cAMP-mediated catabolite repression and electrochemical potential-dependent production of an extracellular amylase in Vibrio alginolyticus

• Published in: Bioscience, biotechnology, and biochemistry Vol. 63; no. 2; pp. 288 - 292
• Main Authors: Kim, U.O. (Changwon National Univ., Kyungnam (Korea R.)), Hahm, K.S, Park, Y.H, Kim, Y.J
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.02.1999; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: AMILASAS; AMYLASE; AMYLASES; Amylases - biosynthesis; aquatic bacteria; Bacteriology; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Carbonyl Cyanide m-Chlorophenyl Hydrazone - metabolism; carbonyl cyanide m-chlorophenylhydrazone; CATABOLISM; CATABOLISME; CATABOLISMO; catabolite repression; cyanides; Cyclic AMP - metabolism; electrochemical potential; electrochemistry; Electrophoresis, Polyacrylamide Gel; extracellular amylase; Fundamental and applied biological sciences. Psychology; Hot Temperature; Hydrogen-Ion Concentration; Membrane Potentials - physiology; Metabolism. Enzymes; Microbiology; Mission oriented research; Molecular Weight; mutants; Nephelometry and Turbidimetry; Physiology and metabolism; production; Proton Pumps - physiology; Sodium-Potassium-Exchanging ATPase - physiology; VIBRIO; Vibrio - enzymology; Vibrio alginolyticus; Electrochemical potential; Amylase; Enzyme; Cyclic AMP; Bacteria; Vibrionaceae; Biosynthesis; Vibrio alginolyticus; Extracellular; Catabolic repression
• ISSN: 0916-8451; 1347-6947; 1347-6947
• DOI: 10.1271/bbb.63.288

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 mu-M 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 mu-M 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 mu-M CCCP