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Information on EC 1.10.3.2 - laccase and Organism(s) Trametes hirsuta and UniProt Accession Q02497
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1.10.3.2 laccaseIUBMB Comments
A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
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Word Map
- 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
The taxonomic range for the selected organisms is: Trametes hirsuta
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
laccase, lacc, phenol oxidase, laccase a, cota-laccase, lac i, poxa1b, diphenol oxidase, laccase2, cota laccase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Benzenediol:oxygen oxidoreductase
-
-
-
-
Diphenol oxidase
-
-
-
-
Laccase allele OR
-
-
-
-
Laccase allele TS
-
-
-
-
Ligninolytic phenoloxidase
-
-
-
-
p-diphenol oxidase
-
-
-
-
urishiol oxidase
-
-
-
-
urushiol oxidase
-
-
-
-
additional information
-
the enzyme belongs to the multicopper oxidase family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
benzenediol:oxygen oxidoreductase
A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
CAS REGISTRY NUMBER
COMMENTARY
80498-15-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,4-dioxane + O2
?
the oxidation reaction is accelerated by 25, 22, 6 and 19% in presence of 1 mM syringaldehyde, vanillin, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) and guaiacol mediators respectively
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
i.e. syringaldazine
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
high activity
-
-
?
tyrosine + O2
?
the enzyme catalyzes oxidative cross-linking of tyrosine and potato patatin and lysozyme-derived peptides
-
-
?
additional information
?
-
-
overview substrates, kinetics and stoichiometry
-
-
?
additional information
?
-
-
substrate specificities of a laccase chemically modified by attachment of PEG on soluble and cellulose-bound dye substrates, overview
-
-
?
additional information
?
-
-
polymerization of gliadins by laccase is observed only when a high enzyme dosage and prolonged incubation are used
-
-
?
additional information
?
-
-
no activity with veratryl alcohol, phenol, and L-tyrosine, substrate specificity, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
-
complete inhibition at over 10 mM with substrate 3,6-dimethoxyphenol and at over 20 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
NaF
-
complete inhibition at over 10 mM with substrates 3,6-dimethoxyphenol and 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
NaN3
-
complete inhibition at over 80 mM with substrate 3,6-dimethoxyphenol and at over 40 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CuSO4
-
activates 113% at over 40 mM with substrate 3,6-dimethoxyphenol, and 46% at over 10 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
EDTA
-
activates 10% at over 80 mM with substrate 3,6-dimethoxyphenol, and 50% at over 80 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
MnSO4
-
activates 49% at over 80 mM with substrate 3,6-dimethoxyphenol, and 28% at over 80 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
oxalic acid
-
activates 42% at 2 mM with substrate 3,6-dimethoxyphenol, and 303% at 20 mM with substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, temperature not specified in the publication
0.041
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C
0.00134
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 50°C, free enzyme
0.005
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 50°C, enzyme conjugated with 1.1 kDa PEG
0.00632
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 50°C, enzyme conjugated with 2 kDa PEG
0.00704
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 50°C, enzyme conjugated with 5 kDa PEG
additional information
additional information
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
-
study on kinetics, stoichiometries
-
additional information
additional information
-
analysis of enzyme dynamics and catalytic, spectral properties. Analysis of the structural state of the purified native laccase in solution at the phase transition before freezing, at freezing, and subsequent thawing of enzyme solution, processes in the active site on environmental temperature changes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
198.29
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, temperature not specified in the publication
196
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9914.5
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, temperature not specified in the publication
4780
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH 5.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
pH 3.0: about 75% of maximal activity, pH 8.0: about 60% of maximal activity, substrate: 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
20°C: about 80% of maximal activity, 50°C: about 60% of maximal activity, substrate: 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 from Trametes hirsuta is a high redox potential enzyme. Structure-function study, mass spectrometry, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LAC1_TRAHI
520
0
55688
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
the structure of laccase active sites including all copper centers of types T1, T2, and T3 changes during the phase transition, overview
monomer
-
laccase exists in solution as a mixture of monomeric and aggregated particles in the percent ratio 85:15, the ratio does not change on phase transitions, small-angle X-ray scattering, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
12% carbohydrate content, sugar chain are composed of mannose and N-acetyl-glycosamine
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme adsorption to cellulose fibers from cotton and denim, attachment of PEG of 1.1-5.0 kDa to the purified enzyme, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50
-
purified free enzyme half-life: 140 min, purified enzyme conjugated with 1.1 kDa PEG half-life: 70 min, purified enzyme conjugated with 2 kDa PEG half-life: 150 min, purified enzyme conjugated with 5.0 kDa PEG half-life: 210 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from culture filtrate by anion exchange and hydrophobic interaction chromatography
native enzyme 180fold by cold precipitation, ultrafiltration ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native extracellular enzyme by a three-stage chromatographic purification to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, primary structure of the gene, sequence comparisons
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
advantageous for laccases in industrial application as it acts as broad pH range acting enzyme
food industry
-
both laccase and tyrosinase increase the dough strength and improved the bread-making quality of white wheat flour breads, especially when used in combination with xylanase
industry
-
laccases can be considered as one of the most important biocatalyst which can be exploited for divergent industrial applications viz. paper pulp bleaching, fiber modification, dye decolorization, bioremediation as well as organic synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Smirnov, S.A.; Koroleva, O.V.; Gavrilova, V.P.; Belova, A.B.; Klyachko, N.L.
