Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution.
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.
D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D002415:Cats; D005796:Genes; D007770:L-Lactate Dehydrogenase / Q000235:genetics; D009132:Muscles / Q000201:enzymology; D011487:Protein Conformation; D011770:Pyruvate Kinase / Q000235:genetics; D013329:Structure-Activity Relationship; D014305:Triose-Phosphate Isomerase / Q000235:genetics; D014961:X-Ray Diffraction
D007770:L-Lactate Dehydrogenase; D011770:Pyruvate Kinase; D014305:Triose-Phosphate Isomerase