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 f...
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| Published in | Bioscience, biotechnology, and biochemistry Vol. 63; no. 2; pp. 288 - 292 |
|---|---|
| Main Authors | , , , |
| 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 | |
| Online Access | Get full text |
| ISSN | 0916-8451 1347-6947 1347-6947 |
| DOI | 10.1271/bbb.63.288 |
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| Abstract | 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 |
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| AbstractList | 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 μM 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 μM 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 μM CCCP. 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. 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 super(+) 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 super(+) 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 super(+) pump was almost completely inhibited even at pH 8.5 as well as pH 6.5 by the addition of 2 mu M CCCP. 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 μM 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 μM 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 μM CCCP. 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.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. 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 μM 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 μM 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 μM CCCP. 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 |
| Author | Kim, Y.J Park, Y.H Hahm, K.S Kim, U.O. (Changwon National Univ., Kyungnam (Korea R.)) |
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| Keywords | Electrochemical potential Amylase Enzyme Cyclic AMP Bacteria Vibrionaceae Biosynthesis Vibrio alginolyticus Extracellular Catabolic repression |
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| References | (14) 1980; 24 Tokuda, H. and Unemoto, T. (11) 1983; 156 (7) 1990; 265 (16) 1996; 38 (3) 1983; 114 (4) 1990; 172 KIM Y J (1) 1991; 109 Welker, N. E. and Campbell, L. L. (9) 1963; 86 Boethling, R. S. (13) 1975; 123 (5) 1985; 82 Laemmli, U. K. (10) 1970; 227 Tokuda, H. and Unemoto, T. (2) 1984; 259 8 (15) 1981; 127 (6) 1986; 83 Pastan, I. and Adhya, S. (12) 1976; 40 |
| References_xml | – volume: 127 start-page: 193 issn: 0022-1287 issue: 1 year: 1981 ident: 15 publication-title: J. Gen. Microbiol. – volume: 38 start-page: 223 issn: 1039-9712 issue: 2 year: 1996 ident: 16 publication-title: Biochem. Mol. Biol. Int. – volume: 227 start-page: 680 issn: 0028-0836 year: 1970 ident: 10 publication-title: Nature (London) doi: 10.1038/227680a0 – volume: 156 start-page: 636 issn: 0021-9193 year: 1983 ident: 11 publication-title: J. Bacteriol. doi: 10.1128/JB.156.2.636-643.1983 – volume: 114 start-page: 113 issn: 0006-291X issue: 1 year: 1983 ident: 3 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(83)91601-7 – volume: 172 start-page: 6809 issn: 0021-9193 issue: 12 year: 1990 ident: 4 publication-title: J. Bacteriol. doi: 10.1128/jb.172.12.6809-6817.1990 – volume: 109 start-page: 616 issn: 0021-924X issue: 4 year: 1991 ident: 1 publication-title: J. Biochem. doi: 10.1093/oxfordjournals.jbchem.a123429 – volume: 86 start-page: 681 issn: 0021-9193 year: 1963 ident: 9 publication-title: J. Bacteriol. doi: 10.1128/JB.86.4.681-686.1963 – volume: 82 start-page: 4384 issn: 0027-8424 issue: 13 year: 1985 ident: 5 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.82.13.4384 – ident: 8 doi: 10.1016/0014-5793(90)80751-4 – volume: 259 start-page: 7785 issn: 0021-9258 issue: 12 year: 1984 ident: 2 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)42862-6 – volume: 83 start-page: 4219 issn: 0027-8424 issue: 12 year: 1986 ident: 6 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.83.12.4219 – volume: 123 start-page: 954 issn: 0021-9193 year: 1975 ident: 13 publication-title: J. Bacteriol. doi: 10.1128/JB.123.3.954-961.1975 – volume: 24 start-page: 803 issn: 0385-5600 issue: 9 year: 1980 ident: 14 publication-title: Microbiol. Immunol. doi: 10.1111/j.1348-0421.1980.tb02885.x – volume: 265 start-page: 18843 issn: 0021-9258 issue: 31 year: 1990 ident: 7 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)30590-2 – volume: 40 start-page: 527 issn: 0005-3678 year: 1976 ident: 12 publication-title: Bacteriol. Rev. doi: 10.1128/MMBR.40.3.527-551.1976 |
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| SubjectTerms | 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 |
| Title | cAMP-mediated catabolite repression and electrochemical potential-dependent production of an extracellular amylase in Vibrio alginolyticus |
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