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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.


Journal article



Publication Date





626 - 630


Animals, Binding Sites, Biological Evolution, Cats, Genes, L-Lactate Dehydrogenase, Muscles, Protein Conformation, Pyruvate Kinase, Structure-Activity Relationship, Triose-Phosphate Isomerase, X-Ray Diffraction