Advertisement

Bioenergetik und Enzymologie

  • G. Löffler
  • B. Wiederanders
Chapter
Part of the Springer-Lehrbuch book series (SLB)

Zusammenfassung

Für das Leben gelten dieselben physikalisch-chemischen Gesetze wie für die unbelebte Welt. Diese Erkenntnis setzte sich vor ungefähr 100 Jahren allgemein durch und hat unsere Betrachtungsweise biologischer Systeme revolutioniert. Diese wurden nämlich damit der naturwissenschaftlichen Beobachtung und Analyse zugänglich.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Literatur

Monographien und Lehrbücher

  1. Eisenthal R (1992) Enzyme assays. Irl Press, EnglandGoogle Scholar
  2. Ferscht A (1985) Enzyme structure and Mechanism. Freemann, New YorkGoogle Scholar
  3. Here G (1989) Allosteric Enzymes. Crc Press, Boca RatonGoogle Scholar
  4. Kuby SA (1991) A study of enzymes, vols I, II. Crc Press, Boca RatonGoogle Scholar
  5. Meister A (ed) Advances in enzymology. Vol 1–69, Wiley, New YorkGoogle Scholar
  6. Ogita ZI, Markert CL (eds) (1990) Isoenzymes: structure, function and use in biology and medicine. Wiley, New YorkGoogle Scholar
  7. Page MI, Williams A (eds) (1987) Enzyme mechanisms. The Royal Society of Chemistry, LondonGoogle Scholar
  8. Schellenberger A (Hrsg) (1989) Enzymkatalyse. Springer, Berlin Heidelberg New York TokioGoogle Scholar
  9. Webb EC (ed) (1992) Enzyme nomenclature. Academic Press, OrlandoGoogle Scholar
  10. Weber G (ed)(1994) Advances in enzyme regulation. Vols 1–34. Elsevier, OxfordGoogle Scholar

Original- und Übersichtsarbeiten

  1. Abe KR, Butker MH, Wright BE (1990) Cellular Concentrations of enzymes and their substrates. J Theor Biol 143: 163–195CrossRefGoogle Scholar
  2. Aragon JJ, Sols A (1991) Regulation of enzyme activity in the cell: effect of enzyme concentration. Faseb J 5, 2945–2950PubMedGoogle Scholar
  3. Goldberg DM (1992) Enzymes as agents for the treatment of desease. Clin Chim Acta 206: 45–76PubMedCrossRefGoogle Scholar
  4. Kisselev AF, Songyang Z, Goldberg AL (2000) Why does threonine, and not serine, function as the active site nucleophile in proteasomes? J Biol Chem 275 (20), 14831–14837PubMedCrossRefGoogle Scholar
  5. MA J, Sigler PB, Xu Z, Karplus M (2000) A dynamic model for the allosteric mechanism of GroEL. J Mol Biol 302 (2): 303–313PubMedCrossRefGoogle Scholar
  6. Rupert PB, Ferre-D’Amare AR (2001) Crystal structure of a hairpin ribozyme-inhibitor complex with implications for catalysis, Nature 410, 780PubMedCrossRefGoogle Scholar
  7. Schramm VL, Horenstein BA, Kline PC (1994) Transition state analysis and inhibitor design for enzymatic reactions. J Biol Chem 269: 18 259–18 262Google Scholar
  8. Srere PA, Ovadi J (1990) Enzyme-enzyme interactions and their metabolic role. Febs Lett 268, 360–364PubMedCrossRefGoogle Scholar
  9. Vocadlo DJ, Davies GJ, Laine R, Withers SG (2001) Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412: 835–838PubMedCrossRefGoogle Scholar
  10. Walpole CS, Wrigglesworth R (1989) Enzyme inhibitors in medicine. Nat Prod Rep 6: 311–346PubMedCrossRefGoogle Scholar
  11. Westerhoff HV, Welch GR (1992) Enzyme organization and the direction of metabolic flow: physicochemical considerations. Curr Top Cell Regul 33, 361–390PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2003

Authors and Affiliations

  • G. Löffler
  • B. Wiederanders

There are no affiliations available

Personalised recommendations