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 (General Information
General Information 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
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
the enzyme belongs to the blue multicopper oxidase superfamily
malfunction
metabolism
the three copper sites play related but distinct roles in CueO oxidase activities. The internal Cu5 site is part of the essential electron transfer pathway connecting surface-exposed sites Cu6 and Cu7 to site T1. Both Cu6 and Cu7 are dominant substrate-docking-oxidation sites on the protein surface. The two surface-exposed sites Cu6 and Cu7 are the direct substrate-docking-oxidation sites for both oxidase functions and buried site Cu5 channels electrons from the oxidations to the Type 1 site of the multicopper oxidase machinery
physiological function
additional information
malfunction
changes in the C-terminus of MaL caused major defects in protein production in both expression hosts
malfunction
elimination of the N-terminal sequence decreases the specific activity 15fold, which is partially restored in the presence of 1 M NaCl, and alters the secondary and tertiary structures and the pH dependence of optimal stability
malfunction
-
elimination of the N-terminal sequence decreases the specific activity 15fold, which is partially restored in the presence of 1 M NaCl, and alters the secondary and tertiary structures and the pH dependence of optimal stability
-
physiological function
laccases are ligninolytic enzymes that play a role in the hostpathogen interaction in the first step of infection. Pleurotus eryngii is weakly pathogenic when colonizing the roots and stems of Eryngiumcampestre
physiological function
laccases are ligninolytic enzymes that play a role in the hostpathogen interaction in the first step of infection. Pleurotus ferulae is mostly pathogenic when colonizing the roots and stems of Ferula communis
physiological function
-
the enzyme inhibits proliferation of murine leukemia cell line L1210 and human heptoma cell line Hep-G2, and reduces the activity of HIV-1 reverse transcriptase, IC50 is 0.022 mM, but shows no mitogenic activity on mouse splenocytes, nor hemagglutinin/hemolytic activity towards rabbit erythrocytes
physiological function
-
laccase inhibits HIV-1 reverse transcriptase and proliferation of hepatoma Hep-G2 cells and breast cancer MCF-7 cells with an IC50 of 0.00065 mM, 0.0014 mM, and 0.0042 mM, respectively, indicating that it is also an antipathogenic protein
physiological function
-
supplying free radical form of monolignol units, such as q-coumaryl, sinapyl, and coniferyl alcohols for production of lignins
physiological function
-
survival of the fungal hyphomycete in the presence of the toxic compounds produced by host plants
physiological function
-
the enzyme is involcved in the development and morphogenesis of fungi
physiological function
-
the enzyme is involved in defense against the toxic compounds produced by host plantscuticle maturation
physiological function
-
the enzyme is involved in metabolism of solorinin and solorinic acid (responsible for the orange color of the thallus)
physiological function
-
the enzyme is involved in metabolism of solorinin and solorinic acid (responsible for the orange color of the thallus)
physiological function
-
the enzyme is involved in oxidation of cuticular catechols for cuticle hardening and pigmentation
physiological function
-
the enzyme is involved in solubilization and mineralization of lignin
physiological function
-
the enzyme is involved in the production of brownish spore pigment
physiological function
-
virulence of the yeast via the synthesis of a eumelanin biopolymer
physiological function
in order to act as a phenol oxidase, a T4 copper atom must be in place to mediate electron transfer between the buried T1 copper center and the organic substrates. The lability of this copper center restricts optimal phenol oxidase activity to the micro- to nanomolar concentration range for available Cuaq2+. This suggests that CueO cannot function as a phenol oxidase in vivo
physiological function
presence of CueO in the periplasm protects alkaline phosphatase from copper-induced damage
physiological function
when expressed in an Escherichia coli CueO knock-out strain, enzyme exhibits phenol oxidase activity in vivo and enhances the copper tolerance of the strain
physiological function
-
