Article
A study of D52S hen lysozyme-GlcNAc oligosaccharide complexes by NMR spectroscopy and electrospray mass spectrometry.
FEBS letters - 20 Jan 1992
Lumb K J, Aplin R T, Radford S E, Archer D B, Jeenes D J, Lambert N, MacKenzie D A, Dobson C M, Lowe G
Abstract excerpt
The production of a mutant hen lysozyme is described in which Asp-52, one of the catalytically important residues, is replaced by Ser. The mutant enzyme has very low catalytic activity but NMR studies show that its structure is closely similar to that of the wild-type protein. NMR experiments also show that well defined complexes are formed with GlcNAc4 and GlcNAc6 bound in the active site of the mutant enzyme....
Topics
- Acetylglucosamine
- Animals
- Binding Sites
- Chickens
- Magnetic Resonance Spectroscopy
- Mass Spectrometry
- Muramidase
- Mutation
- Oligosaccharides