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Literature summary for 1.11.1.6 extracted from

  • Moore, R.L.; Cook, C.O.; Williams, R.; Goodwin, D.C.
    Substitution of strictly conserved Y111 in catalase-peroxidases: Impact of remote interdomain contacts on active site structure and catalytic performance (2008), J. Inorg. Biochem., 102, 1819-1824.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Y111A substantial increase in hexa-xoordinate low-spin heme with the appearance of a transition between the wild-type primarily high-spin and the N-terminal pure low-spin domain alone. Decrease in activity is for catalase activity more substantially than for peroxidase activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5
-
H2O2 wild-type, pH 7.0, 23°C Escherichia coli
5.2
-
H2O2 mutant Y111A, pH 7.0, 23°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
bifunctional catalase-peroxidase KatG
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2
-
Escherichia coli O2 + H2O
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2140
-
H2O2 mutant Y111A, pH 7.0, 23°C Escherichia coli
11000
-
H2O2 wild-type, pH 7.0, 23°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme in wild-type, primarily high-spin. In mutant Y111A, substantial increase in hexa-coordinate low-spin heme Escherichia coli