2.1.1.228 additional information - additional information binding kinetics of TrmD ligands 757409 2.1.1.228 additional information - additional information kinetic analysis of tRNA truncation mutants and tRNA mutant with alterations in the anticodon loop reveals that TrmD and Trm5 exhibit separate and distinct mode of tRNA recognition, suggesting that they evolved by independent and nonoverlapping pathways from their unrelated AdoMet families 712739 2.1.1.228 additional information - additional information kinetics and thermodynamics analysis, overview. Steady-state kinetics with S-adenosyl-L-methionine (SAM) and tRNALeu(GAG) show that PaTrmD catalyzes the two-substrate reaction by way of a ternary-complex, while isothermal titration calorimetry revealed that SAM and tRNALeu(GAG) bind to PaTrmD independently, each with a dissociation constant of 0.014 mM 758329 2.1.1.228 additional information - additional information KM-values for truncated tRNAPhe variants 673850 2.1.1.228 additional information - additional information measurement of the pre-steady-state rate constant of methyl transfer of TrmD, a proton abstraction step is rate limiting, steady-state kinetics 735927 2.1.1.228 additional information - additional information Michaelis-Menten kinetic analysis 756161 2.1.1.228 additional information - additional information Michaelis-Menten steady-state kinetics analysis 736428 2.1.1.228 additional information - additional information pre-steady-state and steady-state kinetic analysis of wild-type and mutant enzymes, the rate-determining step is product release from the enzyme, kinetic isotope effect, overview 737226 2.1.1.228 additional information - additional information pre-steady-state and steady-state kinetics, rapid burst phase followed by a slower and linear phase in reaction, single-turnover and from steady-state analysis, overview 720240 2.1.1.228 additional information - additional information pre-steady-state and steady-state kinetics, time-dependent linear reaction, overview. TrmD exhibits half-of-the-sites reactivity in which only one of the two active sites is functional at a given time 720240