When.com Web Search

  1. Ad

    related to: carboxypeptidase of zinc and cancer

Search results

  1. Results From The WOW.Com Content Network
  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. CPA4 (gene) - Wikipedia

    en.wikipedia.org/wiki/CPA4_(gene)

    Carboxypeptidases are zinc-containing exopeptidases that catalyze the release of carboxy-terminal amino acids, and are synthesized as zymogens that are activated by proteolytic cleavage. This gene could be involved in the histone hyperacetylation pathway. It is imprinted and may be a strong candidate gene for prostate cancer aggressiveness. [6]

  4. 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 ...

  5. 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.

  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. Glutamate carboxypeptidase II - Wikipedia

    en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II

    GCPII is a zinc metalloenzyme that resides in membranes. Most of the enzyme resides in the extracellular space. GCPII is a class II membrane glycoprotein. It catalyzes the hydrolysis of N-acetylaspartylglutamate (NAAG) to glutamate and N-acetylaspartate (NAA) according to the reaction scheme to the right. [7] [8]

  8. AZGP1 - Wikipedia

    en.wikipedia.org/wiki/AZGP1

    AZGP1, also referred to as zinc-alpha-2-glycoprotein (ZAG), is a glycoprotein with a molecular weight of 38-40 kDa. [6] In 1961, AZGP1 was initially isolated from normal human plasma and named as ZAG due to its distinctive electrophoretic mobility within the alpha-2 region and its ability to bind to zinc. [ 6 ]

  9. ZNF839 - Wikipedia

    en.wikipedia.org/wiki/ZNF839

    ZNF839 or zinc finger protein 839 is a protein which in humans is encoded by the ZNF839 gene. It is located on the long arm of chromosome 14. [5] Zinc finger protein 839 is speculated to play a role in humoral immune response to cancer as a renal carcinoma antigen (NY-REN-50). This is because NY-REN-50 was found to be over expressed in cancer ...