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  • Crystal Structure of an ATP-Dependent DNA Ligase from Bacteriophage T7
    This lysine residue is part of a conserved KxDG motif which is the same as that found at the active site of DNA and RNA ligases (Lindahl and Barnes 1992) Furthermore, there are several other motifs that are also conserved between DNA ligases, RNA ligases, and tRNA ligases, with a similar spacing between them (Shuman and Schwer 1995)
  • Bacteriophage T7 DNA Ligase - Journal of Biological Chemistry
    These capping enzymes contain a similar active site motif to DNA ligase (K X DG), and replacement of the active site lysine with alanine was shown to be lethal (43), in common with a number of RNA and DNA ligases (10, 12)
  • ATP-Dependent DNA Ligase (Bacteriophage T7) - proteopedia. org
    Finally, T7 ligase creates the phosphodiester bond between the 5' -phosphoryl and the 3' – hydroxyl group, with AMP being freed [4] All ATP-dependent DNA ligases contain a conserved amino acid sequence of [3] This includes the lysine residue which binds the ATP in the groove between the two domains
  • Location of the active site for enzyme-adenylate formation in DNA ligases.
    The ATP-dependent DNA ligases of mammalian cells, fission yeast, budding yeast, vaccinia virus, and bacteriophages T3, T4, and T7 contain the active site motif Lys-Tyr Ala-Asp-Gly- (Xaa)-Arg, with the reactive lysine residue flanked by hydrophobic amino acids
  • M-CSA Mechanism and Catalytic Site Atlas - EMBL-EBI
    DNA ligase (ATP) DNA ligase is an essential enzyme required for the repair, replication and recombination of DNA In all organisms except the prokaryotes it is dependent on the hydrolysis of ATP to AMP and pyrophosphate
  • Closing the gap on DNA ligase: Structure - Cell Press
    The ATP-dependent ligases and GTP-dependent capping enzymes make up a superfamily of covalent nucleotidyl transferases [4] This assertion is based on several lines of evidence: mapping the adenylylation or guanylylation site of several ligases and capping enzymes to a lysine residue within a universally conserved KxDG element (motif I in Figure 1); the identification of five other sequence
  • T7 DNA Ligase - NEB
    T7 DNA Ligase is an ATP-dependent dsDNA ligase that catalyzes phosphodiester bond formation and cohesive end ligation and nick sealing
  • Closing the gap on DNA ligase - ScienceDirect
    The ATP-dependent ligases and GTP-dependent capping enzymes make up a superfamily of covalent nucleotidyl transferases [4] This assertion is based on several lines of evidence: mapping the adenylylation or guanylylation site of several ligases and capping enzymes to a lysine residue within a universally conserved KxDG element (motif I in Figure 1); the identification of five other sequence
  • Characterization of proteolytic fragments of bacteriophage T7 DNA ligase.
    The N-terminal 16 kDa region of the intact T7 ligase is labelled selectively in the presence of [alpha-32P]ATP, confirming that it contains the active site lysine residue In common with the intact enzyme, the C-terminal portion of the protein retains the ability to band shift DNA fragments of various lengths, implicating it in DNA binding
  • Functional domains of an ATP-dependent DNA ligase
    The T7 enzyme represents one of the smallest known DNA ligases, and sequence similarity with other ligases shows that it corresponds to the highly conserved C-terminal region, with only a 33 amino acid N-terminal extension beyond the active site lysine (Kletzin, 1992)





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