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Information on EC 1.10.3.2 - laccase and Organism(s) Pleurotus ostreatus and UniProt Accession Q12739
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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: Pleurotus ostreatus
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, diphenol oxidase, poxa1b, 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
-
-
-
-
POXA1b
POXA3a
POXA3b
urishiol oxidase
-
-
-
-
urushiol oxidase
-
-
-
-
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
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
best substrate
-
-
?
additional information
?
-
-
no significant enzymic activity with guaiacol
-
-
?
additional information
?
-
-
no activity with tyrosine and hydroquinone, the enzyme in absence of a mediator oxidizes anthracene to anthraquinone to 95%
-
-
?
additional information
?
-
-
no activity with ferulic acid and veratryl alcohol
-
-
?
additional information
?
-
-
the isolated enzyme from Pleurotus ostreatus mycelium has both bilirubin oxidase and laccase activities
-
-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of a wide range of compounds, including poly-phenols and anilines. The one electron oxidation of the reducing substrate occurs concomitantly with the four-electron reduction of molecular oxygen to water
-
-
?
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
additional information
?
-
-
the enzyme catalyzes the oxidation of a wide range of compounds, including poly-phenols and anilines. The one electron oxidation of the reducing substrate occurs concomitantly with the four-electron reduction of molecular oxygen to water
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
construction of enzymesubstrate complexes and molecular dynamics simulations, complex of mutant D205R with 2,5-xylidine, molecular dynamics simulations, overview
-
0.07
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 3.0, 22°C, recombinant wild-type enzyme
0.11
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 3.0, 22°C, recombinant truncated mutant POXA1bDELTA16
0.11
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 3.0, 22°C, recombinant truncated mutant POXA1bDELTA4
0.32
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 3.0, 22°C, recombinant truncated mutant POXA1bD205R
0.0552
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6.0, 25°C
0.07
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA3a, pH 3.6, 25°C
0.074
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA3b, pH 3.6, 25°C
0.09
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA1w, pH 3.0, 25°C
0.12
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA2, pH 3.0, 25°C
0.28
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXC, pH 3.0, 25°C
0.37
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
isoform POXA1b, pH 3.0, 25°C
0.07
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
25°C, isozyme POXA3a
0.074
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
25°C, isozyme POXA3b
0.11
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.0, 25°C
0.43
2,6-dimethoxyphenol
pH 5.3, 22°C, recombinant truncated mutant POXA1bDELTA16
0.43
2,6-dimethoxyphenol
pH 5.3, 22°C, recombinant truncated mutant POXA1bDELTA4
0.57
2,6-dimethoxyphenol
pH 5.3, 22°C, recombinant wild-type enzyme
1.26
2,6-dimethoxyphenol
pH 5.3, 22°C, recombinant truncated mutant POXA1bD205R
0.03
syringaldazine
pH 6.0, 22°C, recombinant truncated mutant POXA1bDELTA16
0.03
syringaldazine
pH 6.0, 22°C, recombinant truncated mutant POXA1bDELTA4
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.7
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.0, 25°C
73300
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
25°C, isozyme POXA3a
158300
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
25°C, isozyme POXA3b
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0552
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
partially purified recombinant truncated mutant POXA1bDELTA4, substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
12
partially purified recombinant truncated mutant POXA1bDELTA16, substrate syringaldazine
129
partially purified recombinant truncated mutant POXA1bDELTA16, substrate 2,6-dimethoxyphenol
15
partially purified recombinant wild-type enzyme, substrate syringaldazine
155
partially purified recombinant wild-type enzyme, substrate 2,6-dimethoxyphenol
162
partially purified recombinant wild-type enzyme, substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
17
partially purified recombinant truncated mutant POXA1bDELTA4, substrate syringaldazine
189
partially purified recombinant truncated mutant POXA1bDELTA4, substrate 2,6-dimethoxyphenol
19.1
-
crude enzyme, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 3.0 and 50°C
261
-
purified enzyme, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 3.0 and 50°C
3
partially purified recombinant truncated mutant POXA1bD205R, substrate 2,6-dimethoxyphenol
33
additional information
33
partially purified recombinant truncated mutant POXA1bD205R, substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
33
partially purified recombinant truncated mutant POXA1bDELTA16, substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3
assay at, substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
3 - 3.6
-
using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate
3.6
-
POXA3a and POXA3b, substrate 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.3
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
