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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

Renatured

Renatured on EC 1.10.3.2 - laccase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
incubation of apo-CueO with excess CuSO4 (10 equiv) in Mops buffer (pH 7) in the presence of GSH (1 mM) at 4°C leads to incorporation of copper ions
purification and recovery of immobilized and extractable transgenic enzyme, treatment with copper for activation of apoenzyme and as purification step
-
reconstitution of Cu-depleted enzyme
the enzyme is denatured in the presence of a number of denaturing agents (EDTA, DTT and GdnHCl) and refolded back to functional state with copper. In the folding experiments under alkaline conditions, zinc can replace copper in restoring 100% of laccase activity
the isolated enzyme does not exhibit any enzymatic activity and lacks the blue colour typical of multicopper oxidase. Supplementation of purified CueO with CuSO4 activates the enzyme and renders it blue
unfolding of the purified laccase, chemical reagents like 1-100 mM EDTA, 50-200 mM DTT and 1-6 M guanidinium hydrochloride, 100% activity is regained with 1 mM copper at pH 8.0 or by 1 mM Zn2+ at pH 5.5