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Isolation of bioluminescent functions from Photobacterium leiognathi: analysis of luxA, luxB, luxG and neighboring genes / B. A. Illarrionov [et al.] // Gene. - 1990. - Vol. 86, Is. 1. - P89-94 . - ISSN 0378-1119
Кл.слова (ненормированные):
Bioluminescence -- expression in E. coli -- luciferase -- molecular evolution -- nucleotide sequence -- protein alignment -- recombinant DNA -- luciferase -- amino acid sequence -- article -- bioluminescence -- fungus -- gene structure -- genetic engineering -- heredity -- nonhuman -- nucleotide sequence -- priority journal -- vibrionaceae -- Acyltransferases -- Amino Acid Sequence -- Bacterial Proteins -- Base Sequence -- Cloning, Molecular -- DNA, Bacterial -- Genes, Structural, Bacterial -- Luciferase -- Luminescence -- Molecular Sequence Data -- Operon -- Photobacterium -- Restriction Mapping -- Escherichia coli -- Fungi -- Photobacterium leiognathi -- Vibrio harveyi -- Vibrionaceae
Аннотация: Genes encoding luminescence of Photobacterium leiognathi have been cloned in Escherichia coli. The luminescent clones were readily apparent. Among them, a clone containing a recombinant plasmid with a 13.5-kb insertion was identified. This DNA fragment contained all of the luminescence-encoding genes. The luciferase-encoding genes (lux) in this DNA fragment were localized. We have sequenced a part of the cloned lux region and identified the luxA, luxB and luxG genes encoding the ? and ? subunits of luciferase and a ? protein with an Mr of 26 180, respectively. The analysis of deduced amino acid sequences and comparison with known luciferase sequences from Vibrio harveyi, indicate the common origin of these proteins. В© 1990.

Scopus
Держатели документа:
Krasnoyarsk State University, Krasnoyarsk, 660062, Russian Federation
All-Union Research Institute of Molecular Biology, Novosibirsk Region, 633159, Russian Federation
Institute of Biophysics, Krasnoyarsk, 660036, Russian Federation
Institute of Clinical and Experimental Medicine, Novosibirsk, Russian Federation
Novosibirsk Institute of Bioorganic Chemistry, Novosibirsk, 630090, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Illarrionov, B.A.; Blinov, V.M.; Douchenko, A.P.; Protopopova, M.V.; Karginov, V.A.; Mertvetsov, N.P.; Gitelson, J.I.

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Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha / T. G. Volova [и др.] // Prikladnaia biokhimiia i mikrobiologiia. - 2004. - Vol. 40, Is. 2. - С. 201-209 . - ISSN 0555-1099
Кл.слова (ненормированные):
acetoacetyl coenzyme a reductase -- acetoacetyl-CoA reductase -- acetyl coenzyme A acyltransferase -- acyltransferase -- alcohol dehydrogenase -- carboxylesterase -- hydroxybutyrate dehydrogenase -- hydroxybutyric acid -- poly(3 hydroxyalkanoic acid) depolymerase -- poly(3-hydroxyalkanoic acid) depolymerase -- poly(3-hydroxyalkanoic acid) synthase -- polyhydroxyalkanoate synthase -- polymer -- article -- chemistry -- comparative study -- culture medium -- enzymology -- growth, development and aging -- metabolism -- Wautersia eutropha -- Acetyl-CoA C-Acyltransferase -- Acyltransferases -- Alcohol Oxidoreductases -- Carboxylic Ester Hydrolases -- Culture Media -- Cupriavidus necator -- Hydroxybutyrate Dehydrogenase -- Hydroxybutyrates -- Polymers
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of the key enzymes of PHB metabolism (beta-ketothiolase, acetoacetyl-CoA reductase, PHA synthase, D-hydroxybutyrate dehydrogenase, and PHA 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 PHA synthase were recorded at the stage of acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only at stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not cause any marked changes in the time course of enzyme activity.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036 Russia. : 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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The synthesis of hydroxybutyrate and hydroxyvalerate copolymers by the bacterium Ralstonia eutropha / T. G. Volova, G. S. Kalacheva // Mikrobiologiya. - 2005. - Vol. 74, Is. 1. - С. 63-69 . - ISSN 0026-3656
Кл.слова (ненормированные):
?-ketothiolase -- Controlled synthesis -- Poly(hydroxybutyrate-co-hydroxyvalerate) -- Ralstonia eutropha -- Bacteria (microorganisms) -- Cupriavidus necator -- acetoacetyl coenzyme a -- acetyl coenzyme A acyltransferase -- acyl coenzyme A -- acyltransferase -- butyric acid derivative -- carbon dioxide -- fructose -- hydrogen -- poly(3 hydroxybutyrate) co (3 hydroxyvalerate) -- poly(3-hydroxyalkanoic acid) synthase -- poly(3-hydroxybutyrate)-co-(3-hydroxyvalerate) -- polyester -- polyhydroxyalkanoate synthase -- valeric acid derivative -- article -- chemistry -- crystallization -- culture medium -- metabolism -- Wautersia eutropha -- Acetyl-CoA C-Acyltransferase -- Acyl Coenzyme A -- Acyltransferases -- Butyrates -- Carbon Dioxide -- Crystallization -- Culture Media -- Cupriavidus necator -- Fructose -- Hydrogen -- Polyesters -- Valerates
Аннотация: The paper deals with the study of the synthesis of 3-hydroxybutyrate (3HB) and 3-hydroxyvalerate (3HV) copolymers by the bacterium Ralstonia eutropha B-5786 grown under different carbon nutrition conditions (growth on carbon dioxide, fructose, and CO2-valerate and fructose-valerate mixtures). The parameters to be analyzed included the yield of biomass, the yield, synthesis rate, and composition of copolymers, the activity of the key enzymes of polyhydroxyalkanoate (PHA) synthesis (?-ketothiolase, acetoacetyl-CoA reductase, and PHA synthase), the maximum tolerable concentration of valerate to the bacterium, and the conditions that govern the incorporation of hydroxyvalerate to copolymers. This allowed the relationship between cultivation conditions and the proportion of monomers in the copolymers to be deduced. We were able to synthesize a range of 3HB/3HV copolymers and found that the thermal characteristics and the degree of crystallinity of these copolymers depend on the molar fraction of 3HV.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.

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