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

页码：76 / 78

页数：3

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