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  2. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site.

  3. Adenosine deaminase - Wikipedia

    en.wikipedia.org/wiki/Adenosine_deaminase

    The ADA active site contains a zinc ion, which is located in the deepest recess of the active site and coordinated by five atoms from His15, His17, His214, Asp295, and the substrate. Zinc is the only cofactor necessary for activity. The substrate, adenosine, is stabilized and bound to the active site by nine hydrogen bonds.

  4. ADARB1 - Wikipedia

    en.wikipedia.org/wiki/ADARB1

    1ZY7, 5ED1, 5ED2, 5HP3, 5HP2. Identifiers. Aliases. ADARB1, ADAR2, DRABA2, DRADA2, RED1, adenosine deaminase, RNA specific B1, adenosine deaminase RNA specific B1, NEDHYMS. External IDs. OMIM: 601218; MGI: 891999; HomoloGene: 8280; GeneCards: ADARB1; OMA: ADARB1 - orthologs. EC number.

  5. RNA editing - Wikipedia

    en.wikipedia.org/wiki/RNA_editing

    The adenosine deaminase of E. coli cannot deaminate a nucleoside in the RNA; the enzyme's reaction pocket is too small for the RNA strand to bind to. However, this active site is widened by amino acid changes in the corresponding human analog genes, APOBEC1 and ADAR, allowing deamination.

  6. Adenosine deaminase z-alpha domain - Wikipedia

    en.wikipedia.org/wiki/Adenosine_deaminase_z...

    This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA-editing enzyme. The z-alpha domain is a Z-DNA binding domain, and binding of this region to B-DNA has been shown to be disfavoured by steric hindrance.

  7. 5-HT2C receptor - Wikipedia

    en.wikipedia.org/wiki/5-HT2C_receptor

    There are three members of the ADAR family ADARs 1–3 with ADAR1 and ADAR2 being the only enzymatically active members. ADAR3 is thought to have a regulatory role in the brain. ADAR1 and ADAR2 are widely expressed in tissues while ADAR3 is restricted to the brain.

  8. IGFBP7 - Wikipedia

    en.wikipedia.org/wiki/IGFBP7

    IGFBP7. Insulin-like growth factor-binding protein 7 is a protein that in humans is encoded by the IGFBP7 gene. [5] [6] [7] The major function of the protein is the regulation of availability of insulin-like growth factors (IGFs) in tissue as well as in modulating IGF binding to its receptors. IGFBP7 binds to IGF with low affinity compared to ...

  9. LEAPER gene editing - Wikipedia

    en.wikipedia.org/wiki/LEAPER_gene_editing

    A-to-I editing is catalyzed by adenosine deaminase acting on RNA (ADAR) enzymes, whose substrates are double-stranded RNAs. Three human ADAR genes have been identified with ADAR1 (official symbol ADAR) and ADAR2 (ADARB1) proteins developed activity profiles.

  10. CYFIP2 - Wikipedia

    en.wikipedia.org/wiki/CYFIP2

    There are three members of the ADAR family ADARs 1-3 with ADAR1 and ADAR2 being the only enzymatically active members. ADAR3 is thought to have a regulatory role in the brain. ADAR1 and ADAR 2 are widely expressed in tissues while ADAR3 is restricted to the brain.

  11. Kv1.1 - Wikipedia

    en.wikipedia.org/wiki/Kv1.1

    Kv1.1. Potassium voltage-gated channel subfamily A member 1 also known as Kv1.1 is a shaker related voltage-gated potassium channel that in humans is encoded by the KCNA1 gene. [5] [6] [7] Isaacs syndrome is a result of an autoimmune reaction against the K v 1.1 ion channel. [8]