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
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2.1.1.228
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methyltransferases
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anticodon
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adomet
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1-methylguanosine
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drug development
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n2-guanine
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trmt10a
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1-methyladenine
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adomet-dependent
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5-methyluridine
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trmfo
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n1-methylation
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methyl-deficient
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7-methylguanine
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spout
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epitranscriptome
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nsun2-mediated
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medicine
- 2.1.1.228
- methyltransferases
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anticodon
- adomet
- 1-methylguanosine
- drug development
-
n2-guanine
- trmt10a
- 1-methyladenine
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adomet-dependent
- 5-methyluridine
- trmfo
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n1-methylation
-
methyl-deficient
- 7-methylguanine
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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
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results (Engineering
Engineering on EC 2.1.1.228 - tRNA (guanine37-N1)-methyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C20S
the C20S mutant protein forms a dimer structure even though it is missing the Cys20Cys20 disulfide bond between its two subunits. Incubation at 85°C for 20 min causes the precipitation of more than half of the C20S protein, while more than 70% of the wild-type enzyme is soluble at that temperature. Methyl-transfer activity of the C20S mutant protein is slightly less than that of the wild-type enzyme at 70°C. Comparison of the CD-spectra of wild-type and C20S proteins reveals that some of the alpha-helices in the C20S mutant protein are less tightly packed than the alpha-helices of the wild-type enzyme at 70°C
S88L
naturally occuring mutation of trmD, the mutation confers thermal lability to the enzyme with a minor effect. The mutation decreases the catalytic efficiency of the enzyme to 1% of wild-type activity at permissive temperature. At nonpermissive temperature, it renders further deterioration of activity to 0.1%. These changes are accompanied by losses of both the quantity and quality of tRNA methylation, leading to the potential of cellular pleiotropic effects
D275A
site-directed mutagenesis, the mutation leads to significantly reduced activity
E288A
site-directed mutagenesis, the mutation at the general base position leads to highly reduced activity
E394K
site-directed mutagenesis, the mutation facilitates enzyme expression in Escherichia coli
H289A
site-directed mutagenesis, the mutation C-terminally adjacent to the general base does not affect the enzyme activity
H289R
site-directed mutagenesis, the mutation C-terminally adjacent to the general base does not affect the enzyme activity
M261L
site-directed mutagenesis, the single M261L substitution that recapitulates the archaeal residue minimizes the 27-kDa protease product upon enzyme expression in Escherichia coli, indicating improved stability
M261L/T261I
site-directed mutagenesis, the double M261L substitution also shows improved stability
M386V
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naturally occuring TRMT5 mutation, the mutant shows diminished G37 modification of a mitochondrial tRNA and a pathogenic phenotype
R291H
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naturally occuring TRMT5 mutation, the mutant shows diminished G37 modification of a mitochondrial tRNA and a pathogenic phenotype
D223A
D223E
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
D223L
site-directed mutagenesis, the mutant shows complete loss of activity
D223N
site-directed mutagenesis, the mutant shows complete loss of activity
E185A
site-directed mutagenesis, the mutant shows complete loss of activity
E185D
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
E185Q
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
G205A/G207A
K137A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
K318A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
N225A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 5% of the wild-type value
N265A
N265H
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
N265Q
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
P226A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 6% of the wild-type value
P267A
R144A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 6% of the wild-type value
R145A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
R181A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
R186A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
Y176A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 5% of the wild-type value
Y177A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
Y177F
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
D243A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
E173A
site-directed mutagenesis, the mutant shows 9 and 26% of wild-type activity for imG and imG2 formation, respectively
E213A
H128A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
P260N
site-directed mutagenesis, the mutant shows no and 114% of wild-type activity for imG and imG2 formation, respectively
P262A
site-directed mutagenesis, the mutant shows 5 and 8% of wild-type activity for imG and imG2 formation, respectively
R133A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R134A
site-directed mutagenesis, the mutant shows 2 and 4% of wild-type activity for imG and imG2 formation, respectively
R135A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R174A
Y318A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
E173A
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site-directed mutagenesis, the mutant shows 9 and 26% of wild-type activity for imG and imG2 formation, respectively
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R134A
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site-directed mutagenesis, the mutant shows 2 and 4% of wild-type activity for imG and imG2 formation, respectively
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R174A
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site-directed mutagenesis, the mutant shows 8 and 69% of wild-type activity for imG and imG2 formation, respectively
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S88L
additional information
D223A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 1% of the wild-type value
D223A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
G205A/G207A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 3% of the wild-type value
N265A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 1% of the wild-type value
N265A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
P267A
kcat/Km for guanine37 in Methanocaldococcus jannaschii tRNACys is 0.1% of the wild-type value
P267A
site-directed mutagenesis, the mutant shows altered single turnover kinetics compared to the wild-type enzyme
