Phosphomethylpyrimidine kinase inhibitor

images phosphomethylpyrimidine kinase inhibitor

Kim, Y. Nodwell, M. Arabidopsis thaliana. This linker region and a flexible N-terminal extension occupy the interface between the ThiD-like and TenA-like dimers. A relatively flexible linker region composed of a loop and a short helix joins the two domains. Search UniProt Accession: Search. Thi20p is involved in thiamine synthesis from pyrithiamin and oxythiamin. Enzyme Structure. SCOPe 4jjp. Please wait a moment until all data is loaded.

  • 4Amino5Hydroxymethyl2Methylpyrimidine DrugBank
  • BRENDA Information on EC hydroxymethylpyrimidine kinase
  • BRENDA Information on EC phosphooxymethylpyrimidine kinase

  • PubMed · articles · NCBI · proteins.

    4Amino5Hydroxymethyl2Methylpyrimidine DrugBank

    In enzymology, a phosphomethylpyrimidine kinase (EC ) is an enzyme that catalyzes the chemical reaction. Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal. 4-aminohydroxymethylmethyl pyrimidine kinase, 4-aminohydroxymethyl- 2-methylpyrimidine (phosphate) kinase.
    Reddick, J. Escherichia coli.

    Molecular Properties. Rapala-Kozik, M.

    images phosphomethylpyrimidine kinase inhibitor

    Onozuka, M.

    images phosphomethylpyrimidine kinase inhibitor
    Brookhaven national labs brookhaven ny
    Please make sure you have JavaScript enabled in your browser settings. Saccharomyces cerevisiae QSaccharomyces cerevisiae.

    BRENDA Information on EC hydroxymethylpyrimidine kinase

    InterPro database of protein families, domains and functional sites. GeneOntology No. GeneOntology No. Please make sure you have JavaScript enabled in your browser settings.

    Information on EC - phosphomethylpyrimidine kinase.

    P. lactone isolated from Cryptocarya rugulosa, covalent inhibition.

    BRENDA Information on EC phosphooxymethylpyrimidine kinase

    The uncompetitive inhibition of TMP synthase by ATP was analysed from the . for the phosphomethylpyrimidine kinase/thiamin-phosphate. UHydroxymethylpyrimidine/phosphomethylpyrimidine kinase, Not Available, Salmonella typhimurium (strain LT2 / SGSC / ATCC ).
    SCOPe 2i5b.

    Please wait a moment until the data is sorted. GeneOntology No. Substrate pyridoxal is 8-times less preferred than the phosphorylation of hydroxymethyl pyrimidine by the last ancestor. Kim, Y.

    images phosphomethylpyrimidine kinase inhibitor

    Rapala-Kozik, M.

    images phosphomethylpyrimidine kinase inhibitor
    KARINAS GOLF TOURNAMENT
    Thiamine metabolism.

    Thiamine metabolism. Release See terms of use. Salmonella enterica subsp.

    The three genes encode hydroxyethylthiazole kinase, hydroxymethylpyrimidine ( HMP) kinase and phosphomethylpyrimidine (HMP-P) kinase, respectively. ), phosphomethylpyrimidine kinase (EC ), hydroxyethylthiazole known to be a specific inhibitor of thiamine biosynthesis in microorganisms (12). kinase (EC ), phosphomethylpyrimidine kinase (EC.

    ).

    Video: Phosphomethylpyrimidine kinase inhibitor Use of VEGF-Targeted Tyrosine Kinase Inhibitors

    analog that inhibits the growth of this species, and the inhibition is relieved competitively.
    SCOPe 4jjp. CATH 1jxi.

    images phosphomethylpyrimidine kinase inhibitor

    Search Reference ID: Search. Search Reference ID: Search. ATPaminomethyl phosphooxymethyl pyrimidine phosphotransferase. Saccharomyces cerevisiae QSaccharomyces cerevisiae.

    images phosphomethylpyrimidine kinase inhibitor
    28 DAVITA RD BURLINGTON MA MOVIE
    Arabidopsis thaliana.

    This message will disappear when all data is loaded. Staphylococcus aureus. Brassica napus.

    Functional Parameters. Thiamine metabolism. Overexpression, purification and characterization of two pyrimidine kinases involved in the biosynthesis of thiamin: 4-aminohydroxymethylmethylpyrimidine kinase and 4-aminohydroxymethylmethylpyrimidine phosphate kinase.

    3 Replies to “Phosphomethylpyrimidine kinase inhibitor”
    1. The structure reveals an overall dimeric organization in which N-terminal domains and C-terminal domains form ThiD-like and TenA-like local dimers.