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  • cofactor
  • Initially PLP cofactor is bound to the active-site lysine via a Schiff base to form the holo-form or internal aldimine of the enzyme. (wikipedia.org)
  • Studies of the isoform of the enzyme found in the Gram-negative bacterium S. paucimobilis were the first to elucidate the structure of the enzyme, revealing that PLP cofactor is held in place by several active site residues including Lys265 and His159. (wikipedia.org)
  • Molybdenum is bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants, is the active compound at the catalytic site of all molybdenum-containing enzymes in nature, except bacterial molybdenum nitrogenase. (nih.gov)
  • mitochondria
  • When this energetic capacity is harnessed by mitochondria in eukaryotic cells, the energy flux supported by a given genome size increases by a factor of ∼8,000 ( 3 ), potentially paving the way for increased complexity at the cellular level (but see ref. 4 ). (pnas.org)
  • catalytic
  • The active site of LCB2 contains lysine and other key catalytic residues that are not present in LCB1, which does not participate in catalysis but is nevertheless required for the synthesis and stability of the enzyme. (wikipedia.org)
  • In Escherichia coli, Lys-193, Lys-194, Cys-195, His-197, and His-356 are thought to be catalytic residues, while His-184 is thought to be involved in the assembly of the tetrameric enzyme. (wikipedia.org)
  • amino
  • The aromatic amino acid transaminases, Aro8p and Aro9p and the branched chain amino acid transaminases, Bat1p and Bat2p, seemed to be the main enzymes exhibiting the MOB transaminase activity. (chalmers.se)
  • Comparison of 26 cytosolic malate dehydrogenase (cMDH) orthologs of marine molluscs adapted to temperatures ranging from −1.9 °C (Antarctica) to ∼55 °C (South China coast) shows how amino acid usage in different regions of the enzyme varies with adaptation temperature. (pnas.org)
  • To link the effects of specific amino acid substitutions with adaptive variations in enzyme thermal stability, we combined site-directed mutagenesis (SDM) and in vitro protein experimentation with in silico mutagenesis using molecular dynamics simulation (MDS) techniques. (pnas.org)
  • MDS analysis is shown to provide insights into how specific amino acid substitutions affect the conformational flexibilities of mobile regions (MRs) of the enzyme that are essential for binding and catalysis. (pnas.org)
  • These additional amino acids account for the difference in molecular mass: the prokaryotic ICL is 48kDa, while the eukaryotic ICL is 67 kDa. (wikipedia.org)
  • These acids and bases are amino acid side chains in the active site of the enzyme. (wikipedia.org)
  • cysteine residue
  • In enzymes of the sulfite oxidase family, X is represented by a single-bonded sulfur provided by a cysteine residue of the respective protein, whereas Y corresponds to a double-bonded oxygen. (nih.gov)
  • Cells
  • A long-standing and pervasive view is that there have been intimate mechanistic links between the evolution of complex life on Earth-in other words, the emergence and ecological expansion of eukaryotic cells and their aggregation into multicellular organisms-and the secular evolution of ocean−atmosphere oxygen levels ( 1 ). (pnas.org)
  • hydrolyse
  • Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family. (genome.jp)
  • whereas
  • In enzymes of the xanthine oxidase family, X is represented by a double-bonded inorganic sulfur, whereas Y corresponds to a hydroxyl group. (nih.gov)
  • coli
  • In comparing C. glutamicum and E. coli, monomer and dimer, respectively, both enzymes were found to "efficiently catalyze identical reactions. (wikipedia.org)
  • oxidative
  • Time-course effects of antioxidants and phase II enzymes on diesel exhaust particles-induced oxidative damage in the mouse lung. (bioportfolio.com)
  • Copper-caused oxidative stress triggers the activation of antioxidant enzymes via ZmMPK3 in maize leaves. (bioportfolio.com)