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Department of Molecular and Cell Biology

Regulation of nitrogen metabolism in vibrio alginolyticus

Abstract

dc:description.abstract

Aerated cultures of Vibrio alginolyticus produced histidase at 30°C but production of histidase was repressed by either incubation at 37°C or a lack of oxygen. A similar regulation system by temperature and oxygen has been reported for collagenase and prntease production by V. alginolyticus (Hare et al., 1981). V. alginolyticus had identical growth rates at 30 and 37°C. The histidine-utilization (hut) enzymes were coordinately induced by histidine. The inducible nitrogen catabolic enzymes arginase, alanine dehydrogenase and histidase were not subject to nitrogen catabolite repression. Various amino acids and ammonium ions stimulated the production of histidase and arginase. Urocanase and formiminoglutamate hydrolase were repressed by nitrogen-containing compounds. Tryptophan, glutamine and isoleucine either repressed or had little effect on the production of histidase and urocanase. The hut enzymes and alanine dehydrogenase were sensitive to catabolite repression by glucose. The addition of (NH₄)₂SO₄ stimulated histidase production. Cyclic AMP did npt relieve repression by glucose. Catabolite repression by glucose of collagenase and protease production in V. alginolyticus was also not relieved by cyclic AMP (Reid, 1981; Long et al., 1981).

Degree

thesis:*
Grantor dc:publisher.institution
Department of Molecular and Cell Biology
Year dc:date.issued
1984

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Bodasing, Sandhya Juggat
Advisor dc:contributor.advisor
  • Woods, David R

Rights

Language dc:language.iso
eng

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/11427/21893
OAI identifier oai:identifier
oai:open.uct.ac.za:11427/21893

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University of Cape Town
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Last updated
2026-07-22
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citation

Bodasing, Sandhya Juggat. Regulation of nitrogen metabolism in vibrio alginolyticus. Department of Molecular and Cell Biology, 1984. http://hdl.handle.net/11427/21893