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KCl
TRM5 enzyme is stimulated 4fold by 100 mM KCl. TRM5 tends to lose all activity in 600 mM KCl
Ca2+
can substitute Mg2+ to lesser extent
Ca2+
-
can partially substitute for Mg2+
Ca2+
can substitute Mg2+ to lesser extent
Ca2+
can substitute Mg2+ to lesser extent
Ca2+
can substitute Mg2+ to lesser extent
Ca2+
-
divalent cation (in oder of decreasing efficiency: Mg2+, Mn2+, Ca2+) required, optimal activity in presence of 10 mM Mg2+
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Mg2+
totally inactive without Mg2+
Mg2+
-
dependent on, one Mg2+ per enzyme dimer. Mg2+ is not involved in substrate binding, but in promoting methyl transfer. Mg2+ promotes methyl transfer of TrmD not by stabilizing the binding of tRNA or AdoMet, but by accelerating the chemical rate. Mg2+ interacts with the O6 of G37-tRNA
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Mg2+
required, one PaTrmD monomer can bind to one Mg2+ ion. Mg2+ ion does not bind tightly to PaTrmD
Mg2+
methyl transfer by TrmD requires Mg2+ in the catalytic mechanism, kinetics
Mg2+
required, cells expressing the native trmD show more than a 6fold activation of transcription upon switching from high to low Mg2+ media, whereas cells expressing a S88L mutant trmD show less than a 2fold activation. For cells expressing the native trmD, the level of Mg2+ modulates the level of TrmD-dependent m1G37-tRNA synthesis, which in turn modulates the speed of ribosomal translation of m1G37-dependent codons in the 5'-leader ORF. At high Mg2+, TrmD is active and the abundantly synthesized m1G37-tRNA facilitates ribosomal translation through the 5'-leader ORF
Mg2+
-
divalent cation (in oder of decreasig efficiency: Mg2+, Mn2+, Ca2+) required, optimal activity in presence of 10 mM Mg2+
Mn2+
-
can partially substitute for Mg2+
Mn2+
-
divalent cation (in oder of decreasing efficiency: Mg2+, Mn2+, Ca2+) required, optimal activity in presence of 10 mM Mg2+
Ni2+
can substitute Mg2+ to lesser extent
Ni2+
can substitute Mg2+ to lesser extent
Ni2+
can substitute Mg2+ to lesser extent
Ni2+
can substitute Mg2+ to lesser extent
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
additional information
-
bacterial enzyme TrmD is strongly dependent on divalent metal ions and Mg2+ is the most physiologically relevant. Divalent metal ions are recruited to stabilize the developing negative charge at the 6-position of G37, while also favoring the abstraction of the N1 proton to activate the nucleophile. Co2+ is unable to substitute for Mg2+, replacement of Mg2+ with Co2+ decreases methyl transfer, substitution of the 6-oxygen (O6) of G37 with 6-thio (S6) in the substrate tRNA restores the activity. Kinetics of metal ions in the reaction,overview
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
additional information
no absolute requirement for Mg2+
additional information
-
no absolute requirement for Mg2+
additional information
it is reported that TrmD-catalyzed methyl transfer from SAM to the N1 atom of G37 from the tRNA is strongly dependent on the presence of divalent metal ions, with Mg2+ as the most physiologically relevant
additional information
-
it is reported that TrmD-catalyzed methyl transfer from SAM to the N1 atom of G37 from the tRNA is strongly dependent on the presence of divalent metal ions, with Mg2+ as the most physiologically relevant
additional information
in addition to Mg2+, TrmD can also use Ca2+ and Mn2+ as an active ion, but not Ni2+ or Co2+. The single Mg2+ required for methyl transfer is involved in the abstraction of the N1 proton from G37-tRNA, which is likely the rate-limiting step of the TrmD-catalyzed methyl transfer
additional information
-
no activity is observed in absence of divalent cation or ion presence of Co2+. TrmD activity increases only 10% in the presence of a monovalent cation, indicating the nonessential nature of this factor
2.1.1.228 tRNA (guanine37-N1)-methyltransferase
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