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  2. Zinc carboxypeptidase - Wikipedia

    en.wikipedia.org/wiki/Zinc_carboxypeptidase

    The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A (digestive). [1] Members of the H family have longer C-termini than those of family A, [2] and carboxypeptidase M (a member of the H family) is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble.

  3. Carboxypeptidase A - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase_A

    Carboxypeptidase A (CPA) contains a zinc (Zn 2+) metal center in a tetrahedral geometry with amino acid residues in close proximity around zinc to facilitate catalysis and binding. Out of the 307 amino acids bonded in a peptide chain, the following amino acid residues are important for catalysis and binding; Glu-270, Arg-71, Arg-127, Asn-144 ...

  4. Carboxypeptidase - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase

    A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases , which cleave peptide bonds at the N-terminus of proteins.

  5. Glutamate carboxypeptidase II - Wikipedia

    en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II

    Research has also shown that small-molecule-based NP inhibitors are beneficial in animal models that are relevant to neurodegenerative diseases. [37] Some specific applications of this research include neuropathic and inflammatory pain, traumatic brain injury, ischemic stroke, schizophrenia, diabetic neuropathy, amyotrophic lateral sclerosis ...

  6. Zinc in biology - Wikipedia

    en.wikipedia.org/wiki/Zinc_in_biology

    Zinc fingers help read DNA sequences.. Zinc is an essential trace element for humans [1] [2] [3] and other animals, [4] for plants [5] and for microorganisms. [6] Zinc is required for the function of over 300 enzymes and 1000 transcription factors, [3] and is stored and transferred in metallothioneins.

  7. Lysine carboxypeptidase - Wikipedia

    en.wikipedia.org/wiki/Lysine_carboxypeptidase

    Lysine carboxypeptidase (EC 3.4.17.3) is an enzyme. [1] [2] [3] This enzyme catalyses the following chemical reaction: Release of a C-terminal basic amino acid (lysine or arginine), preferentially lysine. This is a zinc-activated enzyme found in plasma. It inactivates proteins such as bradykinin and anaphylatoxins in the blood in order to ...

  8. Peptidoglycan binding domain - Wikipedia

    en.wikipedia.org/wiki/Peptidoglycan_binding_domain

    Zinc-containing D-alanyl-D-alanine-cleaving carboxypeptidase, VanX. ... Several MMPs are implicated in cancer progression, since degradation of the extracellular ...

  9. Zinc finger and BTB domain-containing protein 16 - Wikipedia

    en.wikipedia.org/wiki/Zinc_finger_and_BTB_domain...

    This gene is a member of the Krueppel C2H2-type zinc-finger protein family and encodes a zinc finger transcription factor that contains nine Kruppel-type zinc finger domains at the carboxyl terminus. This protein is located in the nucleus, is involved in cell cycle progression, and interacts with a histone deacetylase .