• Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. (wikipedia.org)
  • Compound 7a exhibits improved potencies against both the trypanosomal AdoMetDC enzyme and parasites, and better blood brain barrier penetration than 1. (elsevierpure.com)
  • S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein. (wikipedia.org)
  • MGBG, a structural analog of spermidine, was proven to competitively inhibit AdoMetDC and decrease intracellular degrees of both spermidine and spermine [49]. (researchensemble.com)
  • Although MGBG became too toxic for even more clinical development, additional inhibitors of AdoMetDC had been developed and examined for their capability to considerably decrease spermidine and spermine amounts without significant off-target results, including mitochondrial toxicity. (researchensemble.com)
  • Focusing on AdoMetDC Furthermore to focusing on the 1st rate-limiting part of polyamine biosynthesis, effective attempts have already been made in focusing on the next rate-limiting stage, AdoMetDC. (researchensemble.com)
  • Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. (wikipedia.org)
  • To test this hypothesis, we sought to identify candidate AdoMetDC/SpeD homologs encoding L-ornithine and L-arginine decarboxylases in bacteria and archaea. (bvsalud.org)
  • Phylogenetic analysis indicated that L-arginine decarboxylases emerged at least three times from AdoMetDC/SpeD, whereas L-ornithine decarboxylases arose only once, potentially from the AdoMetDC/SpeD-derived L-arginine decarboxylases, revealing unsuspected polyamine metabolic plasticity. (bvsalud.org)
  • We identified fusion proteins of bona fide AdoMetDC/SpeD with homologous L-ornithine decarboxylases that possess two, unprecedented internal protein-derived pyruvoyl cofactors. (bvsalud.org)
  • Autocatalytic self-processing of the AdoMetDC/SpeD proenzyme generates a pyruvoyl cofactor from an internal serine. (bvsalud.org)
  • In the presence of the AdoMetDC inhibitor, ODC activity and the intracellular pool of putrescine were enhanced, whereas the spermidine and spermine pools were decreased. (cnrs.fr)
  • Recently, we discovered that diverse bacteriophages encode AdoMetDC/SpeD homologs that lack AdoMetDC activity and instead decarboxylate L-ornithine or L-arginine. (bvsalud.org)
  • We searched for the anomalous presence of AdoMetDC/SpeD homologs in the absence of its obligatory partner enzyme spermidine synthase, or the presence of two AdoMetDC/SpeD homologs encoded in the same genome. (bvsalud.org)
  • 2. Adenovirus-mediated expression of both antisense ODC and AdoMetDC inhibited colorectal cancer cell growth in vitro. (nih.gov)
  • 16. [Inhibitory effects of ODC and AdoMetDC bi-antisense virus on the growth and invasion of lung cancer cell A-549]. (nih.gov)