MUTATION OF LYS-120 AND LYS-134 DRASTICALLY REDUCES THE CATALYTIC RATE OF CU,ZN SUPEROXIDE-DISMUTASE

被引：24
|
作者：
POLTICELLI, F
BATTISTONI, A
BOTTARO, G
CARRI, MT
ONEILL, P
DESIDERI, A
ROTILIO, G
机构：
[1] MRC, RADIOBIOL UNIT, DIDCOT OX11 0RD, OXON, ENGLAND
[2] UNIV ROMA TOR VERGATA, DEPT BIOL, I-00133 ROME, ITALY
[3] UNIV MESSINA, DEPT ORGAN & BIOL CHEM, I-98100 MESSINA, ITALY
来源：
FEBS LETTERS | 1994年 / 352卷 / 01期
关键词：
SUPEROXIDE DISMUTASE; SITE-DIRECTED MUTAGENESIS; PULSE RADIOLYSIS; BROWNIAN DYNAMICS; ELECTROSTATIC INTERACTION;
D O I：
10.1016/0014-5793(94)00885-X
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：76 / 78
页数：3
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