My NCBI | Sign In
RSS Settings
  • Search:

Display Settings:

Format

Send to:

Choose Destination

    Science. 1995 Jun 2;268(5215):1312-8.

    Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.

    Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL.

    Fred Hutchinson Cancer Research Center, Program in Structural Biology, Seattle, WA 98104, USA.

    Erratum in:

    • Science 1995 Oct 20;270(5235):365.

    Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.

    PMID: 7761851 [PubMed - indexed for MEDLINE]

    Publication Types, MeSH Terms, Substances, Grant Support

    Publication Types:

    MeSH Terms:

    Substances:

    Grant Support:

    LinkOut - more resources

    Full Text Sources:

    Other Literature Sources:

    Molecular Biology Databases:

    Supplemental Content

    Click here to read

    Related articles

    Cited by 10 PubMed Central articles

    Structures reported by this article

    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.

    • Compound (MeSH Keyword)

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

    • Gene

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

    • 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.

    • Protein Clusters

      Clusters of related proteins from the Protein Clusters database that cite the current articles. Sources of references in Protein Clusters include the associated Gene and Conserved Domain records as well as NCBI added citations.

    • 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).

    • 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.

    • Structure

      Three-dimensional structure records in the NCBI Structure database for data reported in the current articles.

    • 3D Domains

      Structural domains in the NCBI Structure database that are parts of the 3D structures reported in the current articles.

    • 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.

    • Cited in PMC

      Full-text articles in the PubMed Central Database that cite the current articles.

    Recent activity