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Substitution of arginine for lysine 134 alters electrostatic parameters of the active site in shark Cu,Zn superoxide dismutase
Author(s) -
Calabrese Lilia,
Polticelli Fabio,
O'Neill Peter,
Galtieri Antonio,
Barra Donatella,
Schininà Eugenia,
Bossa Francesco
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80682-9
Subject(s) - superoxide dismutase , chemistry , active site , enzyme , lysine , arginine , copper , biochemistry , amino acid , stereochemistry , organic chemistry
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 O − 2 to the catalytically active copper. This change may be related to observed alterations of electrostatic parameters of the enzyme (p K of the pH dependence of the enzyme activity, rate of inactivation by H 2 O 2 ), although it preserves a high efficiency of dismutation at neutral pH.