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Information on EC 1.10.3.2 - laccase and Organism(s) Melanocarpus albomyces and UniProt Accession Q70KY3
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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: Melanocarpus albomyces
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
-
-
-
-
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-ethylbenzo-6-thiazolinesulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
-
i.e. syringaldazine
-
-
?
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
Cu2+
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
additional information
additional information
-
Michaelis-Menten steady-state kinetics, overview
-
0.26
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 22°C, recombinant enzyme expressed in Saccharomyces cerevisiae
0.28
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant enzyme expressed in Trichoderma reesei
0.4
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant wild-type enzyme
0.9
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
0.011
2,6-dimethoxyphenol
pH 4.5, 25°C, recombinant wild-type enzyme
0.016
2,6-dimethoxyphenol
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
0.031
syringaldazine
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
0.037
syringaldazine
pH 4.5, 25°C, recombinant wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
109
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
6.57
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
28.1
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
pH 4.5, 25°C, recombinant wild-type enzyme
9.08
2,6-dimethoxyphenol
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
10.2
2,6-dimethoxyphenol
pH 4.5, 25°C, recombinant wild-type enzyme
21.05
syringaldazine
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae
40.17
syringaldazine
pH 4.5, 25°C, recombinant wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
380
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0079
NaN3
pH 4.5, 25°C, recombinant wild-type enzyme versus 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
0.029
NaN3
pH 4.5, 25°C, recombinant wild-type enzyme, versus 2,6-dimethoxyphenol
0.055
NaN3
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae, versus 2,6-dimethoxyphenol
0.085
NaN3
pH 4.5, 25°C, recombinant mutant L559A expressed in Saccharomyces cerevisiae versus 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24 - 36.6
recombinant enzyme expressed in Saccharomyces cerevisiae
850
-
substrate 2,2-azinobis(3-ethylbenzothiazoline-6-sulfonic acid), pH 4.5
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.55
recombinant MaL, expressed in Saccharomyces cerevisiae, has several pI forms, whereas the recombinant MaL, produced in Trichoderma reesei only had one pI form at pI 4.0
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
changes in the C-terminus of MaL caused major defects in protein production in both expression hosts
additional information
-
the laccase from Melanocarpus albomyces is a low 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_MELAO
623
0
68958
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
x * 70000, recombinant nonglycosylated enzyme expressed in Trichodrma reesei, SDS-PAGE, x * 100000, recombinant glycosylated enzyme expressed in Saccharomyces cerevisiae, SDS-PAGE
70000
x * 70000, recombinant nonglycosylated enzyme expressed in Trichodrma reesei, SDS-PAGE, x * 100000, recombinant glycosylated enzyme expressed in Saccharomyces cerevisiae, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 70000, recombinant nonglycosylated enzyme expressed in Trichodrma reesei, SDS-PAGE, x * 100000, recombinant glycosylated enzyme expressed in Saccharomyces cerevisiae, SDS-PAGE
additional information
additional information
in MaL, the four C-terminal amino acids of the mature protein penetrate into a tunnel leading towards the trinuclear site. The C-terminal carboxylate group forms a hydrogen bond with a side chain of His140, which also coordinates to the type 3 copper, three-dimensional structure of mutant L559A, overview
additional information
-
in MaL, the four C-terminal amino acids of the mature protein penetrate into a tunnel leading towards the trinuclear site. The C-terminal carboxylate group forms a hydrogen bond with a side chain of His140, which also coordinates to the type 3 copper, three-dimensional structure of mutant L559A, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
the C-terminus is post-translationally processed after Leu559, leading to removal of the last 14 aminoacids of the mature protein
glycoprotein
