1.10.3.2: laccase
This is an abbreviated version!
For detailed information about laccase, go to the full flat file.
Word Map on EC 1.10.3.2
-
1.10.3.2
-
trametes
-
decolor
-
versicolor
-
abts
-
white-rot
-
manganese
-
basidiomycete
-
pleurotus
-
oxidases
-
wastewater
-
textile
-
effluent
-
ostreatus
-
bioremediation
-
electrode
-
lignocellulosic
-
recalcitrant
-
pulp
-
guaiacol
-
straw
-
wood
-
tyrosinase
-
mushroom
-
solid-state
-
submerged
-
cellulase
-
xylanase
-
brilliant
-
phanerochaete
-
chemoradiation
-
chrysosporium
-
malachite
-
trinuclear
-
veratryl
-
kraft
-
chemoradiotherapy
-
copper-containing
-
reusability
-
monophenols
-
indigo
-
edodes
-
humic
-
bagasse
-
brachytherapy
-
bioelectrocatalytic
-
copper-binding
-
azoreductase
-
monolignols
-
industry
-
para-aortic
-
food industry
-
degradation
-
biofuel production
-
energy production
-
medicine
-
environmental protection
-
biotechnology
-
analysis
-
cmcase
-
synthesis
- 1.10.3.2
- trametes
-
decolor
- versicolor
- abts
-
white-rot
- manganese
-
basidiomycete
- pleurotus
- oxidases
-
wastewater
-
textile
-
effluent
- ostreatus
-
bioremediation
-
electrode
-
lignocellulosic
-
recalcitrant
- pulp
- guaiacol
- straw
- wood
- tyrosinase
- mushroom
-
solid-state
-
submerged
- cellulase
- xylanase
-
brilliant
- phanerochaete
-
chemoradiation
- chrysosporium
- malachite
-
trinuclear
-
veratryl
-
kraft
-
chemoradiotherapy
-
copper-containing
-
reusability
- monophenols
- indigo
- edodes
-
humic
- bagasse
-
brachytherapy
-
bioelectrocatalytic
-
copper-binding
- azoreductase
- monolignols
- industry
-
para-aortic
- food industry
- degradation
- biofuel production
- energy production
- medicine
- environmental protection
- biotechnology
- analysis
- cmcase
- synthesis
Reaction
4 benzenediol
+
Synonyms
ATM, benzenediol oxygen oxidoreductase, benzenediol-oxygen oxidoreductase, benzenediol: oxygen oxidoreductase, benzenediol:O2 oxidoreductase, Benzenediol:oxygen oxidoreductase, blue laccase, blue multicopper oxidase, CcLCC6, CotA, CotA laccase, CotA-laccase, CotA-type laccase, CueO, DA2_0547, DcLac1, DcLac2, Diphenol oxidase, EpoA, Ery4, Ery4 laccase, FpLcc1, FpLcc2, GMET_RS10855, Hvo_B0205, LAC, Lac I, Lac II, Lac-3.5, Lac-4.8, LAC1, Lac2, Lac2a, LAC3, Lac4, LacA, Lacc, laccase, laccase 1, laccase 3, laccase A, Laccase allele OR, Laccase allele TS, laccase CueO, laccase POXA3b, laccase-2, laccase2, LacCh, lacTT, LacTv, LacZ1, Lcc, lcc1, Lcc2, Lcc3, Lcc4, Lcc9, LccA, lccdelta, lccgamma, Ligninolytic phenoloxidase, MAL, McoP, MmPPO laccase, MmPPOA, More, MSK laccase, multicopper oxidase, p-benzenediol:dioxygen oxidoreductase, p-diphenol dioxygen oxidoreductase, p-diphenol oxidase, p-diphenol: dioxygen oxidoreductase, p-diphenol:dioxygenoxidoreductase, p-diphenol:O2 oxidoreductase, p-diphenol:oxygen oxidoreductase, p-diphenol:oxygen-oxidoreductase, PCL, phenol oxidase, PM1 laccase, polyphenol oxidase A, POXA1b, POXA1w, POXA2, POXA3 laccase, POXA3a, POXA3b, POXC, PpoA, PsLac1, PsLac2, rlac1338, SLAC, SN4LAC, spore coat A protein, spore coat protein A, SRL1, SvLAC13, SvLAC15, SvLAC50, SvLAC52, SvLAC9, TaLac1, ThL, TTC1370, TthLAC, two-domain laccase, urishiol oxidase, urushiol oxidase, Wlac, YacK, yellow laccase
ECTree
1.10.3.2 laccaseAdvanced search results
results (
results (Organic Solvent Stability
Organic Solvent Stability on EC 1.10.3.2 - laccase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
ORGANIC SOLVENT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-propanol
Acetone
acetonitril
acetonitrile
diethylene triamine
-
amongst 42 solvents tested, significant deactivation is observed only in the presence of diethylene triamine (less than 50% of activity retains after 6 h incubation), which is probably due to the stripping-off of the crucial bound-water monolayer from the enzyme molecule essential for its activity
dimethyl formamide
dimethyl sulfoxide
dimethylformamide
DMSO
Ethanol
Methanol
propanol
additional information
-
1% (v/v) Triton X-100 and 8 M urea have little or no influence on the strength of cuticle laccase activity
1-propanol
9% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
1-propanol
-
9% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
-
Acetone
-
the laccase retains about 60% of its activity in the presence of 5% (v/v) acetone
Acetone
-
the laccase retains about 60% of its activity in the presence of 5% (v/v) acetone
-
Acetone
rLac1 retains less than 20% activity in 50% v/v acetone after a 3 h incubation at 25°C
Acetone
-
rLac1 retains less than 20% activity in 50% v/v acetone after a 3 h incubation at 25°C
-
Acetone
Sporothrix carnis
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 27% loss of activity
Acetone
Sporothrix carnis CPF-05
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 27% loss of activity
-
acetonitril
rLac1 retains less than 20% activity in 50% v/v acetonitril after a 3 h incubation at 25°C
acetonitrile
-
presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
acetonitrile
-
presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
-
acetonitrile
30% (v/v), 70% loss of activity, recombinant enzyme
acetonitrile
-
30% (v/v), 70% loss of activity, recombinant enzyme
-
acetonitrile
-
the laccase retains about 75% of its activity in the presence of 5% (v/v) acetonitrile
acetonitrile
-
