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Literature summary for 1.1.5.3 extracted from

  • Cottingham, I.R.; Ragan, C.I.
    Purification and properties of mitochondrial L-3-glycerophosphate-ubiquinone oxidoreductase (1978), Biochem. Soc. Trans., 6, 1307-1310.
    View publication on PubMed
Search for more literature for 1.1.5.3

Inhibitors

Inhibitors Comment Organism Structure
Chloroquine inhibits reaction with coenzyme Q1, no inhibition of the reaction with 2,6-dichloroindophenol Sus scrofa
m-Chlorohydroxamate
-
 Sus scrofa
Salicylhydroxamate
-
 Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Sus scrofa 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Iron contains 1 nmol non-heme iron per mg of protein Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sn-glycerol 3-phosphate + 2,6-dichlorophenolindophenol
-
 Sus scrofa glycerone phosphate + reduced 2,6-dichlorophenylindophenol
-
 ?
sn-glycerol 3-phosphate + coenzyme Q0
-
 Sus scrofa glycerone phosphate + reduced coenzyme Q0
-
 ?
sn-glycerol 3-phosphate + coenzyme Q1
-
 Sus scrofa glycerone phosphate + reduced coenzyme Q1
-
 ?
sn-glycerol 3-phosphate + coenzyme Q2
-
 Sus scrofa glycerone phosphate + reduced coenzyme Q2
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD contains up to 1 nmol of FAD/mg of protein Sus scrofa
FMN contains 0.1 nmol of FMN /mg of protein Sus scrofa