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Titolo:
Ca2+-independent activity of nitric oxide synthase
Autore:
Lee, SJ; Beckingham, K; Stull, JT;
Indirizzi:
Univ Texas, SW Med Ctr, Dept Physiol, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 ed Ctr, Dept Physiol, Dallas, TX 75390 USA Rice Univ, Dept Biochem & Cell Biol, Houston, TX 77005 USA Rice Univ Houston TX USA 77005 Biochem & Cell Biol, Houston, TX 77005 USA
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 2, volume: 284, anno: 2001,
pagine: 526 - 530
SICI:
0006-291X(20010608)284:2<526:CAONOS>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
BINDING-SITE MUTANTS; CALCIUM-BINDING; POINT MUTATIONS; CA2+ BINDING; 2 SERIES; ELECTRON-TRANSFER; TARGET PEPTIDES; CALMODULIN; DOMAIN; ACTIVATION;
Keywords:
Ca2+-independent activity; calcium; calmodulin; chimera; mutation; nitric-oxide synthase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Lee, SJ Res Genet Inc, Invitrogen Corp, ResGen, Dept Res & Dev, 2130 Mem Pkwy,2nd Floor,2700 Bldg, Huntsville, AL 35801 USA Res Genet Inc 2130 Mem Pkwy,2nd Floor,2700 Bldg Huntsville AL USA 35801
Citazione:
S.J. Lee et al., "Ca2+-independent activity of nitric oxide synthase", BIOC BIOP R, 284(2), 2001, pp. 526-530

Abstract

Ca2+-independent forms of nitric-oxide synthase have significant activity when the endogenous calmodulin subunit is Ca2+ free, Further activation is seen when Ca2+ is added. We have examined the activation of a Ca2+-independent nitric-oxide synthase variant and its two point mutants that are more dependent on Ca2+ for activation using mutant calmodulins containing non-functional Ca2+-binding sites. These studies provide evidence that the Ca2+ independent activity of these enzymes can be exerted through specific adaptedinteractions between the enzyme and the Ca2+-binding site 2 of calmodulin,Further, the results suggest that EGTA-sensitive metals other than Ca2+ complexed to calmodulin may be involved in maximal activation of these nitric-oxide synthase variants. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 01:13:27