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Source: The Open Library

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1Cytochrome P-450 Dependent Biotransformation of Endogenous Substrates (Frontiers in Biotransformation)

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“Cytochrome P-450 Dependent Biotransformation of Endogenous Substrates (Frontiers in Biotransformation)” Metadata:

  • Title: ➤  Cytochrome P-450 Dependent Biotransformation of Endogenous Substrates (Frontiers in Biotransformation)
  • Author:
  • Language: English
  • Number of Pages: Median: 214
  • Publisher: Vch Pub
  • Publish Date:

“Cytochrome P-450 Dependent Biotransformation of Endogenous Substrates (Frontiers in Biotransformation)” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 1991
  • Is Full Text Available: Yes
  • Is The Book Public: No
  • Access Status: Printdisabled

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    2Stereospecificity in chemistry and biochemistry

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    “Stereospecificity in chemistry and biochemistry” Metadata:

    • Title: ➤  Stereospecificity in chemistry and biochemistry
    • Author:
    • Language: English
    • Number of Pages: Median: 255
    • Publisher: Robert A. Welch Foundation
    • Publish Date:
    • Publish Location: Houston, Tex

    “Stereospecificity in chemistry and biochemistry” Subjects and Themes:

    Edition Identifiers:

    • The Open Library ID: OL2448837M
    • Online Computer Library Center (OCLC) ID: 16870366
    • Library of Congress Control Number (LCCN): 87147520

    Access and General Info:

    • First Year Published: 1984
    • Is Full Text Available: No
    • Is The Book Public: No
    • Access Status: No_ebook

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    3Development and partial structural characterization of a recombinant inhibitor of pepsin from Ascaris

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    “Development and partial structural characterization of a recombinant inhibitor of pepsin from Ascaris” Metadata:

    • Title: ➤  Development and partial structural characterization of a recombinant inhibitor of pepsin from Ascaris
    • Author:
    • Language: English
    • Number of Pages: Median: 146
    • Publish Date:

    “Development and partial structural characterization of a recombinant inhibitor of pepsin from Ascaris” Subjects and Themes:

    Edition Identifiers:

    Access and General Info:

    • First Year Published: 1999
    • Is Full Text Available: Yes
    • Is The Book Public: Yes
    • Access Status: Public

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      4Detailed investigation into the enzymatic specificity of porcine pepsin

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      “Detailed investigation into the enzymatic specificity of porcine pepsin” Metadata:

      • Title: ➤  Detailed investigation into the enzymatic specificity of porcine pepsin
      • Author:
      • Language: English
      • Number of Pages: Median: 132
      • Publisher: Gainesville, FL
      • Publish Date:

      “Detailed investigation into the enzymatic specificity of porcine pepsin” Subjects and Themes:

      Edition Identifiers:

      Access and General Info:

      • First Year Published: 1994
      • Is Full Text Available: Yes
      • Is The Book Public: Yes
      • Access Status: Public

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        5Site-directed mutagenesis of the aspartic proteinase rhizopuspepsin

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        “Site-directed mutagenesis of the aspartic proteinase rhizopuspepsin” Metadata:

        • Title: ➤  Site-directed mutagenesis of the aspartic proteinase rhizopuspepsin
        • Author:
        • Language: English
        • Number of Pages: Median: 152
        • Publisher: Gainesville, FL
        • Publish Date:

        “Site-directed mutagenesis of the aspartic proteinase rhizopuspepsin” Subjects and Themes:

        Edition Identifiers:

        Access and General Info:

        • First Year Published: 1994
        • Is Full Text Available: Yes
        • Is The Book Public: Yes
        • Access Status: Public

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          Wiki

          Source: Wikipedia

          Wikipedia Results

          Search Results from Wikipedia

          Chemical specificity

          ligands. The fewer ligands a protein can bind, the greater its specificity. Specificity describes the strength of binding between a given protein and ligand

          Nonribosomal peptide

          computationally switch the specificities of A-domains. The condensation C-domain is also believed to have substrate specificity, especially if located behind

          Serine protease

          active site. These enzymes can be further categorised based on their substrate specificity as either trypsin-like, chymotrypsin-like or elastase-like. Trypsin-like

          Specificity constant

          different substrates (i.e., substrate specificity). The higher the specificity constant, the more the enzyme "prefers" that substrate. The following equation

          Lewis C. Cantley

          identify the substrate specificity of protein kinases toward synthetic peptides. This approach was then extended to characterize the specificity of Ser/Thr

          Caspase 3

          sequences on their substrates and hydrolyze peptide bonds after aspartic acid residues. Caspase 3 and caspase 7 share similar substrate specificity by recognizing

          Ascorbate peroxidase

          Raven EL (August 2003). "Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase

          Protein phosphatase

          strictly tyrosine-specific, and the DSPs (c) which target Ser/Thr as well as Tyr and are the most diverse in terms of substrate specificity. The third class

          Major facilitator superfamily

          substrate specificity is largely determined by specific side chains which line the aqueous pocket at the center of the membrane. While one substrate of

          D-octopine dehydrogenase

          complexity. Evolutionary modification in substrate specificity is seen most drastically in the amino acid substrate. OcDH from some sea anemones has been