the recombinant MaL, expressed in Saccharomyces cerevisiae, is heavily overglycosylated, while the recombinant enzyme overexpressed in Trichoderma reesei is not
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, at 22 °C in hanging drops by combining 0.002 ml of 8 mg/ml protein in sodium acetate, pH 5.0, with 0.002 ml of reservoir solution, the reservoir solution contains 13% PMME 2000, 0.1 M ammonium sulfate, and 0.1 M sodium acetate at pH 4.5, microseeding, space group C2, X-ray diffraction structure determination and analysis at 2.0 A resolution
purified recombinant mutant L559A, by vapor diffusion method at 20°C, 10 mg/ml protein mixed with 15% PMME 2000, 0.2 M ammonium sulfate, and 0.1 M sodium acetate, pH 4.5, microseeding using 13% PMME 2000 and an equilibrium time of 4 h,usage of 25% glycerol as cryoprotectant, X-ray diffraction structure determination and analysis at 2. A resolution by molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L559A
the C-terminal mutation affects the trinuclear site geometry of the mutant enzyme, which also shows 3-4fold reduced activity compared to the wild-type enzyme
additional information
additional information
deletion of the last four amino acids dramatically affected the activity of the enzyme, as the deletion mutant delDSGL559 is practically inactive
additional information
-
deletion of the last four amino acids dramatically affected the activity of the enzyme, as the deletion mutant delDSGL559 is practically inactive
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8
the L559A mutant remains stable within this pH range after 330 h at 4°C, the enzyme looses 60% at pH 5.0, and 95% at pH 4.0 after 330 h. No activity remains at pH 3.0 and pH 2.0 after 330 h
697913
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
half-life of recombinant, expressed in Saccharomyces cerevisiae, wild-type enzyme is over 50 h, and of the L559A mutant is 24 h
50
half-life of recombinant, expressed in Saccharomyces cerevisiae, wild-type enzyme is 23 h, and of the L559A mutant is 6 h
60
half-life of recombinant, expressed in Saccharomyces cerevisiae, wild-type enzyme is 4.5 h, and of the L559A mutant is below 10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Trichoderma reesei and Saccharomyces cerevisiae by two different steps of anion exchange chromatography, hydrophobic interaction chromatography, and gel filtration
recombinant enzyme from a Trichoderma reeseicbh1 cbh1 disruption mutant strain
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Trichoderma reesei and Saccharomyces cerevisiae, expression of mutant L559A in Saccharomyces cerevisiae. The yeast is not able to process MaL correctly, and the additional 14 amino acids are present in the protein. Therefore, expression is performed with another construct, pMS175, where mature MaL cDNA, with a stop codon, is introduced after the C-terminal processing site. Changes in the C-terminus of MaL cause major defects in protein production in both expression hosts
enzyme expression in Trichoderma reesei under the strong cbh1 (cel7A) promoter in a strain in which the major cellulase gene cbh1 is disrupted
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
expression of non-fused enzyme and hydrophobin-enzyme fusion protein in Trichoderma reesei, intracellular accumulation and degradation of fusion protein, production of non-fused enzyme at up to 920 mg per l of fed-batch culture, purification from culture supernatant
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hakulinen, N.; Kiiskinen, L.L.; Kruus, K.; Saloheimo, M.; Paananen, A.; Koivula, A.; Rouvinen, J.
Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site
Nat. Struct. Biol.
9
601-605
2002
Melanocarpus albomyces (Q70KY3), Melanocarpus albomyces
Kiiskinen, L.L.; Viikari, L.; Kruus, K.
Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces
Appl. Microbiol. Biotechnol.
59
198-204
2002
Melanocarpus albomyces
Kiiskinen, L.L.; Kruus, K.; Bailey, M.; Ylosmaki, E.; Siika-Aho, M.; Saloheimo, M.
Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme
Microbiology
150
3065-3074
2004
Melanocarpus albomyces
Hakulinen, N.; Kruus, K.; Koivula, A.; Rouvinen, J.
A crystallographic and spectroscopic study on the effect of X-ray radiation on the crystal structure of Melanocarpus albomyces laccase
Biochem. Biophys. Res. Commun.
350
929-934
2006
Melanocarpus albomyces (Q70KY3), Melanocarpus albomyces
Andberg, M.; Hakulinen, N.; Auer, S.; Saloheimo, M.; Koivula, A.; Rouvinen, J.; Kruus, K.
Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure
FEBS J.
276
6285-6300
2009
Melanocarpus albomyces (Q70KY3), Melanocarpus albomyces
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)
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