Insights into bacterial CO2 metabolism revealed by the characterization of four carbonic anhydrases in Ralstonia eutropha H16
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چکیده
منابع مشابه
Genomic 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 کاملPeriplasmic α-carbonic anhydrase plays an essential role in Ralstonia eutropha CO2 metabolism
Background Carbonic anhydrase (CA) enzymes catalyze the interconversion of CO2 and bicarbonate. These enzymes play important roles in cellular metabolism such as CO2 transport, ion transport, and internal pH regulation. Understanding the roles of CAs in the chemolithotropic betaproteobacteria Ralstonia eutropha is important for the development of fermentation processes based on the bacterium’s ...
متن کاملEssential 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 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...
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ژورنال
عنوان ژورنال: AMB Express
سال: 2014
ISSN: 2191-0855
DOI: 10.1186/2191-0855-4-2