Sacchettini J C, Frazier M W, Chiara D C, Banaszak L J, Grant G A
Department of Biological Chemistry, Washington University School of Medicine, St. Louis, Missouri 63110.
Biochem Biophys Res Commun. 1988 May 31;153(1):435-40. doi: 10.1016/s0006-291x(88)81243-9.
The complete amino acid sequence of porcine heart fumarase (EC 4.2.1.2) has been determined from peptides produced by cyanogen bromide, endoproteinase Arg-C, S. aureus V8 protease, and trypsin. The enzyme is a tetramer of identical subunits with Mr = 50,015 and composed of 466 amino acid residues. Porcine heart fumarase displays 96% identity to human liver fumarase. Prediction of the secondary structural elements of porcine fumarase indicate that the enzyme contains a large amount of alpha helix with very little beta structure.
