Article
Mutation of Lys-120 and Lys-134 drastically reduces the catalytic rate of Cu,Zn superoxide dismutase.
FEBS letters - 19 Sept 1994
Polticelli F, Battistoni A, Bottaro G, Carrì M T, O'Neill P, Desideri A, Rotilio G
Abstract excerpt
Lys-120 and Lys-134, located at the edge of the active site channel in most Cu,Zn superoxide dismutases, have been suggested to play a major role in steering the anionic substrate towards the catalytic copper ion. In this study, mutants of Xenopus laevis Cu,Zn superoxide dismutase have been engineered, with Lys-120 and Lys-134 changed into leucine and threonine, respectively, and their catalytic properties have...
Topics
- Animals
- Binding Sites
- Catalysis
- Copper
- Kinetics
- Lysine
- Mutation
- Osmolar Concentration
- Pulse Radiolysis
- Recombinant Fusion Proteins
- Superoxide Dismutase