laccase activity is positively correlated to the growth of the fungus. Four laccase isoforms are secreted by the fungus, and tentatively named LI1, LI2, LI3 and LI4. LI2, LI3 and LI4 are produced during the stationary phase (between 408 and 456 h approximately) while LI1 is produced during the lag, exponential and stationary phases of growth. Maximal laccase activity is observed at the beginning of the stationary phase
additional information
additional information
-
solid-phase culture, natural substrate are sunflower-seed shells
additional information
-
optimization of culture conditions for high yield of extracellular enzyme requiring Mg2+ and glucose, overview
additional information
-
cultivation of Pleurotus ostreatus on tomato pomace medium
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme is involcved in the development and morphogenesis of fungi
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). LAC2_PLEOS
533
0
56767
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43700
59000
67000
67000
-
x * 67000 + x * 16000-18000, SDS-PAGE and MALDI-TOF, both POXA3a and POXA3b
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 67000 + x * 16000-18000, SDS-PAGE and MALDI-TOF, both POXA3a and POXA3b
additional information
the POXA1b laccase possesses an unusual C-terminal extension of sixteen amino acids compared to other laccases
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
carbohydrate content about 10%, two N-glycosilation sites, both POXA3a and POXA3b
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
needle-shaped crystals of sPOXA3b (the small subunit of laccase) grew in a few days at 21 °C using the sitting-drop vapour-diffusion method to approximate dimensions of 0.1 * 0.1 * 0.3 mm. The crystals belong to the primitive tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 126.6, c = 53.9 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D205R
site-directed mutagenesis, the mutation in a highly conserved region perturbs the structural local environment in POXA1b, leading to a large rearrangement of the enzyme structure. The mutant shows highly reduced activity compared to the wild-type enzyme and is inactive with substrate syringaldazine
additional information
deletion of the C-terminal extension of 4 or 16 amino acids leads to truncated mutants which lose the high stability at pH 10, while they show an increased stability at pH 5.0, the thermostability is unaltered compared to the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
stability of recombinant wild-type and mutant enzymes, overview
697668
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
POXA3a, 50% residual activity after 6 h, POXA3b, 50% residual activity after 14h
40 - 60
-
isoform POXA1b shows a inactivation half-period of 3 h at 60°C, isoform POXA1w shows a inactivation half-period of 3.3 h at 60°C, isoform POXA2 shows a inactivation half-period of 0.2 h at 60°C, isoform POXA3a shows a inactivation half-period of 6 h at 40°C, isoform POXA3b shows a inactivation half-period of 14 h at 40°C, isoform POXC shows a inactivation half-period of 30 min at 40°C
60
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
POXA3a dissociates in 3 M urea, while POXA3b is not dissociated even in 6 M urea
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography, ConA-Sepharose column chromatography, and Toyopearl HW-55 column chromatography
-
method development for one-step affinity chromatographic purifcation, 46fold purification on 1,4-butanediol diglycidyl ether affinity resin, analysis of affinity chromatographic matrices containing either urea, acetamide, ethanolamine, or iminodiacetic acid, and best with 1,4-butanediol diglycidyl ether, as affinity ligands for enzyme purification from fermentation broth
-
native extracellular enzyme 3.67fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration to homogeneity
-
native extracellular enzyme by anion exchange chromatography, ammonium sulfate fractionation, and gel filtration
-
recombinant wild-type and mutant enzymes partially from Saccharomyces cerevisiae strain W303-1A
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli strain Top10, expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain W303-1A
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
industry
-
the laccase has a wide application in industrial processes, particularly in renewable bio-energy industry
environmental protection
-
LI1 shows activity over a broad range of pH and temperature, which may make it useful in the biodegradation of phenolic compounds present in wastewater from several industrial processes
environmental protection
decolorization of industrial dyes with different chemical structures and decolorization of industrial wastewaters
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sannia, G.; Giardina, P.; Luna, M.; Rossi, M.; Buonocore, V.
Laccase from Pleurotus ostreatus
Biotechnol. Lett.
8
797-800
1986
Pleurotus ostreatus
-
Garzillo, A.M.; Colao, M.C.; Buonocore, V.; Oliva, R.; Falcigno, L.; Saviano, M.; Santoro, A.M.; Zappala, R.; Bonomo, R.P.; Bianco, C.; Giardina, P.; Palmieri, G.; Sannia, G.
Structural and kinetic characterization of native laccases from Pleurotus ostreatus, Rigidoporus lignosus, and Trametes trogii
J. Protein Chem.
20
191-201
2001
Rigidoporus microporus, Pleurotus ostreatus, Coriolopsis trogii
Palmieri, G.; Cennamo, G.; Faraco, V.; Amoresano, A.; Sannia, G.; Giardina, P.
Atypical laccase isoenzymes from copper supplemented Pleurotus ostreatus cultures
Enzyme Microb. Technol.
33
220-230
2003
Pleurotus ostreatus
-
Baldrian, P.; Gabriel, J.
