Crystallographic studies of the activity of hen egg-white lysozyme

@article{Blake1967CrystallographicSO,
  title={Crystallographic studies of the activity of hen egg-white lysozyme},
  author={Colin C. F. Blake and Louise N. Johnson and Gerald Mair and A. C. North and David Chilton Phillips and V. R. Sarma},
  journal={Proceedings of the Royal Society of London. Series B. Biological Sciences},
  year={1967},
  volume={167},
  pages={378 - 388}
}
  • C. Blake, L. N. Johnson, V. R. Sarma
  • Published 18 April 1967
  • Chemistry, Biology
  • Proceedings of the Royal Society of London. Series B. Biological Sciences
The chemical evidence for the enzymic activity of lysozyme will be discussed in detail by other speakers at this meeting, but in order to describe our crystallographic studies of the interactions between the enzyme and its substrates it is necessary to summarize briefly what was known about them at the beginning of our work. Simultaneously with his discovery of lysozyme Fleming (1922) discovered a Gram-positive species of bacteria, Micrococcus lysodeikticus, which is particularly susceptible to… 
Chemical Evidence for the Phillips Model of the Action of Hen Egg White Lysozyme
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A THREE-dimensional model of the ES-complex formed between a chito-oligosaccharide and hen egg white lyso-zyme was presented and it was reported that partially O-carboxymethylated chitin was highly susceptible to the action of lysozyme.
ROLE OF THE LYSINE, TYROSINE AND TRYPTOPHAN RESIDUES IN THE ACTIVITY OF MILK LYSOZYMES
TLDR
The crystallographic studies of Blake et al. (1965, 1967) and Phillips (1967) have confirmed the involvement of tryptophan residues 62 and 63 as well as tryPTophan 108 in the substrate binding of EWL.
Histidine-114 at Subsites E and F Can Explain the Characteristic Enzymatic Activity of Guinea Hen Egg-white Lysozyme
The courses of the reaction catalyzed by guinea hen egg-white lysozyme (GHL), in which Asn113 and Arg114 at subsites E and F in hen egg-white lysozyme (HEL) are replaced by Lys and His, respectively,
Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes.
TLDR
The crystal structure of the enzyme in which all tryptophan residues have been replaced by aza-tryptophan has been solved by X-ray crystallography at 2.3 A using a combination of multiple isomorphous replacement, non-crystallographic symmetry averaging and density modification techniques.
Lysozyme: a model enzyme in protein crystallography.
TLDR
The binding of substrate analogues, transition state mimics and oligosaccharide products of hydrolysis to HEWL, GEWL and T4L have contributed greatly to the understanding of sugar binding to proteins.
Activity of crystalline turkey egg white lysozyme
TLDR
It has been shown that turkey egg white lysozyme is enzymatically active in the crystal and the reduced radiolabeled oligosaccharide has a unique cleavage pattern with trisaccharides as the products.
A Covalent Enzyme-Substrate Adduct in a Mutant Hen Egg White Lysozyme (D52E)*
TLDR
It is suggested that the catalytic mechanism of D52E mutant lysozyme proceeds through a covalent enzyme-substrate intermediate indicating a different catalytic mechanisms from the wild type hen egg white lyso enzyme.
Crystal structures of K33 mutant hen lysozymes with enhanced activities.
TLDR
The results suggest that the enhancement of activity in K33N mutant lysozyme was due to an alteration in the orientation of the side chain of N37, which may have helped Lysozyme acquire the conformational stability at position 33.
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