Journal ArticleDOI
The nuclear magnetic resonance determination of the conformation of saccharides bound in subsite D of lysozyme.
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TLDR
The coupling constant for the bound saccharides indicates that the dihedral angle between C1 and C2 for the reducing saccharide is not significantly changed upon binding to lysozyme, which is discussed in terms of other evidence for the role of distortion of thesaccharide bound in subsite D in the lyso enzyme-catalyzed hydrolysis of cell wall oligosaccharides.Abstract:
The binding of the trisaccharide (2-acetamido-2-deoxy-D-muramic acid)-β(1→4)-(2-aceta-mido-2-deoxy-D-glucosyl)-β(1→4)-(2-acetamido-2-deoxy-D-muramic acid) to subsites B, C, and D in lysozyme has been studied by 1H nuclear magnetic resonance methods. In particular, the coupling constant between H1 and H2 of the reducing saccharide bound in subsite D has been determined. The coupling constant for the bound saccharide indicates that the dihedral angle between C1 and C2 for the reducing saccharide is not significantly changed upon binding to lysozyme. This result is discussed in terms of other evidence for the role of distortion of the saccharide bound in subsite D in the lysozyme-catalyzed hydrolysis of cell wall oligosaccharides.read more
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Journal ArticleDOI
What's new in lysozyme research? Always a model system, today as yesterday.
Pierre Jollès,Jacqueline Jollès +1 more
TL;DR: A review of the main achievements realized in the lysozyme research field since the meeting held in 1972 to commemorate the fiftieth anniversary of the discovery of this enzyme is presented in this article.
Journal ArticleDOI
Lysozyme revisited : crystallographic evidence for distortion of an n-acetylmuramic acid residue bound in site d
TL;DR: The resulting atomic co-ordinates indicate that the NAM residue in site D is distorted from the full 4C1 chair conformation to one in which the ring atoms C-1, C-2, O-5 and C-5 are approximately coplanar, and the hydroxymethyl group is positioned axially (a conformation best described as a sofa).
Journal ArticleDOI
Microcalorimetric study of wheat germ agglutinin binding to N-acetylglucosamine and its oligomers.
TL;DR: A model of four independent binding sites was found to adequately describe the binding curves, except in the case of (GlcNAc)4 which exhibited positive cooperativity, indicating that the binding process is enthalpically driven.
Journal ArticleDOI
X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme.
Judith A. Kelly,Judith A. Kelly,Anita R. Sielecki,Brian D. Sykes,Michael N.G. James,David Phillips +5 more
TL;DR: The X-ray structure of the non-hydrolysed13 trisaccharide NAM-NAG-NAM bound in subsites B, C, D is presented and it is shown that the interpretation of the 2.5-Å resolution difference map does not involve distortion of this residue in site D.
Journal ArticleDOI
Mechanism and stereoelectronic effects in the lysozyme reaction.
TL;DR: Lysozyme occupies a special place in the history of enzymology as the first enzyme to have its three-dimensional crystal structure elucidated by Phillips and co-workers in 1965, but discussion of the conformational question came to a head only very recently with the suggestion that the fundamental stereoelectronic requirements of the glycoside-cleavage reaction might be decisive.