the laccase retains about 75% of its activity in the presence of 5% (v/v) acetonitrile
-
acetonitrile
Sporothrix carnis
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 39% loss of activity
acetonitrile
Sporothrix carnis CPF-05
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 39% loss of activity
-
dimethyl formamide
-
presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
dimethyl formamide
-
presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
-
dimethyl sulfoxide
10% v/v, 10°C, 1 h, 72% of activity remains
dimethyl sulfoxide
-
presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
dimethyl sulfoxide
-
presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
-
dimethyl sulfoxide
30% (v/v), 65% loss of activity, recombinant enzyme
dimethyl sulfoxide
-
30% (v/v), 65% loss of activity, recombinant enzyme
-
dimethyl sulfoxide
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity
dimethyl sulfoxide
-
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity
-
dimethyl sulfoxide
Sporothrix carnis
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 46% loss of activity
dimethylformamide
-
10% (v/v), 15 min, 58.8% activity compared to control
dimethylformamide
-
10% (v/v), 15 min, 58.8% activity compared to control
-
dimethylformamide
rLac1 retains more than 80% activity in 50% v/v dimethylformamide after a 3 h incubation at 25°C
dimethylformamide
-
rLac1 retains more than 80% activity in 50% v/v dimethylformamide after a 3 h incubation at 25°C
-
dimethylformamide
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity
dimethylformamide
-
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity
-
dimethylformamide
Sporothrix carnis
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 36% loss of activity
dimethylformamide
Sporothrix carnis CPF-05
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 36% loss of activity
-
DMSO
-
the laccase retains about 70% of its activity in the presence of 5% (v/v) DMSO
DMSO
-
the laccase retains about 70% of its activity in the presence of 5% (v/v) DMSO
-
DMSO
rLac1 retains more than 80% activity in 50% v/v DMSO after a 3 h incubation at 25°C
DMSO
-
rLac1 retains more than 80% activity in 50% v/v DMSO after a 3 h incubation at 25°C
-
Ethanol
25% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
Ethanol
30% (v/v), 65% loss of activity, recombinant enzyme
Ethanol
-
25% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
-
Ethanol
-
the laccase retains about 75% of its activity in the presence of 5% (v/v) ethanol
Ethanol
-
the laccase retains about 75% of its activity in the presence of 5% (v/v) ethanol
-
Ethanol
rLac1 retains more than 80% activity in 50% v/v ethanol after a 3 h incubation at 25°C
Ethanol
-
rLac1 retains more than 80% activity in 50% v/v ethanol after a 3 h incubation at 25°C
-
Ethanol
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity
Ethanol
-
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity
-
Ethanol
Sporothrix carnis
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 34% loss of activity
Ethanol
Sporothrix carnis CPF-05
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 34% loss of activity
-
Ethanol
-
10% (v/v), the enzyme retains more than 92.55% activity. At 50% (v/v), the enzyme loses about 85% activity after 1 h
Ethanol
Trametes polyzona WRF03
-
10% (v/v), the enzyme retains more than 92.55% activity. At 50% (v/v), the enzyme loses about 85% activity after 1 h
-
Methanol
-
presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
Methanol
-
presence of 10% organic solvent reduces melting temperature from 79°C to to 45-52°C but activity remains practically unimpaired
-
Methanol
18% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
Methanol
30% (v/v), 50% loss of activity, recombinant enzyme
Methanol
-
18% (v/v), 50% of activity of wild-type enzyme remains. The stability of laccase in organic solvents is improved by introducing nonpolar (E188: A, I, L, and V) and positively charged (E188: K and R) residues in this region by site-directed mutagenesis. All variants show higher C50 values when compared to the wild type. Nonpolar amino acid substitutions are found to be the most efficient mutants for their remarkable increase in C50 value and a decrease in thermoinactivation rate in the presence of solvent. Replacing a negative residue with hydrophobic residues on the surface of a protein can enhance thermoresistance as well as solvent stability. The stability of the resulting enzymes is dependent on the length of the alkyl chain
-
Methanol
-
the laccase retains more than 75-80% of its activity in the presence of 5% (v/v) methanol
Methanol
-
the laccase retains more than 75-80% of its activity in the presence of 5% (v/v) methanol
-
Methanol
rLac1 retains more than 80% activity in 50% v/v methanol after a 3 h incubation at 25°C
Methanol
-
rLac1 retains more than 80% activity in 50% v/v methanol after a 3 h incubation at 25°C
-
Methanol
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity
Methanol
-
25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity
-
Methanol
Sporothrix carnis
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 29% loss of activity
Methanol
Sporothrix carnis CPF-05
-
50% (v/v), preincubation at 30°C for 30 min before addition of substrate, 29% loss of activity
-
