Abstract
THE regulatory enzyme aspartate transcarbamylase (ATCase) from Escherichia coli contains two non-identical protein sub-units, one the catalytic subunit which provides the active sites of the enzyme, and the other the regulatory subunit which provides the binding sites for nucleotide inhibitors and activators1,2. The catalytic subunit is a trimer of “C” polypeptide chains, associated by three heterologous c: c domains of bonding (terminology given by Monod et al.3 and Cohlberg et al.4). The regulatory subunit is a dimer of “R” chains, associated by an isologous r: r domain. Two catalytic and three regulatory subunits interact specifically across six r: c domains of inter-subunit bonding to complete the quaternary structure of the ATCase molecule.
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Regulatory Properties of Intergeneric Hybrids of Aspartate Transcarbamylase. Nature New Biology 238, 264–266 (1972). https://doi.org/10.1038/newbio238264a0
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DOI: https://doi.org/10.1038/newbio238264a0
