Sites of cleavage of rabbit muscle aldolase by purified cathepsin M from rabbit liver.
Rabbit liver cathepsin M, a sulfhydryl proteinase similar in catalytic properties to cathepsin B, causes a decrease in the activity of rabbit muscle aldolase assayed with fructose 1,6-bisphosphate but not with fructose 1-phosphate. Proteolytic modification of aldolase by cathepsin M is limited to the removal of small peptides from the COOH-terminus, including the COOH-terminal hexapeptide NH2-Ile-Ser-Asn-His-Ala-TyrOH. Correlation of loss of aldolase activity with COOH-terminal modification indicates that only three of the four subunits of muscle aldolase contribute to the catalytic activity of the tetrameric enzyme.
S
S
Erickson-Viitanen
E
E
Balestreri
M
M
McDermott
B L
BL
Horecker
D000818:Animals; D002403:Cathepsins / Q000302:isolation & purification / Q000494:pharmacology*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D008247:Lysosomes / Q000201:enzymology; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis / Q000378:metabolism; D011817:Rabbits; D013379:Substrate Specificity
D010446:Peptide Fragments; D002403:Cathepsins; C034114:cathepsin M; D005634:Fructose-Bisphosphate Aldolase