E213A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R174A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
R174A
site-directed mutagenesis, the mutant shows 8 and 69% of wild-type activity for imG and imG2 formation, respectively
S88L
mutant trmD harbors a mutation near the AdoMet binding site, the mutation prevents the enzyme from binding to the methyl donor and from performing the Mg2C-dependent methyl transfer. The reported observation supports a model of codon-specific translation in the 5'-leader ORF
S88L
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mutant trmD harbors a mutation near the AdoMet binding site, the mutation prevents the enzyme from binding to the methyl donor and from performing the Mg2C-dependent methyl transfer. The reported observation supports a model of codon-specific translation in the 5'-leader ORF
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S88L
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mutant trmD harbors a mutation near the AdoMet binding site, the mutation prevents the enzyme from binding to the methyl donor and from performing the Mg2C-dependent methyl transfer. The reported observation supports a model of codon-specific translation in the 5'-leader ORF
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additional information
generation of T-DNA insertion attrm5a deletion mutants, phenotypes, overview
additional information
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generation of T-DNA insertion attrm5a deletion mutants, phenotypes, overview
additional information
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identification of TRMT5 enzyme mutants in patients, the loss of m1G37 does not appear to impact tRNA stability, phenotype, overview
additional information
structure-guided mutational analysis of HsTrm5 in comparison to the archaeal enzyme from Methanococcus jannaschii, MjTrm5, overview. Validation of the MjTrm5 ternary structure as a useful model for HsTrm5
additional information
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structure-guided mutational analysis of HsTrm5 in comparison to the archaeal enzyme from Methanococcus jannaschii, MjTrm5, overview. Validation of the MjTrm5 ternary structure as a useful model for HsTrm5
additional information
proline at position 267 is a critical residue for catalysis, because substitution of this residue severely decreases kcat of the methylation reaction in steady-state kinetic analysis. However, substitution of P267 has milder effect on Km and little effect on Kd of either substrate. Because P267 has no functional side chain that can directly participate in the chemistry of methyl transfer, we suggest that its role in catalysis is to stabilize conformations of enzyme and substrates for proper alignment of reactive groups at the enzyme active site. Sequence analysis shows that P267 is embedded in a peptide motif that is conserved among the Trm5 family, but absent from the TrmD family, supporting the notion that the two families are descendants of unrelated protein structures
additional information
the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
additional information
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the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
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additional information
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the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
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additional information
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the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
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additional information
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the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
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additional information
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the m.4435A->G mutation introduces an m1G37 modification of tRNAMet, altering its structure and function. Primer extension and methylation activity assays indeed confirm that the m.4435A3G mutation creates a tRNA methyltransferase 5 (TRMT5)-catalyzed m1G37 modification of tRNAMet
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additional information
attempts to construct a PA14_15990/trmD mutant in Pseudomonas aeruginosa strain PA14 using homologous recombination are not successful, due to the fact that the enzyme is essential in Pseudomonas aeruginosa. A temperature-sensitive allele of a Pseudomonas replicon, mSFts1 is used, to regulate expression of extra chromosomal trmD. Wild-type strain PA14 containing pBBR-trmD-mSFts1 and the trmD conditional knockout strain (trmD::Gm/pBBR-trmD-mSFts1) are both grown at a permissive temperature to maintain the stability of the plasmid (28 and 37°C) or at a non-permissive temperature to cause plasmid loss (46°C). The growth of the trmD conditional knockout strain at the permissive temperature is similar to wild-type PA14, while growth of the knockout strain is no longer observed at the non-permissive temperature
additional information
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attempts to construct a PA14_15990/trmD mutant in Pseudomonas aeruginosa strain PA14 using homologous recombination are not successful, due to the fact that the enzyme is essential in Pseudomonas aeruginosa. A temperature-sensitive allele of a Pseudomonas replicon, mSFts1 is used, to regulate expression of extra chromosomal trmD. Wild-type strain PA14 containing pBBR-trmD-mSFts1 and the trmD conditional knockout strain (trmD::Gm/pBBR-trmD-mSFts1) are both grown at a permissive temperature to maintain the stability of the plasmid (28 and 37°C) or at a non-permissive temperature to cause plasmid loss (46°C). The growth of the trmD conditional knockout strain at the permissive temperature is similar to wild-type PA14, while growth of the knockout strain is no longer observed at the non-permissive temperature
additional information
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attempts to construct a PA14_15990/trmD mutant in Pseudomonas aeruginosa strain PA14 using homologous recombination are not successful, due to the fact that the enzyme is essential in Pseudomonas aeruginosa. A temperature-sensitive allele of a Pseudomonas replicon, mSFts1 is used, to regulate expression of extra chromosomal trmD. Wild-type strain PA14 containing pBBR-trmD-mSFts1 and the trmD conditional knockout strain (trmD::Gm/pBBR-trmD-mSFts1) are both grown at a permissive temperature to maintain the stability of the plasmid (28 and 37°C) or at a non-permissive temperature to cause plasmid loss (46°C). The growth of the trmD conditional knockout strain at the permissive temperature is similar to wild-type PA14, while growth of the knockout strain is no longer observed at the non-permissive temperature
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additional information
construction of the D1-truncated PaTrm5b73-330 mutant using full-length Trm5b as the template
additional information
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construction of the D1-truncated PaTrm5b73-330 mutant using full-length Trm5b as the template
additional information
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
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generation of enzyme knockout lines using a TbTRM5 RNAi plasmid in procyclic Trypanosoma brucei 29-13 cells
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additional information
generation of enzyme knockout lines using a TbTRM5 RNAi plasmid in procyclic Trypanosoma brucei 29-13 cells
