Difference between tortoise and hen lysozymes in the mode of association with N-acetyl D-glucosamine as revealed by proton magnetic resonance spectroscopy.
Tortoise lysozyme, unlike hen lysozyme, does not distinguish between the alpha- and beta-anomeric forms of N-acetyl D-glucosamine. This indicates that alpha- and beta-anomeric forms of the inhibitor have the same affinities and experience identical magnetic environments in tortoise lysozyme. The dissociation constant of tortoise lysozyme-inhibitor complex was calculated from chemical shift data and found to be 3.5 X 10(-2) M. The enthalpy of dissociation was calculated to be 5.0 kcal/mol.
D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D005944:Glucosamine / Q000031:analogs & derivatives*; D009682:Magnetic Resonance Spectroscopy; D009113:Muramidase / Q000378:metabolism*; D014426:Turtles
D009113:Muramidase; D005944:Glucosamine; D000117:Acetylglucosamine