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

共 32 条

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[22] MOTOR-NEURON DEGENERATION IN MICE THAT EXPRESS A HUMAN CU,ZN SUPEROXIDE-DISMUTASE MUTATION (VOL 264, PG 1772, 1994)
GURNEY, ME
SCIENCE, 1995, 269 (5221) : 149 - 149
[23] A HOMOZYGOUS MUTATION DETECTED IN EXON-4 OF THE CU,ZN SUPEROXIDE-DISMUTASE GENE ASSOCIATED WITH FAMILIAL AMYOTROPHIC-LATERAL-SCLEROSIS
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AMERICAN JOURNAL OF HUMAN GENETICS, 1995, 57 (04) : 1912 - 1912
[24] A novel missense point mutation (S134N) of the Cu/Zn superoxide dismutase gene in a patient with familial amyotrophic lateral sclerosis
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AMYOTROPHIC LATERAL SCLEROSIS: PROGRESS AND PERSPECTIVES IN BASIC RESEARCH AND CLINICAL APPLICATION, 1996, 1104 : 289 - 292
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HUMAN MUTATION, 1997, 9 (01) : 69 - 71
[26] EVOLUTIONARY CONSERVATIVENESS OF ELECTRIC-FIELD IN THE CU,ZN SUPEROXIDE-DISMUTASE ACTIVE-SITE - EVIDENCE FOR COORDINATED MUTATION OF CHARGED AMINO-ACID-RESIDUES
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[27] A KINETIC-STUDY OF THE REACTIONS BETWEEN H2O2 AND CU,ZN SUPEROXIDE-DISMUTASE - EVIDENCE FOR AN ELECTROSTATIC CONTROL OF THE REACTION-RATE
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[28] IDENTIFICATION OF A NEW MISSENSE POINT MUTATION IN EXON-4 OF THE CU/ZN SUPEROXIDE-DISMUTASE (SOD-1) GENE IN A FAMILY WITH AMYOTROPHIC-LATERAL-SCLEROSIS
ELSHAFEY, A
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HUMAN MOLECULAR GENETICS, 1994, 3 (02) : 363 - 364
[29] FAMILIAL AMYOTROPHIC-LATERAL-SCLEROSIS (ALS) IN JAPAN ASSOCIATED WITH H46R MUTATION IN CU/ZN SUPEROXIDE-DISMUTASE GENE - A POSSIBLE NEW SUBTYPE OF FAMILIAL ALS
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JOURNAL OF THE NEUROLOGICAL SCIENCES, 1994, 126 (01) : 77 - 83
[30] MUTATION OF THE METAL-BRIDGING PROTON-DONOR HIS63 RESIDUE IN HUMAN CU, ZN SUPEROXIDE-DISMUTASE - BIOCHEMICAL AND BIOPHYSICAL ANALYSIS OF THE HIS63-]CYS MUTANT
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