Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.

Ítems similars

• Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase.
  per: Robey, E A, et al.
  Publicat: (1986)
• A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity.
  per: Markby, D W, et al.
  Publicat: (1991)
• Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability.
  per: Peterson, C. B., et al.
  Publicat: (1994)
• Propagation of conformational changes in Ni(II)-substituted aspartate transcarbamoylase: Effect of active-site ligands on the regulatory chains
  per: Johnson, Ronald S., et al.
  Publicat: (1980)
• A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.
  per: Zhou, B. B., et al.
  Publicat: (1994)