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Literature summary for 1.3.3.5 extracted from

  • Kamitaka, Y.; Tsujimura, S.; Kataoka, K.; Sakurai, T.; Ikeda, T.; Kano, K.
    Effects of axial ligand mutation of the type I copper site in bilirubin oxidase on direct electron transfer-type bioelectrocatalytic reduction of dioxygen (2007), J. Electroanal. Chem., 601, 119-124.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Pichia pastoris Albifimbria verrucaria

Protein Variants

Protein Variants Comment Organism
M467Q the enzymatic activity of the mutant is very low toward bilirubin but it works as a good catalyst in direct electron transfer-type bioelectrocatalytic reduction of dioxygen into water, the kcat value is 3fold increased Albifimbria verrucaria

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0192
-
K4[Fe(CN)6] wild type recombinant enzyme, at pH 7.0 and 25°C Albifimbria verrucaria
5.966
-
K4[Fe(CN)6] mutant enzyme M467Q, at pH 7.0 and 25°C Albifimbria verrucaria

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ multi-copper oxidase Albifimbria verrucaria

Organism

Organism UniProt Comment Textmining
Albifimbria verrucaria
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Albifimbria verrucaria

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bilirubin + O2
-
Albifimbria verrucaria biliverdin + H2O
-
?
K4[Fe(CN)6] + O2
-
Albifimbria verrucaria K3[Fe(CN)6] + H2O
-
?

Synonyms

Synonyms Comment Organism
BOD
-
Albifimbria verrucaria

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
374
-
K4[Fe(CN)6] wild type recombinant enzyme, at pH 7.0 and 25°C Albifimbria verrucaria
1259
-
K4[Fe(CN)6] mutant enzyme M467Q, at pH 7.0 and 25°C Albifimbria verrucaria