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 been investigated by pulse radiolysis. Results obtained demonstrate that both residues decrease the catalytic rate by about 40%, in partial disagreement with previous brownian dynamics calculations, carried out on bovine Cu,Zn superoxide dismutase.
Polticelli, F., Battistoni, A., Bottaro, G., Carri, M.t., Oneill, P., Desideri, A., et al. (1994). MUTATION OF LYS-120 AND LYS-134 DRASTICALLY REDUCES THE CATALYTIC RATE OF CU,ZN SUPEROXIDE-DISMUTASE RID A-4573-2009. FEBS LETTERS, 352(1), 76-78 [10.1016/0014-5793(94)00885-X WC Biochemistry & Molecular Biology; Biophysics; Cell Biology].
MUTATION OF LYS-120 AND LYS-134 DRASTICALLY REDUCES THE CATALYTIC RATE OF CU,ZN SUPEROXIDE-DISMUTASE RID A-4573-2009
POLTICELLI, Fabio;
1994-01-01
Abstract
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 been investigated by pulse radiolysis. Results obtained demonstrate that both residues decrease the catalytic rate by about 40%, in partial disagreement with previous brownian dynamics calculations, carried out on bovine Cu,Zn superoxide dismutase.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
