The structure/activity relationship in glyceraldehyde-3-phosphate dehydrogenase of pig muscle.
The macromolecular digestion product obtained on limited proteolysis of glyceraldehyde-3-phosphate dehydrogenase (GPDH, EC 1.2.1.12) was fractionated into seven polypeptides. Their position in the known sequence of GPDH was established. The sites of chymotrypsin action at Phe-34, Tyr-91, Val-116, Leu-154, Leu-221 and Leu-246 were identified on the basis of N-terminal sequence and molecular weight of the peptides isolated. Cleavage of particular peptide bonds was related to the enzymatic activity.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis; D013329:Structure-Activity Relationship; D013552:Swine
D000596:Amino Acids; D010446:Peptide Fragments; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases