Primary structure of yeast cytochrome c peroxidase. II. The complete amino acid sequence |
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| Authors: | K Takio K Titani L H Ericsson T Yonetani |
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| Affiliation: | 1. Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA;2. Howard Hughes Medical Institute Laboratory at Department of Biochemistry, University of Washington, Seattle, Washington 98195 USA;3. Department of Biochemistry, University of Washington, Seattle, Washington 98195 USA |
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| Abstract: | The complete amino acid sequence of 293 residues in the single polypeptide chain of yeast cytochrome c peroxidase has been determined. Sequence analyses were performed on fragments obtained by cleavage with cyanogen bromide and by tryptic digestion of citraconylated protein. These fragments were aligned with sequential and compositional data as well as those obtained with intact protein, tryptic, and chymotryptic peptides (Takio and Yonetani, 1980, Arch. Biochem. Biophys.203, 605–614). Residues critical for catalysis by the enzyme were identified as arginine 48, tryptophan 51, histidine 52, and histidine 174 by fitting the sequence to the electron density map derived by others. Sequence comparison with other proteins show limited homology with horseradish peroxidase and myoglobin. |
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