| Literature DB >> 8576067 |
C Haseltine1, M Rolfsmeier, P Blum.
Abstract
An alpha-amylase was purified from culture supernatants of Sulfolobus solfataricus 98/2 during growth on starch as the sole carbon and energy source. The enzyme is a homodimer with a subunit mass of 120 kDa. It catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies. Addition of exogenous glucose represses production of alpha-amylase, demonstrating that a classical glucose effect is operative in this organism. Synthesis of [35S]-alpha-amylase protein is also subject to the glucose effect. alpha-Amylase is constitutively produced at low levels but can be induced further by starch addition. The absolute levels of alpha-amylase detected in culture supernatants varied greatly with the type of sole carbon source used to support growth. Aspartate was identified as the most repressing sole carbon source for alpha-amylase production, while glutamate was the most derepressing. The pattern of regulation of alpha-amylase production seen in this organism indicates that a catabolite repression-like system is present in a member of the archaea.Entities:
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Year: 1996 PMID: 8576067 PMCID: PMC177752 DOI: 10.1128/jb.178.4.945-950.1996
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490