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Literature summary for 1.11.1.7 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
Search for more literature for 1.11.1.7

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Aggregatibacter actinomycetemcomitans A2A1C5
-
-

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
ubiquinol-1 + H2O2
-
 Aggregatibacter actinomycetemcomitans ubiquinone-1 + H2O
-
 ?