2+
-
25 mM, 35% inhibition
Mg2+
slightly stimulatory
Mg2+
-
1 mM, 1.16fold activation
Mg2+
-
10 mM, 1.5fold activation
Mg2+
-
activates, 137% at 2 mM
Mg2+
-
about 10% loss of maximal activity at 10 mM, about 20% loss of activity at 50 mM
Mg2+
-
1 mM, 1.44fold activation
Mg2+
-
10 mM, weak activation
Mg2+
-
50 mM, slight stimulation (105%)
Mg2+
-
5 mM, 15% increase in activity
Mn2+
-
1 mM, enhances activity to 103% of control
Mn2+
-
25 mM, 55% inhibition
Mn2+
-
activates laccase in a concentration-dependent manner (0.1-10 mM)
Mn2+
slightly stimulatory
Mn2+
-
1.25-10 mM, slightly enhance the laccase activity of 3.810.5%
Mn2+
-
activates 40% at 1 mM
Mn2+
-
1 mM, 1.3fold activation
Mn2+
-
10 mM, 2.7fold activation
Mn2+
-
1 mM, activity is enhanced to 127%
Mn2+
-
inhibits the enzyme activity at 100 mM but increases it at 12.5-50 mM
Mn2+
-
about 10% loss of maximal activity at 10 mM, about 20% loss of activity at 50 mM
Mn2+
-
10 mM, 4.3fold activation
Mn2+
Opuntia vulgaris
-
activates 40% at 1 mM
Mn2+
Sporothrix carnis
-
10 mM, 2.5fold activation
Mn2+
10 mM, 32% inhibition
Mn2+
-
2.5 mM, activates to 105.03% of control
Mn2+
-
5 mM, 8% increase in activity
Na+
-
1.25 mM, 1.2fold activation
Na+
-
up to 400 mM NaCl stimulates laccase activity. At 600 to 800 mM NaCl, the laccase retains all of its original activity and at higher concentrations, the activity decreases
Na+
-
exhibits activation of laccase up to 1 mM beyond which it exhibited inhibition of laccase activity
Na+
-
1 mM, 1.4fold activation
NaCl
-
halotolerant with maximum activity at 100 mM NaCl
NaCl
activity is optimal at 200 mM salt, with 1.5fold greater activity in KCl than in NaCl, and the enzyme displays reduced activity after the removal of salt by dialysis. Also active at relatively high concentrations of salt, with 65% activity at 1 M NaCl
NaCl
native wild-type MmPPOA and recombinant wild-type MmPPOA-695-His (both the crude extract and the pure enzyme preparations) retain substantial part of the enzymatic activity in the presence of 1 M NaCl, while recombinant mutant His-tagged MmPPOA-637 activity shows a 90% decrease at 100 mM NaCl and about 20% increase at 1 M NaCl
Ni2+
-
25 mM, 75% inhibition
Ni2+
-
1 mM, 12% increase in activity
Ni2+
-
1 mM, 1.3fold activation
Ni2+
-
1 mM, 1.14fold activation
Ni2+
10 mM, 31% inhibition
Pb2+
-
1.25 mM, 1.2fold activation
Pb2+
10 mM, 72% inhibition
Zn2+
-
1.25 mM, 1.2fold activation
Zn2+
-
1 mM, enhances activity to 120% of control
Zn2+
-
5 mM, 80-87% inhibition (depending on purification method)
Zn2+
slightly stimulatory
Zn2+
zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase
Zn2+
-
10 mM, 6.4fold activation
Zn2+
-
activates, 146% at 2 mM
Zn2+
-
the enzyme contains 1 mol of Fe and Zn and 2 mol of Cu per mol of protein
Zn2+
-
significantly enhances activity at concentrations under 50 mM
Zn2+
10 mM, 7% inhibition
Zn2+
-
2.5 mM, activates to 102.89% of control
additional information
-
no activation or inhibition by 1 mM of MgCl2, CaCl2, MnCl2, ZnSO4, or CuSO4
additional information
except for copper ions, most metal ions inhibit the laccase activity at a high concentration of about 10 mM, EDTA has no inhibitory effect on the laccase activity
additional information
-
except for copper ions, most metal ions inhibit the laccase activity at a high concentration of about 10 mM, EDTA has no inhibitory effect on the laccase activity
additional information
metal ions such as Ca2+, Mg2+, Co2+, Zn2+, Mn2+ and Cu2+ have slight or even no effect on the activities of laccase isoenzyme Lac4
additional information
metal ions such as Ca2+, Mg2+, Co2+, Zn2+, Mn2+ and Cu2+ have slight or even no effect on the activities of laccase isoenzyme Lac4
additional information
-
metal ions such as Ca2+, Mg2+, Co2+, Zn2+, Mn2+ and Cu2+ have slight or even no effect on the activities of laccase isoenzyme Lac4
additional information
metal ions such as Ca2+, Mg2+, Co2+, Zn2+, Mn2+ and Cu2+ have slight or even no effect on the activities of laccase isoenzymes Lac3 and Lac4
additional information
metal ions such as Ca2+, Mg2+, Co2+, Zn2+, Mn2+ and Cu2+ have slight or even no effect on the activities of laccase isoenzymes Lac3 and Lac4
additional information
-
metal ions such as Ca2+, Mg2+, Co2+, Zn2+, Mn2+ and Cu2+ have slight or even no effect on the activities of laccase isoenzymes Lac3 and Lac4
additional information
no effect by EDTA
additional information
-
no effect by EDTA
additional information
-
the enzyme activity is not affected by Ca2+ at 2 mM, and by NaCl up to 1.2 M
additional information
FJ560721
laccase activity remains stable for 24 h against all the ions tested, i.e. Cu2+, Co2+, Pb2+, Ca2+, Cd2+, Mg2+, Mn2+, Fe2+, Ni2+, F-, Zn2+, and Li+, at 10-100 mM
additional information
-
the enzyme activity is not affected by 7 mM Mn2+ and 1 mM H2O2, and by 1 mM of Ag+, Ba2+, Ca2+, Mg2+, Zn2+, Co2+, Ni2+ or Cu2+ or by sulfhydryl or chelating reagents
additional information
-
no or poor effect on enzyme activity by K+, Ca2+, Cu2+, Mg2+, Mn2+, Zn2+, and Ba2+ at 10 mM
additional information
-
the enzyme is not affected by Cu2+, Mn2+, or EDTA
additional information
-
the laccase is highly metal-tolerant. No or poor effects by Mn2+, Na+, Zn2+, Mg2+, Ca2+, K+, Fe2+, and Fe3+