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Results 1 - 10 of 175 > >>
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EC Number Inhibitors Commentary Structure
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228more fragments of S-adenosyl-L-methionine, adenosine and methionine, are selectively inhibitory of TrmD, while they are poor inhibitors for Trm5 from Methanocaldococcus jannaschii Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228more fragments of S-adenosyl-L-methionine, adenosine and methionine, are poor inhibitors of Trm5, while they are selectve inhibitors for TrmD from Escherichia coli Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228more high-throughput small-molecule library inhibitor screening, antibacterial growth inhibitory activities and haemolytic activity of selected TrmD inhibitors, binding affinity confirmed by thermal stability and surface plasmon resonance, overview Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228more the N-terminal domain is a useful construct to probe the molecular interactions with SAM competitive inhibitors, in the search for molecules with antibiotic activity Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228more development of inhibitors against Mycobacterium abscessus tRNA (m1G37) methyltransferase (TrmD) using fragment-based approaches, inhibitor screening, overview. Determination of inhibitor thermodynamics and binding kinetics Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228more synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, overview. The tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228more synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, nanomolar potency against TrmD in vitro, overview. This tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA. Biochemical structure-activity relationships (SAR) for TrmD inhibitors, the thienopyrimidinone substituent flexibility is critical for potent TrmD inhibition. Analysis of hemolytic activity of the compounds. Effect of side chain length of 15 analogues Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228S-adenosyl-L-homocysteine an S-adenosyl-L-methionine analogue Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228KCl the enzyme is most active in absence of KCl Go to the Ligand Summary Page
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.228KCl TRM5 enzyme is stimulated 4fold by 100 mM KCl. TRM5 tends to lose all activity in 600 mM KCl Go to the Ligand Summary Page
Results 1 - 10 of 175 > >>
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