ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Inorganic Chemistry  (1)
  • Protein phosphorylation  (1)
  • sugar transport  (1)
Collection
Keywords
Publisher
Years
  • 1
    Electronic Resource
    Electronic Resource
    Darstellung und Molekülstruktur eines Metallclusters mit Cubanstruktur, [η5-C5H5Mo(CO)3HgMo] 4 (1979)
    Weinheim : Wiley-Blackwell
    Berichte der deutschen chemischen Gesellschaft 112 (1979), S. 2413-2418 
    Details
    ISSN: 0009-2940
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Synthesis and Molecular Structure of a Metal Cluster with Cubane Structure, [η5-C5H5Mo(CO)3HgMo]4(4)The compound [η5-C5H5Mo(CO)3HgMo]4 has been isolated as an additional product of the reaction between [η5-C5H5Mo(CO)3]2, 2-butenyl chloride, and sodium amalgam. The X-ray structure (R = 0·050) analysis of this novel species revealed that the compound has a slightly distorted cubane structure, for the first time the cubane unit being built up by two different metal atoms (Mo and Hg).
    Notes: Die Verbindung [η5-C5H5Mo(CO)3HgMo]4 (4) wurde als weiteres Produkt der Reaktion zwischen [η5-C5H5Mo(CO)3]2, 2-Butenylchlorid und Natriumamalgam isoliert. Die Röntgenstrukturanalyse dieser neuartigen Spezies zeigt eine leicht verzerrte Cubanstruktur, bei der das Cubangerüst erstmals aus zwei verschiedenen Metallatomen (Mo und Hg) aufgebaut ist. Der R-Wert beträgt 0·050.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cber.19791120708
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    The role of phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, in the regulation of carbon metabolism in gram-positive bacteria (1993)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 51 (1993), S. 19-24 
    Details
    ISSN: 0730-2312
    Keywords: phosphotransferase system ; HPr ; sugar transport ; gram-positive bacteria ; protein kinase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: HPr of the Gram-positive bacterial phosphotransferase system (PTS) can be phosphorylated by an ATP-dependent protein kinase on a serine residue or by PEP-dependent Enzyme I on a histidyl residue. Both phosphorylation events appear to influence the metabolism of non-PTS carbon sources. Catabolite repression of the gluconate (gnt) operon of B. subtilis appears to be regulated by the former phosphorylation event, while glycerol kinase appears to be regulated by the latter phosphorylation reaction. The extent of our understanding of these processes will be described. © 1993 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240510105
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Protein Phosphorylation in Bacteria - Regulation of Gene Expression, Transport Functions, and Metabolic Processes (1988)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 27 (1988), S. 1040-1049 
    Details
    ISSN: 0570-0833
    Keywords: Protein phosphorylation ; Phosphorylation ; Bacteria ; Gene expression ; Metabolism ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The importance of protein phosphorylation to the regulation of physiological processes in eukaryotic cells has been known for almost half a century. In contrast, the first conclusive evidence for functionally relevant protein phosphorylation in bacteria was obtained less than a decade ago. To date, only five functionally well-characterized bacterial proteins have been shown to be regulated by reversible phosphorylation. (1) Phosphorylation of isocitrate dehydrogenase in Escherichia coli controls the relative flux of carbon through the Krebs cycle and the glyoxylate shunt. (2) In gram-positive bacteria, phosphorylation of HPr, a phosphoryl carrier protein of the phosphoenolypyruvate-dependent sugar phosphotransferase system, regulates carbohydrate uptake via this system. (3) Phosphorylation of glycerol kinase in Streptococcus faecalis probably serves to regulate the degradation of glycerol. (4) Phosphorylation of the nitrogen regulatory protein I (NR1) in E. coli controls expression of genes encoding the enzymes which participate in nitrogen metabolism. (5) Phosphorylation of citrate lyase ligase in Clostridium sphenoides regulates the conversion of citrate lyase from the inactive sulfhydryl form to the active acetylated form. Recent investigations have shown that more than one hundred proteins in E. coli are phosphorylated. It can therefore be anticipated that protein phosphorylation will prove to be as important to the regulation of physiological processes in bacteria as it is in eukaryotes.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.198810401
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...