Pancreatic lipases: evolutionary intermediates in a positional change of catalytic carboxylates?
Comparison of the fold of lipases from Geotrichum candidum and from human pancreas identified a high degree of similarity which was not expected on the basis of their amino acid sequences. Although both enzymes utilize a serine protease-like catalytic triad, they differ in the topological position of the acid. We speculate that these proteins are evolutionarily related and that the pancreatic lipase is an evolutionary intermediate in the pathway of migration of the catalytic acid to a new position within the fold.
Schrag
J D
JD
Biotechnology Research Institute, National Research Council of Canada, Montréal, Québec.
Winkler
F K
FK
Cygler
M
M
D000595:Amino Acid Sequence; D005075:Biological Evolution; D002264:Carboxylic Acids / Q000378:metabolism; D002384:Catalysis; D004583:Electrons; D005848:Geotrichum / Q000201:enzymology; D006801:Humans; D008071:Lipoprotein Lipase / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology*; D011487:Protein Conformation; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
D002264:Carboxylic Acids; D008071:Lipoprotein Lipase