My NCBI | Sign In
RSS Settings
  • Search:

Display Settings:

Format

Send to:

Choose Destination

    Biochem Biophys Res Commun. 1995 Jan 17;206(2):736-41.

    The identification of the pterin-binding domain in the nitric oxide synthase's sequence.

    Uvarov VYu, Lyashenko AA.

    Institute of biomedical chemistry, Moscow, Russia.

    Comparative studies of primary sequences of nitric oxide synthase (NOS) and pterin-dependent enzymes has shown that the biopterin-dependent site of NOS is localized between the regions responsible for calmodulin and FMN binding. On the example of NOS from rat brain it was demonstrated that this biopterin-binding site is located in the region 750-769. Pairwise alignment of amino acids sequences of NOS from rat brain and rat xantine dehydrogenase revealed that the two proteins are 39.7% identical.

    PMID: 7530005 [PubMed - indexed for MEDLINE]

    Publication Types, MeSH Terms, Substances

    Publication Types:

    MeSH Terms:

    Substances:

    LinkOut - more resources

    Full Text Sources:

    Supplemental Content

    Click here to read

    Related articles

    All links from this record

    • Related Articles

      Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.

    • Gene

      Gene records that cite the current articles. Citations in Gene are added manually by NCBI or imported from outside public resources.

    • HomoloGene

      HomoloGene clusters of homologous genes and sequences that cite the current articles. These are references on the Gene and sequence records in the HomoloGene entry.

    • Nucleotide

      Primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.

    • Nucleotide (RefSeq)

      NCBI nucleotide Reference Sequences (RefSeqs) that are cited in the current articles, included in the corresponding Gene Reference into Function, or that include the PubMed articles as references.

    • Nucleotide (Weighted)

      Nucleotide records associated with the current articles through the Gene database. These are the related sequences on the Gene record that are added manually by NCBI.

    • Protein (RefSeq)

      NCBI protein Reference Sequences (RefSeqs) that are cited in the current articles, included in the corresponding Gene Reference into Function, or that include the PubMed articles as references.

    • Protein (Weighted)

      Protein records associated with the current articles through related Gene database records. These are the related sequences on the Gene record that are added manually by NCBI.

    • Substance (MeSH Keyword)

      PubChem chemical substance (submitted) records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.

    • Taxonomy via GenBank

      Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).

    • UniGene

      UniGene clusters of expressed sequences that are associated with the current articles through references on the clustered sequence records and related Gene records.

    • Protein

      Protein translation features of primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.

    • GEO Profiles

      Gene Expression Omnibus (GEO) Profiles of molecular abundance data. The current articles are references on the Gene record associated with the GEO profile.

    Recent activity