Limited proteolysis of liver aldolase and fructose 1,6-bisphosphatase by lysosomal proteinases: effect on complex formation.
Cathepsin M, which catalyzes inactivation of both rabbit liver fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) and rabbit liver fructose 1,6-bisphosphatase (Fru-P2ase; EC 3.1.3.11), has been characterized as a peptidyl peptidase. Modification of the COOH terminus of aldolase by cathepsin M or by Fru-P2ase converting enzyme 2 abolishes its ability to bind to phosphocellulose P11 and to form the complex with Fru-P2ase. On the other hand, modification of the COOH terminus of Fru-P2ase does not affect its interaction with aldolase. This property is lost, however, when Fru-P2ase is modified in the NH2-terminal region by the converting enzyme or by subtilisin. The results suggest that interaction of aldolase and Fru-P2ase may involve the exposed COOH-terminal region of the former and an exposed proteinase-sensitive region located between residues 57 and 67 of the latter.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D013381:Subtilisins / Q000378:metabolism
D000596:Amino Acids; D006597:Fructose-Bisphosphatase; D002403:Cathepsins; D010447:Peptide Hydrolases; D013381:Subtilisins; C034114:cathepsin M; D005634:Fructose-Bisphosphate Aldolase