Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha.
about
A new type of thermoalkalophilic hydrolase of Paucimonas lemoignei with high specificity for amorphous polyesters of short chain-length hydroxyalkanoic acids.Ralstonia eutropha H16 encodes two and possibly three intracellular Poly[D-(-)-3-hydroxybutyrate] depolymerase genesUnraveling the function of the Rhodospirillum rubrum activator of polyhydroxybutyrate (PHB) degradation: the activator is a PHB-granule-bound protein (phasin).The PHA Depolymerase Engineering Database: A systematic analysis tool for the diverse family of polyhydroxyalkanoate (PHA) depolymerases.Production of the chiral compound (R)-3-hydroxybutyrate by a genetically engineered methylotrophic bacteriumPoly-3-hydroxybutyrate metabolism in the type II methanotroph Methylocystis parvus OBBP.Evidence for lytic transglycosylase and β-N-acetylglucosaminidase activities located at the polyhydroxyalkanoates (PHAs) granules of Thermus thermophilus HB8.Polyester synthases: natural catalysts for plastics.A patatin-like protein associated with the polyhydroxyalkanoate (PHA) granules of Haloferax mediterranei acts as an efficient depolymerase in the degradation of native PHAFunctionalized PHB granules provide the basis for the efficient side-chain cleavage of cholesterol and analogs in recombinant Bacillus megateriumEnoyl-CoA hydratase mediates polyhydroxyalkanoate mobilization in Haloferax mediterranei.Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes).New insights in the formation of polyhydroxyalkanoate granules (carbonosomes) and novel functions of poly(3-hydroxybutyrate).Symbiotic factors in Burkholderia essential for establishing an association with the bean bug, Riptortus pedestris.Absence of ppGpp Leads to Increased Mobilization of Intermediately Accumulated Poly(3-Hydroxybutyrate) in Ralstonia eutropha H16.Low temperature-induced viable but not culturable state of Ralstonia eutropha and its relationship to accumulated polyhydroxybutyrate.Localization of poly(3-hydroxybutyrate) (PHB) granule-associated proteins during PHB granule formation and identification of two new phasins, PhaP6 and PhaP7, in Ralstonia eutropha H16.The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production.Polyhydroxyalkanoate (PHA) Granules Have no Phospholipids.Purification and properties of an intracellular 3-hydroxybutyrate-oligomer hydrolase (PhaZ2) in Ralstonia eutropha H16 and its identification as a novel intracellular poly(3-hydroxybutyrate) depolymerase.The "intracellular" poly(3-hydroxybutyrate) (PHB) depolymerase of Rhodospirillum rubrum is a periplasm-located protein with specificity for native PHB and with structural similarity to extracellular PHB depolymerases.In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases.Photoautotrophic Polyhydroxybutyrate Granule Formation Is Regulated by Cyanobacterial Phasin PhaP in Synechocystis sp. Strain PCC 6803.3-Hydroxybutyrate oligomer hydrolase and 3-hydroxybutyrate dehydrogenase participate in intracellular polyhydroxybutyrate and polyhydroxyvalerate degradation in Paracoccus denitrificans.Examination of PHB Depolymerases in Ralstonia eutropha: Further Elucidation of the Roles of Enzymes in PHB Homeostasis.PhaM is the physiological activator of poly(3-hydroxybutyrate) (PHB) synthase (PhaC1) in Ralstonia eutropha.Assay of poly(3-hydroxybutyrate) depolymerase activity and product determination.Poly(3-hydroxybutyrate) (PHB) depolymerase PhaZa1 is involved in mobilization of accumulated PHB in Ralstonia eutropha H16."Intelligent" descriptions of microbial kinetics in finitely dispersed bioreactors: neural and cybernetic models for PHB biosynthesis by Ralstonia eutropha.Novel intracellular 3-hydroxybutyrate-oligomer hydrolase in Wautersia eutropha H16.Properties of a novel intracellular poly(3-hydroxybutyrate) depolymerase with high specific activity (PhaZd) in Wautersia eutropha H16.Isolated poly(3-hydroxybutyrate) (PHB) granules are complex bacterial organelles catalyzing formation of PHB from acetyl coenzyme A (CoA) and degradation of PHB to acetyl-CoA.To be or not to be a poly(3-hydroxybutyrate) (PHB) depolymerase: PhaZd1 (PhaZ6) and PhaZd2 (PhaZ7) of Ralstonia eutropha, highly active PHB depolymerases with no detectable role in mobilization of accumulated PHB.Comparative proteome analysis reveals four novel polyhydroxybutyrate (PHB) granule-associated proteins in Ralstonia eutropha H16Impact of Ralstonia eutropha's poly(3-Hydroxybutyrate) (PHB) Depolymerases and Phasins on PHB storage in recombinant Escherichia coli.Biochemical characterization of a new type of intracellular PHB depolymerase from Rhodospirillum rubrum with high hydrolytic activity on native PHB granules.Reporting Key Features in Cold-Adapted Bacteria.Enhancement of stress tolerance in the polyhydroxyalkanoate producers without mobilization of the accumulated granules.Biochemical evidence that phaZ gene encodes a specific intracellular medium chain length polyhydroxyalkanoate depolymerase in Pseudomonas putida KT2442: characterization of a paradigmatic enzyme.
P2860
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P2860
Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha.
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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name
Mobilization of poly
@nl
Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha.
@en
type
label
Mobilization of poly
@nl
Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha.
@en
prefLabel
Mobilization of poly
@nl
Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha.
@en
P2093
P2860
P1476
Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha.
@en
P2093
D Jendrossek
R Handrick
S Reinhardt
P2860
P304
P356
10.1128/JB.182.20.5916-5918.2000
P407
P577
2000-10-01T00:00:00Z