An Intermediate Complex in the Dissociation of Aspartate Transcarbamylase

AUTOR(ES)

Evans, David R.

RESUMO

The multisubunit enzyme aspartate transcarbamylase consists of six copies of two types of polypeptide chains, catalytic (C) and regulatory (R). A complex formed by the partial dissociation of this enzyme has been isolated. This species, which has the structure C6R4, is a likely intermediate in the stepwise dissociation of aspartate transcarbamylase induced by mercurials. The formation of the complex is the result of the release of a single regulatory dimer (R2) from the parent molecule.

Documentos Relacionados

• Stopped-flow x-ray scattering: the dissociation of aspartate transcarbamylase.
• The structure of aspartate transcarbamylase, I. A molecular twofold axis in the complex with cytidine triphosphate.
• Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.
• Capture of an intermediate in the catalytic cycle of l-aspartate-β-semialdehyde dehydrogenase
• Unique aspects of the regulation of the aspartate transcarbamylase of Serratia marcescens.