Abstract
MOST intracellular enzymes are composed of more than one subunit. Where this is so, specificity in the interaction between subunits must be as important as specificity for substrates and the integrity of the catalytic structures of the molecule. All these features of enzyme proteins arise from their specific primary structures and may be modified during evolution as a result of changes in amino-acid sequence. The problem is posed as to whether the chemical structures within a subunit enabling it to combine with others are conserved during evolution or, on the other hand, whether they are modified during the divergence of homologous enzymes and isoenzymes.
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WATTS, D., FOCANT, B., MORELAND, B. et al. Formation of a Hybrid Enzyme between Echinoderm Arginine Kinase and Mammalian Creatine Kinase. Nature New Biology 237, 51–53 (1972). https://doi.org/10.1038/newbio237051a0
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DOI: https://doi.org/10.1038/newbio237051a0
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