Copper and cadmium increase laccase activity in Pleurotus ostreatus
FEMS Microbiol. Lett.
206
69-74
2002
Pleurotus ostreatus
Pozdnyakova, N.N.; Turkovskaya, O.V.; Yudina, E.N.; Rodakiewicz-Nowak, Y.
Yellow laccase from the fungus Pleurotus ostreatus D1: purification and characterization
Appl. Biochem. Microbiol.
42
56-61
2006
Pleurotus ostreatus, Pleurotus ostreatus D1
-
Giardina, P.; Autore, F.; Faraco, V.; Festa, G.; Palmieri, G.; Piscitelli, A.; Sannia, G.
Structural characterization of heterodimeric laccases from Pleurotus ostreatus
Appl. Microbiol. Biotechnol.
75
1293-1300
2007
Pleurotus ostreatus (A0AQZ5), Pleurotus ostreatus (A0AQZ6), Pleurotus ostreatus
Tlecuitl-Beristain, S.; Sanchez, C.; Loera, O.; Robson, G.D.; Diaz-Godinez, G.
Laccases of Pleurotus ostreatus observed at different phases of its growth in submerged fermentation: production of a novel laccase isoform
Mycol. Res.
112
1080-1084
2008
Pleurotus ostreatus
Liu, L.; Lin, Z.; Zheng, T.; Lin, L.; Zheng, C.; Lin, Z.; Wang, S.; Wang, Z.
Fermentation optimization and characterization of the laccase from Pleurotus ostreatus strain 10969
Enzyme Microb. Technol.
44
426-433
2009
Pleurotus ostreatus, Pleurotus ostreatus 10969
-
Autore, F.; Del Vecchio, C.; Fraternali, F.; Giardina, P.; Sannia, G.; Faraco, V.
Molecular determinants of peculiar properties of a Pleurotus ostreatus laccase: analysis by site-directed mutagenesis
Enzyme Microb. Technol.
45
507-513
2009
Pleurotus ostreatus (O60199)
-
Moussa, T.
Molecular characterization of the phenol oxidase (pox2) gene from the ligninolytic fungus Pleurotus ostreatus
FEMS Microbiol. Lett.
298
131-142
2009
Pleurotus ostreatus (Q12739), Pleurotus ostreatus
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
Pakhadnia, Y.G.; Malinouski, N.I.; Lapko, A.G.
Purification and characteristics of an enzyme with both bilirubin oxidase and laccase activities from mycelium of the basidiomycete Pleurotus ostreatus
Biochemistry (Moscow)
74
1027-1034
2009
Pleurotus ostreatus, Pleurotus ostreatus 43 BIM F-306D
Freixo, M.d.o..R.; Karmali, A.; Arteiro, J.M.
Production, purification and characterization of laccase from Pleurotus ostreatus grown on tomato pomace
World J. Microbiol. Biotechnol.
28
245-254
2012
Pleurotus ostreatus
Ferraroni, M.; Scozzafava, A.; Ullah, S.; Tron, T.; Piscitelli, A.; Sannia, G.
Crystallization and preliminary X-ray crystallographic analysis of the small subunit of the heterodimeric laccase POXA3b from Pleurotus ostreatus
Acta Crystallogr. Sect. F
70
76-79
2014
Pleurotus ostreatus (A0AQZ6), Pleurotus ostreatus
Forootanfar, H.; Faramarzi, M.A.
Insights into laccase producing organisms, fermentation states, purification strategies, and biotechnological applications
Biotechnol. Prog.
31
1443-1463
2016
Bacillus amyloliquefaciens, Bacillus licheniformis, Bombyx mori, Botrytis cinerea, Thermochaetoides thermophila, Cryptococcus neoformans, Lentinula edodes, Pleurotus ostreatus, Populus x canadensis, Pseudomonas syringae, Toxicodendron vernicifluum, Streptomyces griseus, Streptomyces cyaneus, Solorina crocea, Peltigera aphthosa, Nephotettix cincticeps, Thermothelomyces thermophilus, Toxicodendron succedaneum, Bacillus spp., Riptortus pedestris, Nysius plebeius, Acer pseudoplatanus (Q38757)
Stanzione, I.; Pezzella, C.; Giardina, P.; Sannia, G.; Piscitelli, A.
Beyond natural laccases extension of their potential applications by protein engineering
Appl. Microbiol. Biotechnol.
104
915-924
2020
Bacillus licheniformis, Bacillus pumilus, Trametes versicolor, Lentinula edodes, Lentinula edodes (C5NN27), Rheinheimera sp., Thermothelomyces thermophilus, Pleurotus ostreatus (O60199)
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