The sites of chymotrypsin action on the pig muscle glyceraldehyde 3-phosphate dehydrogenase during limited proteolysis.
1. The sites of chymotrypsin action on glyceraldehyde 3-phosphate dehydrogenase (D-glyceraldehyde 3-phosphate) : DNA+ oxidoreductase (phosphorylating), EC 1.2.1.12) was established; limited proteolysis by chymotrypsin results in lowering of the phosphorolytic activity of the enzyme without affecting its oxidative activity. 2. The low-molecular fraction of the chymotrypsin digest separated by Sephadex G-100 chromatography, was fractionated on Bio-gels. Determination of the amino acid composition of the nine peptides isolated, and of their amino acid sequence, permitted to relate cleavage of Leu-64, Trp-84, Leu-109, Leu-141, Phe-165, Lys-212, Val-239, Leu-242, Leu-271 (or Phe-315) bonds in the enzyme to the decrease of the phosphorolytic activity.
D000595:Amino Acid Sequence; D000818:Animals; D002918:Chymotrypsin / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D013379:Substrate Specificity; D013552:Swine
D010446:Peptide Fragments; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D002918:Chymotrypsin