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-Reference-Cited by-同舟云学术

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

Published:1982-01 Issue:3 Volume:154 Page:525-535
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Grütter M.G.,Matthews B.W.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference26 articles.

1. Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: Implications for the mechanism of catalysis

2. Low-Molecular-Weight Substrate for the Lysozyme of T4 Bacteriophage

3. A Three-Dimensional Atomic Model of the Murein Layer of Bacteria

Cited by 55 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Monomodular Pseudomonas aeruginosa phage JG004 lysozyme (Pae87) contains a bacterial surface-active antimicrobial peptide-like region and a possible substrate-binding subdomain;Acta Crystallographica Section D Structural Biology;2022-03-04

2. Monomodular Pseudomonas aeruginosa phage JG004 lysozyme (Pae87) contains a bacterial surface-active antimicrobial peptide-like region and a possible substrate-binding subdomain;2022-01-10

3. Different Single-Enzyme Conformational Dynamics upon Binding Hydrolyzable or Nonhydrolyzable Ligands;The Journal of Physical Chemistry B;2021-05-26

4. The structure of DLP12 endolysin exhibiting alternate loop conformation and comparative analysis with other endolysins;Proteins: Structure, Function, and Bioinformatics;2017-12-01

5. Probing the Aggregation Mechanism of Gold Nanoparticles Triggered by a Globular Protein;The Journal of Physical Chemistry C;2017-01-05