Three-dimensional structural resemblance between leucine aminopeptidase and carboxypeptidase A revealed by graph-theoretical techniques.
Using 3-D searching techniques based on algorithms derived from graph theory we have established a striking structural similarity between the structure of bovine carboxypeptidase A and that of the C-terminal domain of bovine leucine aminopeptidase. There is no significant sequence homology between the aminopeptidases and the carboxypeptidases but the strong structural relationship detected in this complex fold suggests that there may be a very remote divergent evolutionary relationship between these two enzyme classes.
Artymiuk
P J
PJ
Krebs Institute for Biomolecular Research, The University, Sheffield, UK.
Grindley
H M
HM
Park
J E
JE
Rice
D W
DW
Willett
P
P
D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D002268:Carboxypeptidases / Q000378:metabolism*; D043422:Carboxypeptidases A; D002417:Cattle; D003198:Computer Simulation; D007931:Leucyl Aminopeptidase / Q000378:metabolism*; D011487:Protein Conformation
D002268:Carboxypeptidases; D007931:Leucyl Aminopeptidase; D043422:Carboxypeptidases A