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Results 1 - 10 of 79 > >>
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
-999
-
more
binding kinetics of TrmD ligands
-999
-
more
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
-999
-
more
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
-999
-
more
KM-values for truncated tRNAPhe variants
-999
-
more
measurement of the pre-steady-state rate constant of methyl transfer of TrmD, a proton abstraction step is rate limiting, steady-state kinetics
-999
-
more
Michaelis-Menten kinetic analysis
-999
-
more
Michaelis-Menten steady-state kinetics analysis
-999
-
more
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
-999
-
more
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
-999
-
more
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
Results 1 - 10 of 79 > >>