On the conservation of protein sequences in evolution.
The amino acid sequences of enzymes like alcohol dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase are strongly conserved across all phyla. We suggest that the amino acid conservation of such enzymes might be a result of the fact that they function as part of a multi-enzyme complex. The specific interactions between the proteins involved would hinder evolutionary change of their surfaces.
Kisters-Woike
B
B
Institut für Genetik der Universität zu Köln, Weyertal 121, D-50931 Köln, Germany. b.kisters@uni-koeln.de
Vangierdegom
C
C
Müller-Hill
B
B
D000426:Alcohol Dehydrogenase / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D017124:Conserved Sequence; D018076:DNA, Complementary / Q000378:metabolism; D004798:Enzymes / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins; D019143:Evolution, Molecular; D018014:Gene Transfer Techniques; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry; D006801:Humans; D056968:Lac Repressors; D008958:Models, Molecular; D012097:Repressor Proteins / Q000737:chemistry
D001426:Bacterial Proteins; D018076:DNA, Complementary; D004798:Enzymes; D029968:Escherichia coli Proteins; D056968:Lac Repressors; C539064:LacI protein, E coli; C065825:PurR protein, Bacteria; C489317:PurR protein, E coli; D012097:Repressor Proteins; D000426:Alcohol Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases