David M. Chipman

TL;DR: The association constants for the binding of various saccharides to hen egg-white lyso enzyme and human lysozyme have been measured by fluorescence titration and it is suggested that subsite C of the human enzyme is "looser" than the equivalent site in the hen egg enzyme, so that the rearrangement of a saccharide in this subsite in response to introduction of an N-acetylmuramic acid residue into subsite D destabilizes the saccharid complexes

TL;DR: The catalytic machinery of these AHAS isozymes is entirely contained within the large subunits, and nearly all of the properties of the intact AHAS isozyme I or III can be reconstituted by mixing extracts containing the respective large and small subunits.

TL;DR: Results indicate that in the reactions studied over 90% of the new products must be formed by transglycosylation, and not by reversal of hydrolysis, leading to the formation of high oligosaccharides.

TL;DR: A mechanism is proposed for the enzyme that involves irreversible and rate-determining reaction of pyruvate, at a site which accepts 2-ketobutyrate poorly, if at all, to form an intermediate common to all the reactions.

TL;DR: A model for the structure of Escherichia coli AHAS isozyme II, based on its homology with pyruvate oxidase and experimental testing of the model by site-directed mutagenesis, has been used here to study how AHAS controls the chemical fate of a decarboxylated keto acid.