Productive and unproductive lysozyme-chitosaccharide complexes. Kinetic investigations.
Flow and relaxation methods were used to study the kinetics of oligosaccharides binding to lysozyme and the pre-steady-state kinetics of the lysozyme-catalyzed, hydrolysis of chitohexose. The minimal mechanism demonstrated, and the kinetics parameters pertaining to the elementary steps, allow interpretations of previous equilibrium and steady-state kinetic measurements which had yielded only complex constants, reflecting both productive and unproductive lysozyme-substrate complexes. In contrast to previous assumptions, the data presented in this paper provide evidence for "stable" productive lysozyme-substrate complexes. Our proposed mechanism utilizes structural information and accounts for the difference in efficiency of lysozyme-catalyzed hydrolysis of chitopentose and chitohexose.
D000117:Acetylglucosamine / Q000378:metabolism; D002686:Chitin / Q000378:metabolism; D007700:Kinetics; D009113:Muramidase / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013696:Temperature
D009844:Oligosaccharides; D002686:Chitin; D009113:Muramidase; D000117:Acetylglucosamine