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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.

Type

Journal article

Journal

Nature

Publication Date

16/02/1978

Volume

271

Pages

626 - 630

Keywords

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