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PMID: 625331 Published · ppublish English Journal Article

Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution.

Nature ·Vol. 271 ·No. 5646 ·1978-02-16 ·Pages 626-30

Levine M, Muirhead H, Stammers DK, Stuart DI

Abstract

The structure determination of pyruvate kinase shows that each subunit of the tetrameric molecule consists of three domains. The largest of these domains has a remarkable similarity to the structure of triosephosphate isomerase. Another domain shows similarities to many other nucleotide binding proteins. We discuss these similarities and their implications for current arguments on protein taxonomy and evolution.

MeSH Terms
Animals Binding Sites Biological Evolution Cats Genes L-Lactate Dehydrogenase/genetics Muscles/enzymology Protein Conformation Pyruvate Kinase/genetics Structure-Activity Relationship Triose-Phosphate Isomerase/genetics X-Ray Diffraction
Chemicals
L-Lactate Dehydrogenase Pyruvate Kinase Triose-Phosphate Isomerase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Levine M
Muirhead H
Stammers D K
Stuart D I
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1978-02-16
Pages
626-30
Language
English
Region
England
NLM ID
0410462
Subset
IM
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