monensin and glutaconic-acid

monensin has been researched along with glutaconic-acid* in 1 studies

Other Studies

1 other study(ies) available for monensin and glutaconic-acid

Article	Year
A biotin-dependent sodium pump: glutaconyl-CoA decarboxylase from Acidaminococcus fermentans. FEBS letters, 1982, Nov-01, Volume: 148, Issue:1 The decarboxylation of glutaconyl-CoA to crotonyl-CoA in the anaerobic bacterium Acidaminococcus fermentans is catalysed by a membrane-bound, biotin-dependent enzyme which requires Na+ for activity. Inverted vesicles from A. fermentans accumulated Na+ only if glutaconyl-CoA was decarboxylated. The Na+ uptake was inhibited by avidin but not by the avidin biotin complex. Detergents and ionophores such as monensin also prevented the Na+ transport. The results indicate that the enzyme is able to convert the free energy of decarboxylation (delta Go' approximately equal to -30 kJ/mol) into a Na+ gradient. Topics: Avidin; Biotin; Carboxy-Lyases; Glutarates; Gram-Negative Anaerobic Bacteria; Ion Channels; Monensin; Octoxynol; Polyethylene Glycols; Sodium	1982

Article

Year

A biotin-dependent sodium pump: glutaconyl-CoA decarboxylase from Acidaminococcus fermentans.

FEBS letters, 1982, Nov-01, Volume: 148, Issue:1

The decarboxylation of glutaconyl-CoA to crotonyl-CoA in the anaerobic bacterium Acidaminococcus fermentans is catalysed by a membrane-bound, biotin-dependent enzyme which requires Na+ for activity. Inverted vesicles from A. fermentans accumulated Na+ only if glutaconyl-CoA was decarboxylated. The Na+ uptake was inhibited by avidin but not by the avidin biotin complex. Detergents and ionophores such as monensin also prevented the Na+ transport. The results indicate that the enzyme is able to convert the free energy of decarboxylation (delta Go' approximately equal to -30 kJ/mol) into a Na+ gradient.

Topics: Avidin; Biotin; Carboxy-Lyases; Glutarates; Gram-Negative Anaerobic Bacteria; Ion Channels; Monensin; Octoxynol; Polyethylene Glycols; Sodium

1982