Amino acid sequence of rabbit muscle aldolase and the structure of the active center.
Elucidation of the amino acid sequence of fructose-1,6-bis-phosphate aldolase from rabbit muscle has made it possible to assign the positions of the functional groups known to play specific roles in the catalytic activity, and also to locate the buried, exposed, and active site cysteine residues. The results indicate that the middle portion of the polypeptide chain, including Cys-134, Cys-149, Cys-177, and Cys-l99, is buried in the native structure, with regions containing Cys-72, Lys-107, Lys-227, Cys-336, His-359, and the COOH-terminal residue (Tyr-361) folded into the active center of the enzyme, at or near the surface of the enzyme molecule.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005634:Fructose-Bisphosphate Aldolase / Q000032:analysis* / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D011487:Protein Conformation; D011817:Rabbits
D005634:Fructose-Bisphosphate Aldolase