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Why Are Enzymes Interconvertible?

  • Richard H. Haschke
  • Ludwig HeilmeyerJr.
  • Ernst Helmreich

Abstract

A logical progression from an enzyme with no regulatory capacity (i.e. active in the presence of substrate) to an enzyme with the capacity for activity modulation is not hard to visualize. There is a definite selective advantage gained by an organism that does not waste energy in producing unnecessary products. At present, in evolutionary time, the wide occurrence of allosteric control provides ample evidence of this fact (1). We want to consider, however, a possibly higher level in the sophistication of enzyme regulation; that is covalent interconversion of enzymes. If indeed this represents a more sophisticated type of metabolic control, examples should provide evidence of an advantage to be gained by such modification.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1972

Authors and Affiliations

  • Richard H. Haschke
    • 1
  • Ludwig HeilmeyerJr.
    • 1
  • Ernst Helmreich
    • 1
  1. 1.Physiologisch-chemisches InstitutUniversität WürzburgWürzburgGermany

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