Primary structure of a cationic Cu,Zn Superoxide dismutase
- 20 October 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 207 (1), 7-10
- https://doi.org/10.1016/0014-5793(86)80003-5
Abstract
The complete amino acid sequence of Cu,Zn Superoxide dismutase from sheep erythrocytes has been determined. The sequence is very similar to that of the bovine enzyme, having the same number of residues (151) and only two substitutions in the ‘hypervariable’ region (residues 17–30). The 5 overall substitutions confer a positive charge on the sheep enzyme at neutral pH (pI≈8). This charge is localized outside the active site region. The catalytic efficiency of the sheep enzyme is 15% less than that of the cow enzyme, confirming the hypothesis that the enzyme activity is related to the concentration of positive surface charge near the active site channel.Keywords
This publication has 8 references indexed in Scilit:
- Separation of phenylthiohydantoin-amino acids by high-performance liquid chromatography and some applications in dansyl Edman sequence analysisJournal of Chromatography A, 1985
- Primary structure of porcine Cu,Zn Superoxide dismutaseFEBS Letters, 1985
- The primary structure of human liver manganese superoxide dismutase.Journal of Biological Chemistry, 1984
- A study of the pH dependence of the activity of porcine Cu,Zn superoxide dismutaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Electrostatic recognition between superoxide and copper, zinc superoxide dismutaseNature, 1983
- The complete amino acid sequence of human Cu/Zn superoxide dismutaseFEBS Letters, 1980
- Polarographic determination of superoxide dismutaseAnalytical Biochemistry, 1975
- Strategy and tactics in protein chemistryBiochemical Journal, 1970