Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 435-440 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 153 |
| Issue number | 1 |
| DOIs | |
| State | Published - May 31 1988 |
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Sacchettini, J. C., Frazier, M. W., Chiara, D. C., Banaszak, L. J., & Grant, G. A. (1988). Amino acid sequence of porcine heart fumarase. Biochemical and Biophysical Research Communications, 153(1), 435-440. https://doi.org/10.1016/S0006-291X(88)81243-9