Enzyme catalysis: conflicting requirements of substrate access and transition state affinity.

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  • Author(s): Wolfenden R
  • Source:
    Molecular and cellular biochemistry [Mol Cell Biochem] 1974 May 30; Vol. 3 (3), pp. 207-11.
  • Publication Type:
    Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Springer Country of Publication: Netherlands NLM ID: 0364456 Publication Model: Print Cited Medium: Print ISSN: 0300-8177 (Print) Linking ISSN: 03008177 NLM ISO Abbreviation: Mol Cell Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: New York : Springer
      Original Publication: The Hague, Dr. W. Junk B. V. Publishers.
    • Subject Terms:
      Enzymes/*metabolism; Adenosine Monophosphate ; Binding Sites ; Catalysis ; Cytochrome c Group ; Electron Transport Complex IV/metabolism ; Fumarate Hydratase/metabolism ; Isomerases/metabolism ; Ketosteroids ; Kinetics ; Lyases/metabolism ; Malates ; Models, Biological ; Protein Binding ; Succinates ; Superoxide Dismutase
    • References:
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      J Biol Chem. 1966 Feb 10;241(3):700-6. (PMID: 5908137)
      J Biol Chem. 1966 Feb 10;241(3):580-7. (PMID: 5908123)
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    • Accession Number:
      0 (Cytochrome c Group)
      0 (Enzymes)
      0 (Ketosteroids)
      0 (Malates)
      0 (Succinates)
      415SHH325A (Adenosine Monophosphate)
      EC 1.15.1.1 (Superoxide Dismutase)
      EC 1.9.3.1 (Electron Transport Complex IV)
      EC 4.- (Lyases)
      EC 4.2.1.2 (Fumarate Hydratase)
      EC 5.- (Isomerases)
    • Publication Date:
      Date Created: 19740530 Date Completed: 19740822 Latest Revision: 20190818
    • Publication Date:
      20221208
    • Accession Number:
      10.1007/BF01686645
    • Accession Number:
      4365214