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Literature summary extracted from

  • Abe, T.; Kawarai, T.; Takahashi, Y.; Konishi, K.
    Enzymatic kinetics of the quinol peroxidase of an aggressive periodontopathic bacterium (2017), J. Biochem., 161, 513-520 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.1.7 H2O2 inactivation by H2O2 is expressed by pseudofirst order kinetics and is an irreversible process Aggregatibacter actinomycetemcomitans
1.11.1.7 ubiquinone-1 product inhibition, mixed-type Aggregatibacter actinomycetemcomitans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.7 0.039
-
 H2O2 pH 7.5, temperature not specified in the publication Aggregatibacter actinomycetemcomitans
1.11.1.7 0.111
-
 ubiquinol-1 pH 7.5, temperature not specified in the publication Aggregatibacter actinomycetemcomitans

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.7 Aggregatibacter actinomycetemcomitans A2A1C5
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.11.1.7 2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O Ping Pong Bi Bi mechanism´ Aggregatibacter actinomycetemcomitans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.7 additional information in the reaction sequence, the first substrate (quinol) combines with the enzyme to form a substituted enzyme intermediate, with the concomitant release of the first product. The second substrate, H2O2, then interacts with the substituted enzyme intermediate to form the second product, thereby regenerating the native enzyme Aggregatibacter actinomycetemcomitans ?
-
 ?
1.11.1.7 ubiquinol-1 + H2O2
-
 Aggregatibacter actinomycetemcomitans ubiquinone-1 + H2O
-
 ?