cAMP-mediated catabolite repression and electrochemical potential-dependent production of an extracellular amylase in Vibrio alginolyticus.
Vibrio alginolyticus, a halophilic marine bacterium, produced an extracellular amylase with a molecular mass of approximately 56,000, and the amylase appeared to be subject to catabolite repression mediated by cAMP. The production of amylase at pH 6.5, at which the respiratory chain-linked H+ pump functions, was inhibited about 75% at 24 hours following the addition of 2 microM carbonyl cyanide m-chlorophenylhydrazone (CCCP), while the production at pH 8.5, at which the respiratory chain-linked Na+ pump functions, was only slightly inhibited by the addition of 2 microM CCCP. In contrast, the production of amylase in a mutant bacterium defective in the Na+ pump was almost completely inhibited even at pH 8.5 as well as pH 6.5 by the addition of 2 microM CCCP.
Kim
U O
UO
Department of Microbiology, College of Natural Sciences, Changwon National University, Sarim-Dong, Kyungnam, Korea.
Hahm
K S
KS
Park
Y H
YH
Kim
Y J
YJ
D000681:Amylases / Q000096:biosynthesis*; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000378:metabolism; D000242:Cyclic AMP / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008564:Membrane Potentials / Q000502:physiology; D008970:Molecular Weight; D009391:Nephelometry and Turbidimetry; D017494:Proton Pumps / Q000502:physiology; D000254:Sodium-Potassium-Exchanging ATPase / Q000502:physiology; D014733:Vibrio / Q000201:enzymology*
D017494:Proton Pumps; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D000242:Cyclic AMP; D000681:Amylases; D000254:Sodium-Potassium-Exchanging ATPase