PMID: 2500367Jun 19, 1989Paper

Substitution of arginine for lysine 134 alters electrostatic parameters of the active site in shark Cu,Zn superoxide dismutase

FEBS Letters
L CalabreseF Bossa

Abstract

The complete amino acid sequence was determined for the Cu,Zn superoxide dismutase from the shark Prionace glauca. The active site region shows the substitution of an Arg for Lys at position 134, which is important for electrostatic facilitation of the diffusion of O2- to the catalytically active copper. This change may be related to observed alterations of electrostatic parameters of the enzyme (pK of the pH dependence of the enzyme activity, rate of inactivation by H2O2), although it preserves a high efficiency of dismutation at neutral pH.

References

Jul 8, 1985·FEBS Letters·M E SchininàG Rotilio
Apr 1, 1974·The Biochemical Journal·R C BrayL Calabrese
Nov 15, 1983·Biochemical and Biophysical Research Communications·H J Fuchs, C L Borders

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Citations

Jan 1, 1991·Free Radical Research Communications·J KwiatowskiF J Ayala
Jan 1, 1991·Free Radical Research Communications·L CalabreseG Musci
Jul 1, 1997·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·C CapoA Desideri
Jun 10, 2006·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·Gianfranco SantovitoEster Piccinni
Sep 4, 2003·Journal of Agricultural and Food Chemistry·Chuian-Fu KenChi-Tsai Lin
Feb 7, 2002·Journal of Agricultural and Food Chemistry·Chuian-Fu KenChi-Tsai Lin

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