Superoxide-dependent peroxidase activity of H48Q: a superoxide dismutase variant associated with familial amyotrophic lateral sclerosis.
Arch Biochem Biophys
; 346(2): 263-8, 1997 Oct 15.
Article
em En
| MEDLINE
| ID: mdl-9343373
ABSTRACT
Approximately 20% of cases of familial amyotrophic lateral sclerosis are caused by dominant mutations in the Cu,Zn superoxide dismutase. One such mutant, in which histidine #48 has been replaced by glutamine (H48Q), exhibits a novel activity. It can react sequentially with O2- and H2O2 to generate a potent oxidant at its active site, possibly Cu(II)-OH, which then can oxidize urate to the corresponding radical. This O2- -dependent peroxidase activity exerted on a substrate peculiar to motor neurons may be the toxic gain of function which leads to the deleterious consequences of this mutation. G93A, G93R, and E100G were also examined and found not to exert this O2- -dependent peroxidase activity.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Superóxido Dismutase
/
Superóxidos
/
Esclerose Lateral Amiotrófica
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Revista:
Arch Biochem Biophys
Ano de publicação:
1997
Tipo de documento:
Article
País de afiliação:
Estados Unidos