Ca2+-independent activity of nitric oxide synthase

Shiow Ju Lee, Kathy Beckingham, James T. Stull

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 adapted interactions 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.

Original languageEnglish (US)
Pages (from-to)526-530
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume284
Issue number2
DOIs
StatePublished - 2001

Fingerprint

Calmodulin
Nitric Oxide Synthase
Chemical activation
Binding Sites
Egtazic Acid
Enzymes
Metals

Keywords

  • Ca-independent activity
  • Calcium
  • Calmodulin
  • Chimera
  • Mutation
  • Nitric-oxide synthase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Ca2+-independent activity of nitric oxide synthase. / Lee, Shiow Ju; Beckingham, Kathy; Stull, James T.

In: Biochemical and Biophysical Research Communications, Vol. 284, No. 2, 2001, p. 526-530.

Research output: Contribution to journalArticle

Lee, Shiow Ju ; Beckingham, Kathy ; Stull, James T. / Ca2+-independent activity of nitric oxide synthase. In: Biochemical and Biophysical Research Communications. 2001 ; Vol. 284, No. 2. pp. 526-530.
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