Laccases from Basidiomycetes: Physicochemical characteristics and substrate specificity towards methoxyphenolic compounds
Biochemistry (Moscow)
66
774-779
2001
Coriolisimus fulvocinerea, Trametes hirsuta, Trametes maxima, Trametes ochracea
Pegasova, T.V.; Zwart, P.; Koroleva, O.V.; Stepanova, E.V.; Rebrikov, D.V.; Lamzin, V.S.
Crystallization and preliminary X-ray analysis of a four-copper laccase from Coriolus hirsutus
Acta Crystallogr. Sect. D
59
1459-1461
2003
Trametes hirsuta (Q8TFL8), Trametes hirsuta
Rebrikov, D.N.; Stepanova, E.V.; Koroleva, O.V.; Budarina, Z.I.; Zakharova, M.V.; Yurkova, T.V.; Solonin, A.S.; Belova, O.V.; Pozhidaeva, Z.A.; Leontevsky, A.A.
Laccase of the lignolytic fungus Trametes hirsuta: purification and characterization of the enzyme, and cloning and primary structure of the gene
Appl. Biochem. Microbiol.
42
564-572
2006
Trametes hirsuta, Trametes hirsuta 72
-
Schroeder, M.; Heumann, S.; Silva, C.J.; Cavaco-Paulo, A.; Guebitz, G.M.
Specificities of a chemically modified laccase from Trametes hirsuta on soluble and cellulose-bound substrates
Biotechnol. Lett.
28
741-747
2006
Trametes hirsuta
Selinheimo, E.; Autio, K.; Kruus, K.; Buchert, J.
Elucidating the mechanism of laccase and tyrosinase in wheat bread making
J. Agric. Food Chem.
55
6357-6365
2007
Trametes hirsuta
Stepanova, E.V.; Fedorova, T.V.; Sorokina, O.N.; Volkov, V.V.; Koroleva, O.V.; Dembo, A.T.
Effect of solvent phase transitions on enzymatic activity and structure of laccase from Coriolus hirsutus
Biochemistry (Moscow)
74
385-392
2009
Trametes hirsuta, Trametes hirsuta 72
Haibo, Z.; Yinglong, Z.; Feng, H.; Peiji, G.; Jiachuan, C.
Purification and characterization of a thermostable laccase with unique oxidative characteristics from Trametes hirsuta
Biotechnol. Lett.
31
837-843
2009
Trametes hirsuta, Trametes hirsuta Ig-9 / CGMCC 2422
Erden, E.; Cigdem Ucar, M.; Gezer, T.; Pazarlioglu, N.
Screening for ligninolytic enzymes from autochthonous fungi and applications for decolorization of Remazole Marine Blue
Braz. J. Microbiol.
40
346-353
2009
Agaricus sp., Trametes hirsuta, Trametes versicolor, Pleurotus ostreatus, Cyclocybe aegerita, Inocybe lacera, Inocybe longicystis, Lactarius deliciosus, Lepista nuda, Lepiota sp. 1, Lepiota sp. 2, Leptonia lazunila, Lyophyllum subglobisporium, Ramaria stricta, Russula rosacea, Russula sp., Agrocybe sp. 1, Agrocybe sp. 2, Clitocybe sp., Coprinopsis atramentaria, Parasola plicatilis, Cortinarius sp. 1, Cortinarius sp. 2, Lepista nuda ECN 100605, Pleurotus ostreatus ECN 100607, Cortinarius sp. 2 ECN 100602, Lyophyllum subglobisporium ECN 100606, Trametes versicolor ECN 100609, Ramaria stricta ECN 100608
Frasconi, M.; Favero, G.; Boer, H.; Koivula, A.; Mazzei, F.
Kinetic and biochemical properties of high and low redox potential laccases from fungal and plant origin
Biochim. Biophys. Acta
1804
899-908
2010
Trametes versicolor, Melanocarpus albomyces, Trametes hirsuta (Q02497), Toxicodendron vernicifluum (Q8H979), Trametes hirsuta VTT D-95443 (Q02497)
Sharma, A.; Jain, K.K.; Jain, A.; Kidwai, M.; Kuhad, R.C.
Bifunctional in vivo role of laccase exploited in multiple biotechnological applications
Appl. Microbiol. Biotechnol.
102
10327-10343
2018
Trametes hirsuta, Trametes versicolor, Trametes cinnabarina, Trametes villosa, Ustilago maydis, Crinipellis sp.
Navada, K.K.; Kulal, A.
Kinetic characterization of purified laccase from Trametes hirsuta a study on laccase catalyzed biotransformation of 1,4-dioxane
Biotechnol. Lett.
43
613-626
2021
Trametes hirsuta (Q02497), Trametes hirsuta
Li, M.; Liu, L.; Kermasha, S.; Karboune, S.
Laccase-catalyzed oxidative cross-linking of tyrosine and potato patatin- and lysozyme-derived peptides Molecular and kinetic study
Enzyme Microb. Technol.
143
109694
2021
Trametes hirsuta (B2L9C1), Trametes hirsuta, Trametes versicolor (Q12718), Trametes versicolor
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