Pub. Date : 1991 Dec 10
PMID : 1660723
2 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The double charge, aspartic acid to lysine, point mutations were constructed at positions 37, 79, and 217 on the surface of cytochrome c peroxidase, sites purported to be within or proximal to the recognition site for cytochrome c in an electron-transfer productive complex formed by the two proteins. | Aspartic Acid | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 2 | The double charge, aspartic acid to lysine, point mutations were constructed at positions 37, 79, and 217 on the surface of cytochrome c peroxidase, sites purported to be within or proximal to the recognition site for cytochrome c in an electron-transfer productive complex formed by the two proteins. | Lysine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |