• Lysine carboxypeptidase is also known as: carboxypeptidase N arginine carboxypeptidase kininase I anaphylatoxin inactivator plasma carboxypeptidase B creatine kinase conversion factor bradykinase kininase Ia hippuryllysine hydrolase bradykinin-decomposing enzyme protaminase CPase N creatinine kinase convertase peptidyl-L-lysine(-L-arginine) hydrolase CPN All enzymes are assigned an Enzyme Commission number based on the chemical reaction they catalyze. (wikipedia.org)
  • To examine the role of water penetration, we have measured the 17O and 2H magnetic relaxation dis- persions (MRD) for the V66E and V66K mutants of staphylococcal nuclease, where glutamic acid and lysine residues are buried in predominantly apolar environments. (lu.se)
  • Histone methylation at lysine (K) residues continues to be connected with gene activation (e.g. (tam-receptor.com)
  • NSD2, a Histone Methyltransferase catalyzing di-methylation of histone H3 at lysine 36, has been proved a critical molecule in proliferation, metastasis, and tumorigenesis. (medchemexpress.com)
  • This enzyme catalyses the following chemical reaction: Release of a C-terminal basic amino acid (lysine or arginine), preferentially lysine. (wikipedia.org)
  • Furthermore, when recombinant proteins are fused to the AviTag and incubated with purified BirA, they can be bi-otinylated efficiently around the central lysine residue in the AviTag (16, 17). (biotechnologyconsultinggroup.com)
  • A carboxypeptidase that removes C-terminal lysine or arginine from peptides and proteins. (bvsalud.org)
  • We are studying a thrombin-activatable carboxypeptidase that plays a key role in the physiologic regulation of thrombin 's pro-thrombotic and pro-inflammatory properties. (stanford.edu)
  • The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. (genetex.com)
  • A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. (bvsalud.org)
  • Trypsin digestion of these yielded sets of peptides, in each of which the carboxyl-terminal fragment could be identified by the absence of lysine or arginine, or by the presence of homoserine. (nih.gov)
  • 2. HDAC1 regulates the stability of glutamate carboxypeptidase II protein by modulating acetylation status of lysine 479 residue. (nih.gov)
  • We isolated and structure elucidated PLA3-6, an anabaenopeptin-like cyclic peptide from the marine sponge Theonella swinhoei, harboring a three-residue(L-Phe, L-Ile, D-Lys)13-membered lactam ring formed by cyclization between the C-terminal acid and the ε-amine of an N-terminal lysine residue. (nih.gov)
  • DAP12 is responsible for SIRP beta 2 signaling, and is recruited through a single, positive lysine residue in the transmembrane domain of SIRP beta 2. (medchemexpress.com)
  • The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. (nih.gov)
  • Serum samples from three patients with documented exposure to S. chartarum similarly revealed lysine-, cysteine-, and histidine-SG adducts after exhaustive digestion, affinity column enrichment, and MS analysis. (nih.gov)
  • 9. Amino acids at the N- and C-termini of human glutamate carboxypeptidase II are required for enzymatic activity and proper folding. (nih.gov)
  • Qian, Y.M., Varlamov, O. and Fricker, L.D. Glu 300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway. (enzyme-database.org)
  • 1. Acetylation regulates the stability of glutamate carboxypeptidase II protein in human astrocytes. (nih.gov)
  • Lysine acetylation is a major post-translational modification that plays a key role in many physiological processes and is believed to have a broad spectrumof modulatory functions within the cell. (cas.cz)
  • Recombinant protein encompassing a sequence within the center region of human Carboxypeptidase M. The exact sequence is proprietary. (genetex.com)
  • Carboxypeptidase M antibody [N1C2] detects Carboxypeptidase M protein by western blot analysis. (genetex.com)
  • The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. (nih.gov)
  • Probe Set ID Ref Seq Protein ID Signal Strength Name Gene Symbol Species Function Swiss-Prot ID Amino Acid Sequence 1367452_at NP_598278 7.9 small ubiquitin-related modifier 2 precursor Sumo2 Rattus norvegicus " Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. (nih.gov)
  • and Lys-49 PLA2s (K49 PLA2s), which have a lysine substitutes at position 49 and very low or no hydrolytic activity towards artificial phospholipid substrates [4,5]. (technuc.com)
  • Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. (nih.gov)
  • Several enzymes from the lysine-biosynthesis pathway of have been structurally characterized. (tam-receptor.com)
  • Structural and mechanistic studies of the homoserine dehydrogenase enzyme acquire significance in the context of l-lysine biosynthesis owing to the role of this enzyme in the synthesis of l-homoserine. (tam-receptor.com)
  • We are studying a thrombin-activatable carboxypeptidase that plays a key role in the physiologic regulation of thrombin 's pro-thrombotic and pro-inflammatory properties. (stanford.edu)
  • Recent studies found that mast cells can be activated by snake venom and release carboxypeptidase A and possibly other proteases, which can degrade venom components [21,22]. (technuc.com)