Home LiteratureArticle Details

PMID: 7077670 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

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.

Journal of molecular biology ·Vol. 154 ·No. 3 ·1982-01-25 ·Pages 525-35

Grütter MG, Matthews BW

Abstract

暂无摘要

MeSH Terms

Amino Acid Sequence Amino Acids/analysis Binding Sites Drug Stability Kinetics Models, Molecular Muramidase/genetics,metabolism Mutation Protein Conformation T-Phages/enzymology,genetics X-Ray Diffraction

Chemicals

Amino Acids Muramidase

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Grütter M G

Matthews B W

Article Info

Journal

Journal of molecular biology

Abbr.

J Mol Biol

ISSN

0022-2836

DOI

10.1016/s0022-2836(82)80011-9

Published

1982-01-25

Pages

525-35

Language

English

Region

England

NLM ID

2985088R

Subset

Grants

NIGMS NIH HHS · GM20066 · United States

NIGMS NIH HHS · GM21967 · United States

External Links

PubMed source DOI: 10.1016/s0022-2836(82)80011-9 View journal details

Analysis Services

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.

Contact

WeChat Official Account