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Literature summary for 1.10.3.2 extracted from

  • Melo, E.P.; Fernandes, A.T.; Durao, P.; Martins, L.O.
    Insight into stability of CotA laccase from the spore coat of Bacillus subtilis (2007), Biochem. Soc. Trans., 35, 1579-1582.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
M502F mutations leads to an increase in the redox potential by approx. 100 mV, decrease in the catalytic efficiency, decrease in thermodynamic stability Bacillus subtilis
M502L mutations leads to an increase in the redox potential by approx. 100 mV, decrease in the catalytic efficiency, decrease in thermodynamic stability Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.008
-
syringaldazine mutant enzyme M502F Bacillus subtilis
0.009
-
syringaldazine mutant enzyme M502L Bacillus subtilis
0.01
-
syringaldazine wild-type enzyme Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
spore coat Bacillus subtilis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
syringaldazine + H2O
-
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
0.01
-
syringaldazine mutant enzyme M502F Bacillus subtilis
7.4
-
syringaldazine mutant enzyme M502L Bacillus subtilis
18.4
-
syringaldazine wild-type enzyme Bacillus subtilis