Evidence for the Novel Metabolic Pathway of Ralstonia eutropha H16 to Metabolize L‐ascorbate Ryan Joyce, Tyler Stack, Michael Carter
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منابع مشابه
Essential role of the hprK gene in Ralstonia eutropha H16.
Ralstonia eutropha H16 possesses an incomplete phosphoenolpyruvate (PEP):sugar phosphotransferase system (PTS) composed of EI, HPr, EIIA(Ntr) (PtsN) and EIIA(Man) (PtsM). We could show that in vitro the incomplete PTS phosphorylation cascade is partially functional. HPr becomes phosphorylated by PEP and EI, and transfers the phosphoryl group to EIIA(Ntr), but only extremely slowly to EIIA(Man)....
متن کاملTranscriptional regulation of nitric oxide reduction in Ralstonia eutropha H16.
Nitric oxide reduction in Ralstonia eutropha H16 is catalysed by the quinol-dependent NO reductase NorB. norB and the adjacent norA form an operon that is controlled by the sigma(54)-dependent transcriptional activator NorR in response to NO. A NorR derivative containing MalE in place of the N-terminal domain binds to a 73 bp region upstream of norA that includes three copies of the putative up...
متن کاملGenomic view of energy metabolism in Ralstonia eutropha H16.
Ralstonia eutropha is a strictly respiratory facultative lithoautotrophic beta-proteobacterium. In the absence of organic substrates, H2 and CO2 are used as sole sources of energy and carbon. In the absence of oxygen, the organism can respire by denitrification. The recent determination of the complete genome sequence of strain H16 provides the opportunity to reconcile the results of previous p...
متن کاملComparative proteome analysis reveals four novel polyhydroxybutyrate (PHB) granule-associated proteins in Ralstonia eutropha H16.
Identification of proteins that were present in a polyhydroxybutyrate (PHB) granule fraction isolated from Ralstonia eutropha but absent in the soluble, membrane, and membrane-associated fractions revealed the presence of only 12 polypeptides with PHB-specific locations plus 4 previously known PHB-associated proteins with multiple locations. None of the previously postulated PHB depolymerase is...
متن کاملBinding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules.
The surface of polyhydroxybutyrate (PHB) storage granules in bacteria is covered mainly by proteins referred to as phasins. The layer of phasins stabilizes the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. Phasin PhaP1(Reu) is the major surface protein of PHB granules in Ralstonia e...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2019
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.2019.33.1_supplement.651.12