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Literature summary for 7.1.1.9 extracted from

  • Gaviraghi, A.; Correa Soares, J.; Mignaco, J.; Fontes, C.; Oliveira, M.
    Mitochondrial glycerol phosphate oxidation is modulated by adenylates through allosteric regulation of cytochrome c oxidase activity in mosquito flight muscle (2019), Insect Biochem. Mol. Biol., 114, 103226 .
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0355
-
ferrocytochrome c 28°C, pH not specified in the publication Aedes aegypti
0.0407
-
ferrocytochrome c 28°C, presence of 3 mM ADP, pH not specified in the publication Aedes aegypti

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Aedes aegypti 5739
-

Organism

Organism UniProt Comment Textmining
Aedes aegypti
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle flight muscle Aedes aegypti
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 ferrocytochrome c + O2 + 4 H+/in
-
Aedes aegypti 4 ferricytochrome c + 2 H2O
-
?

General Information

General Information Comment Organism
physiological function mitochondrial glycerol 3-phosphate oxidation is controlled by adenylates through allosteric regulation of cytochrome c oxidase (COX) activity in flight muscle. ADP significantly activates respiratory rates linked to glycerol 3-phosphate oxidation, in a protonmotive force-independent manner. ADP activates respiration through a slightly cooperative mechanism. COX activity ias allosterically activated by ADP. ATP exerts powerful inhibitory effects on respiratory rates linked to glycerol 3-phosphate oxidation and on COX activity Aedes aegypti