2.1.1.228: tRNA (guanine37-N1)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (guanine37-N1)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.228
-
2.1.1.228
-
methyltransferases
-
anticodon
-
adomet
-
1-methylguanosine
-
drug development
-
n2-guanine
-
trmt10a
-
1-methyladenine
-
adomet-dependent
-
5-methyluridine
-
trmfo
-
n1-methylation
-
methyl-deficient
-
7-methylguanine
-
spout
-
epitranscriptome
-
nsun2-mediated
-
medicine
- 2.1.1.228
- methyltransferases
-
anticodon
- adomet
- 1-methylguanosine
- drug development
-
n2-guanine
- trmt10a
- 1-methyladenine
-
adomet-dependent
- 5-methyluridine
- trmfo
-
n1-methylation
-
methyl-deficient
- 7-methylguanine
-
spout
-
epitranscriptome
-
nsun2-mediated
- medicine
Reaction
Synonyms
At3g56120, aTrm5a methyltransferase, aTrm5a/Taw22-like enzyme, AtTrm5a, bacterial tRNA (guanine37-N1)-methyltransferase, bacterial tRNA-(N1G37) methyltransferase, EC 2.1.1.31, EcTrmD, HiTrmD, HsTrm5, m1G37 tRNA methyltransferase, m1G37-forming tRNA methyltransferase, Mj-Trm5, MJ0883, MjTrm5, MjTrm5b, mono-functional methyltransferase, More, MtbTrmD, NEQ228, PA14_15990, PAB2272, PAB_RS03940, PaTrm5a, PaTrm5b, PaTrmD, SaTrmD, Ta0997, TAW22, transfer RNA (m1G37) methyltransferase, Trm1, TRM5, Trm5a, Trm5a/Taw22-like enzyme, trm5b, Trm5p, TrmD, TRMT5, tRNA (guanine(37)-N1)-methyltransferase 1, tRNA (guanine37-N1)-methyltransferase, tRNA (guanosine-1) methyltransferase, tRNA (m1G37) methyltransferase, tRNA (m1G37)-methyltransferase, tRNA m1G37 methyltransferase, tRNA methyltransferase, tRNA methyltransferase 5, tRNA methyltransferase D, tRNA(m(1)G37)methyltransferase, tRNA(m1G37) methyltransferase, tRNA(m1G37) MTase, tRNA(m1G37)methyltransferase, tRNA-(N1G37) methyltransferase, tRNAPhe:imG2 methyltransferase
ECTree
2.1.1.228 tRNA (guanine37-N1)-methyltransferaseAdvanced search results
results (
results (KM Value
KM Value on EC 2.1.1.228 - tRNA (guanine37-N1)-methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.018
guanine37 in human mitochondrial tRNAPro possessing an A36G37 sequence
pH 8.0, 37°C
-
0.00028
guanine37 in Methanocaldococcus jannaschii tRNA(Cys)
pH 8.0, 50°C
-
0.027
guanine37 in tRNAArg
-
pH 8.0, temperature not specified in the publication
-
0.0027
guanine37 in tRNAGlnG36A
-
pH 8.0, temperature not specified in the publication
-
0.184
guanine37 in tRNAGlnG36C
-
pH 8.0, temperature not specified in the publication
-
0.114
guanine37 in tRNAGlnG36U
-
pH 8.0, temperature not specified in the publication
-
0.0012
guanine37 in tRNALeu(CAG)
pH and temperature not specified in the publication
-
0.0008
guanine37 in tRNALeu(GAG)
pH 7.5, 37°C, recombinant enzyme
-
0.001
guanine37 in tRNAPro
-
pH 8.0, temperature not specified in the publication
-
0.000075
guanine37 in yeast tRNAAsp possessing a C36G37 sequence
pH 8.0, 37°C
-
0.00058
guanine37 in yeast tRNAAsp possessing an U36G37 sequence
pH 8.0, 37°C
-
0.0000457
guanine37 in yeast tRNAPhe possessing an A36G37 sequence
pH 8.0, 37°C
-
0.00123
inosine37 in yeast tRNAAsp possessing a G36I37 sequence
below 0.00123 pH 8.0, 37°C
-
0.0007
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, wild-type enzyme
-
0.0025
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme Y176A
-
0.003
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme D223A
-
0.003
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme P226A
-
0.0043
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme R144A
-
0.0046
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme G205A/G207A
-
0.006
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme P267A
-
0.0072
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme N225A
-
0.0083
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme N265A
-
0.0012
guanine37 in Methanocaldococcus jannaschii tRNAPro
pH 8.0, 52°C
-
0.00082
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.0044
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.064
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.067
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.0024
guanine37 in tRNALeu
recombinant wild-type enzyme, pH 8.0, 30°C
-
0.0031
guanine37 in tRNALeu
recombinant wild-type enzyme, pH 8.0, 37°C
-
0.008
guanine37 in tRNALeu
-
pH 8.0, temperature not specified in the publication
-
0.0217
guanine37 in tRNALeu
recombinant wild-type enzyme, pH 8.0, 43°C
-
0.000244
guanine37 in yeast tRNAAsp possessing a G36G37 sequence
pH 8.0, 37°C
-
0.019
guanine37 in yeast tRNAAsp possessing a G36G37 sequence
pH 8.0, 37°C
-
0.00059
guanine37 in yeast tRNAAsp possessing an A36G37 sequence
pH 8.0, 37°C
-
0.046
guanine37 in yeast tRNAAsp possessing an A36G37 sequence
pH 8.0, 37°C
-
0.0005
S-adenosyl-L-methionine
pH 8.0, 50°C, mutant enzyme P267A
0.001
S-adenosyl-L-methionine
pH 8.0, 50°C, wild-type enzyme
0.0018
S-adenosyl-L-methionine
pH and temperature not specified in the publication
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
-
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
-
additional information
additional information
-
KM-values for truncated tRNAPhe variants
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
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
-
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
-
additional information
additional information
-
S-adenosyl-L-methionine and adenosine binding kinetics and kinetic analysis of enzyme reaction, overview
-
additional information
additional information
-
S-adenosyl-L-methionine and adenosine binding kinetics and kinetic analysis of enzyme reaction, overview
-
additional information
additional information
-
single turnover kinetics and thermodynamic analysis of effect of different guanosine analogues on m1G37-tRNA synthesis, kinetic analysis, overview
-
additional information
additional information
-
single turnover kinetics and thermodynamic analysis of effect of different guanosine analogues on m1G37-tRNA synthesis, kinetic analysis, overview
-
additional information
additional information
wild-type and mutant enzymes pH-dependence of the single-turnover rate constant: the pH dependence of kobs in single-turnover analysis corresponds to proton ransfer during a slower process of induced fit, rather than the bond-breaking and bond-forming steps of methyl transfer, detailed analysis and overview
-
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
-
additional information
additional information
Michaelis-Menten steady-state kinetics analysis
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics analysis
-
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
-
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
-
additional information
additional information
-
structure-guided kinetic analysis of TrmD mutants and tRNA variants, overview
-
additional information
additional information
-
structure-guided kinetic analysis of TrmD mutants and tRNA variants, overview
-
additional information
additional information
-
binding kinetics of TrmD ligands
-
additional information
additional information
-
binding kinetics of TrmD ligands
-
additional information
additional information
-
binding kinetics of TrmD ligands
-
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
-
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
-
additional information
additional information
pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays
-
additional information
additional information
pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays
-
additional information
additional information
pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays
-
additional information
additional information
pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays
-
