Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

General Stability

General Stability on EC 1.10.3.2 - laccase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity and stability of laccase in conjugation with chitosan is reduced, overview
-
ammonium sulfate stabilizes
-
Ca-alginate, Cu-alginate, Ca-alginate-chitosan and sol–gel immobilized laccase show an operational stability of 36%, 51%, 66% and 82%, respectively after 6 cycles
-
co-cross-linking method is superior to the other methods of immobilization in terms of operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent
-
freezing/thawing causes inactivation
-
high stability of the surface display laccase biocatalyst (where the enzyme laccase is displayed on the surface of biological cells through synthetic biology) in reuse
-
immobilising the enzyme through the cross-linked enzyme aggregate method significantly improves its tolerance towards extreme pH as well as the presence of organic solvents
-
laccase is stable in the presence of some metal ions such as Cu2+, Co2+, Ca2+, Cd2+, Mg2+, Mn2+, Mo2+, Ni2+, Li+ and Al3+
-
no satnilization by EDTA and Cu2+
-
POXA3a dissociates in 3 M urea, while POXA3b is not dissociated even in 6 M urea
-
soluble enzyme loses 45% of its activity after 8 days at 4°C. Sol-gel matrix immobilized laccase is the most stable with a mere loss of 2% among the Ca-alginate-chitosan, Cu-alginate and Ca-alginate beads with a loss of 10%, 17% and 25%, respectively
-
the activity of CcLCC5I is stable after incubation for 16 h at 4°C in 0.2 M citrate-phosphate buffer at weakly alkaline conditions, the minimal effect on enzyme activity is at pH 8.6
the enzyme is stable in the presence of cationic and anionic detergents. In the presence of non-ionic detergents, the enzyme is stable at lower concentrations
-
the enzyme was stable in the presence of some metal ions such as Ca2+, Cu2+, Ni2+, Mg2+, Mn2+, Ba2+, Co2+, and Zn2+ at 1 mM
-
the purified native enzyme is stable in 4 M urea
unfolding of tertiary structure is a twostate process in the wild-type enzyme, displaying a midpoint at a guanidinium hydrochloride concentration of 4.6 M, unfolding for both mutant enzymes is clearly not a two-state process, overview
-