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Literature summary extracted from

  • Salony, J.L.; Garg, N.; Baranwal, R.; Chhabra, M.; Mishra, S.; Chaudhuri, T.K.; Bisaria, V.S.
    Laccase of Cyathus bulleri: structural, catalytic characterization and expression in Escherichia coli (2008), Biochim. Biophys. Acta, 1784, 259-268.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.10.3.2 DNA and amino acid sequence determination and analysis, expression in Escherichia coli Cyathus bulleri
1.10.3.2 expression in Escherichia coli Cyathus bulleri

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.10.3.2 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide 200 mM, 80% inhibition Cyathus bulleri
1.10.3.2 DTT 1 mM, complete inhibition Cyathus bulleri
1.10.3.2 EDTA 1 mM, 67% inhibition Cyathus bulleri
1.10.3.2 kojic acid 5 mM, complete inhibition Cyathus bulleri
1.10.3.2 L-cysteine 0.1 mM, complete inhibition Cyathus bulleri
1.10.3.2 p-coumaric acid 5 mM, 60% inhibition Cyathus bulleri
1.10.3.2 Sodium azide 0.05 M, complete inhibition Cyathus bulleri

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.2 copper the enzyme is denatured in the presence of a number of denaturing agents 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 indicating the non-essential role of copper in this laccase Cyathus bulleri
1.10.3.2 Cu2+ zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase Cyathus bulleri
1.10.3.2 Zn2+ zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase Cyathus bulleri

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.2 Cyathus bulleri
-
-
-
1.10.3.2 Cyathus bulleri A8W7J6
-
-
1.10.3.2 Cyathus bulleri 195062
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.10.3.2
-
Cyathus bulleri
1.10.3.2 recombinant enzyme 82fold from Escherichia coli Cyathus bulleri

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.10.3.2 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 Cyathus bulleri
1.10.3.2 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 Cyathus bulleri

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.10.3.2 4000
-
purified recombinant enzyme Cyathus bulleri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.2 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
-
Cyathus bulleri ?
-
?
1.10.3.2 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
-
Cyathus bulleri 195062 ?
-
?
1.10.3.2 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonate) + O2
-
Cyathus bulleri ?
-
?
1.10.3.2 2-methylphenol + O2 i.e. guaiacol Cyathus bulleri ?
-
?
1.10.3.2 2-methylphenol + O2 i.e. guaiacol Cyathus bulleri 195062 ?
-
?
1.10.3.2 guaiacol + O2
-
Cyathus bulleri ? + H2O
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.2 4
-
-
Cyathus bulleri

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.10.3.2 2 6
-
Cyathus bulleri

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.10.3.2 additional information
-
additional information inhibition kinetics Cyathus bulleri