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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

Reaction

4 benzenediol +

O2
= 4 benzosemiquinone + 2 H2O

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 Oxidoreductases
         1.10 Acting on diphenols and related substances as donors
             1.10.3 With oxygen as acceptor
                1.10.3.2 laccase

Crystallization

Crystallization on EC 1.10.3.2 - laccase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of mutants M502L and M502F are obtained from a crystallization solution containing 12% 2-propanol, 12% of PEG 4000, 0.1 M sodium citrate, pH 5.5, and a protein concentration of about 5 mg/mL, vapour diffusion method, 2 days at room temperature, X-ray diffraction structure determination and analysis at 2.05-2.3 A resolution
-
recombinant mutant enzymes I494A and L386A at 20°C and 10.8 mg/ml or 7.9 mg/ml, respectively, from a crystallization solution containing 0.1 M sodium citrate, 8-10% PEG MME 5000 and 14% propan-2-ol at pH 5.5, X-ray diffraction structure determination and analysis at 1.6-2.9 A resolution, cryoprotection of crystals of mutants I494A and L386A by 22% ethylene glycol or 25% glycerol, respectively
-
hanging-drop vapour-diffusion method, 2.3 A resolution
four CueO crystal structures are determined at different copper concentrations
-
structure of G304K mutant at 1.49 A resolution. The mutant shows dramatic conformational changes in methionine-rich helix and the relative regulatory loop. In the structure of Cu-soaked enzyme, the addition of Cu ions induces further conformational changes in the regulatory loop and methionine-rich helix as a result of the new Cu-binding sites on the enzyme's surface
structure of the region Pro357-His406 deletion mutant, to 1.81 A resolution
the acetate-bound form of the type II copper is found in the X-ray structure of CueO crystallized in acetate buffer in addition to the conventional OH(-)-bound form as the major resting form. When CueO is crystallized in citrate buffer, the OH(-)-bound form is present exclusively
sitting drop vapor diffusion method, crystal strcuture is solved at 1.5 A
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
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
crystallization of native and selenomethionyl enzyme is performed using the sitting-drop vapour-diffusion method, crystal structure is determined at a resolution of 2.0 A
hanging-drop vapour-diffusion technique. The enzyme crystallizes in a primitive tetragonal lattice, with unit-cell parameters a = b = 179.8, c = 175.3 A. The crystals belong to either space group P4(1)2(1)2 or P4(3)2(1)2. The self-rotation function shows the presence of a noncrystallographic threefold axis in the structure
-
hanging-drop vapor-diffusion method
hanging-drop vapour-diffusion method, X-ray quality crystals are generated and the structure is solved to a resolution of 2.4 A
two-domain-type by sitting-drop vapour-diffusion method, mixing of 0.001 ml of a protein solution, containing 8.5 mg/ml protein, with 0.001 ml of reservoir solution, containing 0.2 M potassium chloride, 0.05 M HEPES, pH 7.5, and 35% v/v pentaerythritol propoxylate, at 20°C, X-ray diffraction structure determination and analysis at 1.7 A resolution, single-wavelength anomalous diffraction technique using Cu atoms
-
complexed with 2,5-xylidine