plant, bacterial, and insect laccases have a polymerizing role in nature, implicated in biosynthesis of lignin, melanin formation, and cuticle hardening, respectively. On the other hand, fungal laccases carry out both polymerizing (melanin synthesis and fruit body formation) as well as depolymerizing roles (lignin degradation)
physiological function
-
plant, bacterial, and insect laccases have a polymerizing role in nature, implicated in biosynthesis of lignin, melanin formation, and cuticle hardening, respectively. On the other hand, fungal laccases carry out both polymerizing (melanin synthesis and fruit body formation) as well as depolymerizing roles (lignin degradation)
physiological function
-
plant, bacterial, and insect laccases have a polymerizing role in nature, implicated in biosynthesis of lignin, melanin formation, and cuticle hardening, respectively. On the other hand, fungal laccases carry out both polymerizing (melanin synthesis and fruit body formation) as well as depolymerizing roles (lignin degradation)
physiological function
-
plant, bacterial, and insect laccases have a polymerizing role in nature, implicated in biosynthesis of lignin, melanin formation, and cuticle hardening, respectively. On the other hand, fungal laccases carry out both polymerizing (melanin synthesis and fruit body formation) as well as depolymerizing roles (lignin degradation)
physiological function
-
plant, bacterial, and insect laccases have a polymerizing role in nature, implicated in biosynthesis of lignin, melanin formation, and cuticle hardening, respectively. On the other hand, fungal laccases carry out both polymerizing (melanin synthesis and fruit body formation) as well as depolymerizing roles (lignin degradation)
physiological function
-
plant, bacterial, and insect laccases have a polymerizing role in nature, implicated in biosynthesis of lignin, melanin formation, and cuticle hardening, respectively. On the other hand, fungal laccases carry out both polymerizing (melanin synthesis and fruit body formation) as well as depolymerizing roles (lignin degradation)
additional information
-
the laccase does not exert any antiproliferative activity against Hep-G2 or MCF-7 tumor cell lines at a concentration of 0.06 mM, but shows significant activity toward human immunodeficiency virus-1 reverse transcriptase with an IC50 of 60 nM
additional information
-
the laccase from Melanocarpus albomyces is a low redox potential enzyme. Structure-function study, mass spectrometry, overview
additional information
the laccase from Rhus vernicifera is a low redox potential enzyme. Structure-function study, mass spectrometry, overview
additional information
the laccase from Trametes hirsuta is a high redox potential enzyme. Structure-function study, mass spectrometry, overview
additional information
-
the laccase from Trametes versicolor is a high redox potential enzyme. Structure-function study, mass spectrometry, overview
additional information
the last 18 amino acids in the C-terminal end of the Ery4 laccase play a critical role in enzyme activity, stability and kinetic and, in particular biochemical and structural data indicate that the K532 residue is fundamental for enzyme activation. Structure-function relationships of fungal laccases, overview
additional information
-
the last 18 amino acids in the C-terminal end of the Ery4 laccase play a critical role in enzyme activity, stability and kinetic and, in particular biochemical and structural data indicate that the K532 residue is fundamental for enzyme activation. Structure-function relationships of fungal laccases, overview
additional information
-
a total of 52 genes encoding laccases (SvLAC1 to SvLAC52) are found in the genome of Setaria viridis, and phylogenetic analyses show that these genes are heterogeneously distributed among the characteristic six subclades of the family and are under relaxed selective constraints. Five SvLAC genes (SvLAC9, SvLAC13, SvLAC15, SvLAC50, and SvLAC52) fulfill the criteria established to identify lignin-related candidates: (1) phylogenetic proximity to previously characterized lignin-related laccases from other species, (2) similar expression pattern to that observed for lignin biosynthetic genes in the Setaria viridis elongating internode, and (3) high expression in Setaria viridis tissues undergoing active lignification
additional information
-
the laccase from Trametes hirsuta is a high redox potential enzyme. Structure-function study, mass spectrometry, overview
-
