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Literature summary for 1.10.3.2 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)

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

Inhibitors

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
Cu2+ zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase Cyathus bulleri
Zn2+ zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase Cyathus bulleri

Organism

Organism UniProt Comment Textmining
Cyathus bulleri
-
-
-
Cyathus bulleri A8W7J6
-
-
Cyathus bulleri 195062
-
-
-

Purification (Commentary)

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

Renatured (Commentary)

Renatured (Comment) Organism
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
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]

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

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
-
Cyathus bulleri

pH Range

pH Minimum pH Maximum Comment Organism
2 6
-
Cyathus bulleri

Ki Value [mM]

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