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EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] active site 487772
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate 487772, 487774, 487779
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] cooperativity between acyl-CoA and peptide binding sites 487752
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] detailed mechanism 487779
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] Glu290, Val-291 and His293 within conserved region EEVEH, are essential for catalysis 487770
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] interactions between enzyme and acyl-CoA and peptide substrates, formation of a high affinity reaction intermediate 487750
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] kinetic analysis 487772, 487774
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] mechanism 487735, 487746, 487750
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] myristoyl-CoA binding site 487763, 487779
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.97tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein 703221
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