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Record 1 2011-01-05


Subject field(s)
  • Biological Sciences

Distinct polypeptide chain in which lies the domain accommodating the catalytic site of complex enzymes. It is completely separated from the domain building up the binding site for the regulatory effector(s). From an evolutionary viewpoint, it is probable that gene fusion did occur in most cases rather than that originally continuous polypeptide chains have separated. In some oligomeric enzymes the allosteric site may have appeared as a result of gene duplication, e.g. in glutamate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase, whereas in others by acquisition of a foreign structural gene, e.g. the NAD-binding domain in glycogen phosphorylase. However, in present day complex enzymes the catalytic and regulatory protein units remained separate, but associable, entities.


The ATCase of E. coli has ... a molecular weight of about 310,000 but can be dissociated by treatment with mercurial reagents to yield two identical catalytic subunits and three identical regulatory subunits. Each of the two catalytic subunits has a molecular weight of about 100,000 and contains three polypeptide chains of molecular weight 34,000 called C chains. Each catalytic subunit contains three binding sites for the substrate aspartate, one on each of the three C chains. The catalytic subunits have enzymatic activity but are not sensitive to the modulator CTP.


  • Sciences biologiques

Lorsque la molécule native d'ATCase est dissociée en un mélange de ses sous-unités catalytiques et régulatrices, ce mélange fait toujours montre d'activité catalytique, mais la réaction n'est pas inhibée par le CTP tant que les sous-unités catalytiques et régulatrices sont séparées les unes des autres. Pour que l'inhibition par le CTP puisse avoir lieu, il faut que les sous-unités catalytiques et régulatrices soient physiquement associées dans la molécule oligomérique d'ATCase intacte.


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