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    Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha B5786 [Text] / T. G. Volova [et al.] // Appl. Biochem. Microbiol. - 2004. - Vol. 40, Is. 2. - P. 170-177, DOI 10.1023/B:ABIM.0000018921.04863.d5. - Cited References: 27 . - ISSN 0003-6838
РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
POLY-BETA-HYDROXYBUTYRATE
   ORGANISM ALCALIGENES-EUTROPHUS

   ESCHERICHIA-COLI

   PHB

   POLY(3-HYDROXYBUTYRATE)

   BIOSYNTHESIS

   CLONING

   GENES

   CHAIN

   H16

Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of key enzymes of PHB metabolism (beta-ketothiolase, acetoacetyl-CoA reductase, PHB synthase, D-hydroxybutyrate dehydrogenase, and PHB depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of beta-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase were recorded during acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only upon stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not affect the time course of the enzyme activity significantly.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Gorbunova, O.V.; Zhila, N.O.

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