Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Methieux, G.; Zitoun, C.
    Mechanisms by which fatty-acyl-CoA esters inhibit or activate glucose-6-phosphasaes in intact and detergent-treated rat liver microsomes (1996), Eur. J. Biochem., 235, 799-803.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.9 fatty-acyl-CoA with chain-length equal to or higher than 16, at 0.001-0.002 mM, the inhibitory effect on the enzyme of untreated microsomes is either partially or totally cancelled, or even changes into an activation effect at higher concentrations, the inhibition is fully reversible in presence of bovine serum albumin. With medium chain-length, 10-14 carbons inhibit the enzyme of untreated microsomes in a dose-dependent manner in the range 0.001-0.02 mM, the higher the chain length, the stronger the inhibitory effect Rattus norvegicus
3.1.3.9 myristoyl-CoA uncompetitive inhibition of enzyme in untreated microsomes, non-competitive inhibition of enzyme from detergent-treated microsomes Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.9 microsome
-
Rattus norvegicus
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.9 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.9 liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.9 D-glucose 6-phosphate + H2O
-
Rattus norvegicus D-glucose + phosphate
-
?