Export of alpha-amylase by Bacillus amyloliquefaciens requires proton motive force.
The secretion of protein directly into the extracellular medium by Bacillus amyloliquefaciens, a gram-positive bacterium, was shown to be dependent on proton motive force. When the electrochemical membrane potential gradient of protons was dissipated either by uncouplers or by valinomycin in combination with K+, a precursor form of alpha-amylase accumulated on the cellular membrane. The proton motive force could be dissipated without altering the intracellular level of ATP, indicating that the observed inhibition of export was not the result of decreased ATP concentration.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001407:Bacillus / Q000201:enzymology* / Q000378:metabolism; D001692:Biological Transport; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D004792:Enzyme Precursors / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008564:Membrane Potentials; D011188:Potassium / Q000494:pharmacology; D011522:Protons; D014634:Valinomycin / Q000494:pharmacology; D000516:alpha-Amylases / Q000378:metabolism*
D004792:Enzyme Precursors; D011522:Protons; D014634:Valinomycin; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D000255:Adenosine Triphosphate; D000516:alpha-Amylases; D011188:Potassium