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Literature summary for 1.10.3.2 extracted from

  • Durao, P.; Chen, Z.; Fernandes, A.T.; Hildebrandt, P.; Murgida, D.H.; Todorovic, S.; Pereira, M.M.; Melo, E.P.; Martins, L.O.
    Copper incorporation into recombinant CotA laccase from Bacillus subtilis: characterization of fully copper loaded enzymes (2008), J. Biol. Inorg. Chem., 13, 183-193.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
 syringaldazine pH 7, holoCotA Bacillus subtilis
0.056
-
 K4Fe(CN)6 pH 3, holoCotA Bacillus subtilis
0.124
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) pH 3, holoCotA Bacillus subtilis
0.216
-
 2,6-dimethoxyphenol pH 7, holoCotA Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
copper copper content of recombinant CotA laccase from Bacillus subtilis produced by Escherichia coli cells is shown to be strongly dependent on the presence of copper and oxygen in the culture media. In copper-supplemented media, a switch from aerobic to microaerobic conditions leads to the synthesis of a recombinant holoenzyme, while the maintenance of aerobic conditions results in the synthesis of a copper-depleted population of proteins. Strikingly, cells grown under microaerobic conditions accumulate up to 80fold more copper than aerobically grown cells. In vitro copper incorporation into apoenzymes is monitored by optical and electron paramagnetic resonance spectroscopy. This analysis reveals that copper incorporation into CotA laccase is a sequential process, with the type 1 copper center being the first to be reconstituted, followed by the type 2 and the type 3 copper centers Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.52
-
 recombinant enzyme from Escherichia coli AH3517 cells grown under aerobic conditions Bacillus subtilis
228.2
-
 recombinant enzyme from Escherichia coli AH3517 cells grown under microaerobic conditions Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
-
 Bacillus subtilis ?
-
 ?
2,6-dimethoxyphenol + O2
-
 Bacillus subtilis ?
-
 ?
K4Fe(CN)6 + O2
-
 Bacillus subtilis ?
-
 ?
syringaldazine + O2
-
 Bacillus subtilis ?
-
 ?

Synonyms

Synonyms Comment Organism
CotA laccase
-
 Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
29
-
 2,6-dimethoxyphenol pH 7, holoCotA Bacillus subtilis
80
-
 syringaldazine pH 7, holoCotA Bacillus subtilis
322
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) pH 3, holoCotA Bacillus subtilis
529
-
 K4Fe(CN)6 pH 3, holoCotA Bacillus subtilis