Disease relevance of Propionigenium

• The three Na(+)-translocating enzymes, oxaloacetate decarboxylase of Klebsiella pneumoniae, NADH: ubiquinone oxidoreductase of Vibrio alginolyticus and ATPase (F1F0) of Propionigenium modestum have been isolated and studied with respect to structure and function [1].
• Expression of subunits a and c of the sodium-dependent ATPase of Propionigenium modestum in Escherichia coli [2].

High impact information on Propionigenium

• A carbodiimide with a photoactivatable diazirine substituent was synthesized and incubated with the Na(+)-translocating F(1)F(0) ATP synthase from both Propionigenium modestum and Ilyobacter tartaricus [3].
• Incubation of the purified F1F0-ATPase of Propionigenium modestum with dicyclohexylcarbodiimide (DCCD) led to inactivation of the enzyme in a strongly pH-dependent manner [4].
• After incorporation of the purified Na(+)-translocating F0F1-ATPase from Propionigenium modestum into preformed phospholipid vesicles the synthesis of ATP from ADP and inorganic phosphate could be observed under conditions where a valinomycin-mediated K+ diffusion potential (delta psi) and/or a Na+ concentration gradient (delta pNa) were imposed [5].
• Nucleotide sequence of the F0 subunits of the sodium dependent F1F0 ATPase of Propionigenium modestum [6].
• Sequence of subunits a and b of the sodium ion translocating adenosine triphosphate synthase of Propionigenium modestum [7].

Chemical compound and disease context of Propionigenium

• Specific protection by Na+ or Li+ of the F1F0-ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide [4].
• A prominent example is Propionigenium modestum, which converts the free energy of the decarboxylation of (S)-methylmalonyl-CoA to propionyl-CoA (DeltaG degrees =-20.6 kJ/mol) into an electrochemical Na(+) ion gradient across the membrane [8].
• Subunit c of the F1Fo-ATPase from Propionigenium modestum was extracted from the particulate cell fraction with chloroform/methanol [9].
• In Propionigenium modestum, ATP biosynthesis is entirely dependent on the Na+ ion gradient established upon decarboxylation of methylmalonyl-CoA [1].
• Sequence of subunit c of the sodium ion translocating adenosine triphosphate synthase of Propionigenium modestum [10].

Biological context of Propionigenium

• Studies on Na+ and H+ translocation through the Fo part of the Na(+)-translocating F1Fo ATPase from Propionigenium modestum: discovery of a membrane potential dependent step [11].
• Kinetics of inactivation of the F1Fo ATPase of Propionigenium modestum by dicyclohexylcarbodiimide in relationship to H+ and Na+ concentration: probing the binding site for the coupling ions [12].
• N-terminal amino acid sequences of the subunits of the Na(+)-translocating F1F0 ATPase from Propionigenium modestum [13].
• A deletion mutant of Escherichia coli lacking the genes for ATPase subunits a, c, b, delta and part of the alpha subunit was transformed with a plasmid containing the corresponding genes of the sodium-translocating ATPase of Propionigenium modestum [14].

Anatomical context of Propionigenium

• The ATP-hydrolyzing activity of Propionigenium modestum was extracted from the membranes with Triton X-100 or by incubation with EDTA at low ionic strength [15].

Gene context of Propionigenium

• Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump [16].
• Purified F1Fo ATPase of Propionigenium modestum was rapidly inactivated by dicyclohexylcarbodiimide (DCCD) with k2 = 1.2 x 10(5) M-1 min-1 at pH 5.6 and 0 degree C. Na+ ions provided specific protection from the modification by DCCD while protons stimulated the reaction [12].
• We report here the N-terminal protein sequences of the subunits of the ATPase from Propionigenium modestum [13].

References