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PMID: 7207627 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Common precursor of lysozymes of hen egg-white and bacteriophage T4.

Nature ·Vol. 290 ·No. 5804 ·1981-03-26 ·Pages 334-5

Matthews BW, Grütter MG, Anderson WF, Remington SJ

Abstract

The lysozymes of hen egg-white and bacteriophage T4 have similar catalytic properties but their amino acid sequences are not homologous. The question therefore arises whether they are derived from a common ancestral protein or have arisen independently. On the basis of the data we have gathered, it is shown here that the two enzymes are similar in the conformation of their backbones, in their modes of binding substrates, in specific protein--substrate interactions and in their presumed modes of action. We conclude that the two enzymes have diverged from a common precursor. This seems to be the most convincing example to date of the divergence of proteins with nonhomologous amino acid sequences.

MeSH Terms
Animals Base Sequence Binding Sites Biological Evolution Catalysis Chickens/genetics Genes Muramidase/genetics Protein Conformation Structure-Activity Relationship T-Phages/genetics
Chemicals
Muramidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Matthews B W
Grütter M G
Anderson W F
Remington S J
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1981-03-26
Pages
334-5
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
NIGMS NIH HHS · GM 05972 · United States
NIGMS NIH HHS · GM 20066 · United States
NIGMS NIH HHS · GM 21967 · United States
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