PRODUCT-INDUCED STABILIZATION OF TERTIARY AND QUATERNARY STRUCTURE INESCHERICHIA-COLI DEHYDROQUINASE

The effects of irreversibly attaching product at the active site of ty pe I dehydroquinase from Escherichia coli have been investigated at th e level of the secondary, tertiary, and quaternary structure of the pr otein by spectroscopic and hydrodynamic techniques. The results agree with the previously identified stabilization of the enzyme but show fo r the first time that the protein dimer is also stabilized and suggest that the E. coli dehydroquinase subunit may be bilobal.