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PMID: 6293874 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 148 ·No. 1 ·1982-11-01 ·Pages 35-8

Buckel W, Semmler R

Abstract

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.

MeSH Terms
Avidin/pharmacology Biotin/physiology Carboxy-Lyases/metabolism Glutarates/metabolism Gram-Negative Anaerobic Bacteria Ion Channels/metabolism Monensin/pharmacology Octoxynol Polyethylene Glycols/pharmacology Sodium/metabolism
Chemicals
Glutarates Ion Channels Avidin glutaconic acid Polyethylene Glycols Biotin Octoxynol Monensin Sodium Carboxy-Lyases glutaconyl CoA decarboxylase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Buckel W
Semmler R
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1982-11-01
Pages
35-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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