Amino acid substitutions far from the active site of bacteriophage T4 lysozyme reduce catalytic activity and suggest that the C-terminal Lobe of the enzyme participates in substrate binding
- 31 January 1982
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 154 (3) , 525-535
- https://doi.org/10.1016/s0022-2836(82)80011-9
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: Implications for the mechanism of catalysisJournal of Molecular Biology, 1981
- Low‐Molecular‐Weight Substrate for the Lysozyme of T4 BacteriophageEuropean Journal of Biochemistry, 1979
- The Specificity Requirements of Bacteriophage T4 LysozymeEuropean Journal of Biochemistry, 1976
- Structural patterns in globular proteinsNature, 1976
- Untersuchungen über PhagenlysozymMolecular Genetics and Genomics, 1974
- The amino acid substitution tyrosine 88 → histidine in the lysozyme of phage T4: The molecular cause of the cold-sensitive phenotype of the mutantcseBU56FEBS Letters, 1974
- A Three‐Dimensional Atomic Model of the Murein Layer of BacteriaEuropean Journal of Biochemistry, 1974
- Crystallographic data for lysozyme from bacteriophage T4Journal of Molecular Biology, 1973
- A computer controlled film scanner for X-ray crystallographyJournal of Physics E: Scientific Instruments, 1972
- Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism.Microbiology and Molecular Biology Reviews, 1968