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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2001-6-7
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:keyword |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
526-30
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11394913-Animals,
pubmed-meshheading:11394913-Binding Sites,
pubmed-meshheading:11394913-COS Cells,
pubmed-meshheading:11394913-Calcium,
pubmed-meshheading:11394913-Calmodulin,
pubmed-meshheading:11394913-Cations, Divalent,
pubmed-meshheading:11394913-Chelating Agents,
pubmed-meshheading:11394913-Egtazic Acid,
pubmed-meshheading:11394913-Enzyme Activation,
pubmed-meshheading:11394913-Nitric Oxide Synthase,
pubmed-meshheading:11394913-Nitric Oxide Synthase Type I,
pubmed-meshheading:11394913-Nitric Oxide Synthase Type II,
pubmed-meshheading:11394913-Point Mutation,
pubmed-meshheading:11394913-Recombinant Fusion Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Ca2+-independent activity of nitric oxide synthase.
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pubmed:affiliation |
Department of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9040, USA. slee@resgen.com
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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