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S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
S-adenosyl-L-methionine + guanine36 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine36 in tRNALeu
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAArg(ACG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAArg(ACG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAArg(CCG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAArg(CCG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAGln(UUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAGln(UUG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAHis(GUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAHis(GUG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNALeu(CAG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Aquifex aeolicus tRNAPro(GGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Aquifex aeolicus tRNAPro(GGG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in elongator tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in elongator tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNA1Leu
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNA1Leu
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNAPro
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNACys(GCA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNACys(GCA)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNALeu(CAA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNALeu(CAA)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNATrp(CCA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNATrp(CCA)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Haloferax volcanii tRNATyr(GUA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Haloferax volcanii tRNATyr(GUA)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in human mitochondrial tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro
S-adenosyl-L-methionine + guanine37 in human mitochondrial tRNAPro possessing an A36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro possessing an A36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in in Escherichia coli tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in in Escherichia coli tRNALeu(CAG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNA(Cys)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNA(Cys)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAArg(UCG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAArg(UCG)
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNACys
-
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNACys(GCA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNACys(GCA)
possessing the sequence A36G37. The enzyme is inactive with mutant forms of Methanocaldococcus jannaschii tRNACys(GCA) containing A37, C37, or U37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAGlu(UUC)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAGlu(UUC)
possessing the sequence C36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNALeu(UCG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNALeu(UCG)
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro(GGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro(GGG)
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro(UGG)
possessing the sequence G36G37
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
S-adenosyl-L-methionine + guanine37 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArg
S-adenosyl-L-methionine + guanine37 in tRNAArgCCG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArgCCG
S-adenosyl-L-methionine + guanine37 in tRNAAsp(GUC)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAAsp(GUC)
enzyme AtTrm5a can methylate Saccharomyces cerevisiae tRNAAsp(GUC) in vivo and in vitro
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-
?
S-adenosyl-L-methionine + guanine37 in tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
S-adenosyl-L-methionine + guanine37 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACysGCA
S-adenosyl-L-methionine + guanine37 in tRNAGlnCUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnCUG
S-adenosyl-L-methionine + guanine37 in tRNAGlnG36A
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnG36A
-
tRNA substrate from Thermotoga maritima
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-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnG36C
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnG36C
-
tRNA substrate from Thermotoga maritima
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnG36U
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnG36U
-
tRNA substrate from Thermotoga maritima
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHis(GUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHis(GUG)
S-adenosyl-L-methionine + guanine37 in tRNAHisGUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHisGUG
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
S-adenosyl-L-methionine + guanine37 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(CAG)
S-adenosyl-L-methionine + guanine37 in tRNALeu(GAC)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(GAC)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu(GAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(GAG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(UAG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeuCAG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeuCAG
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
S-adenosyl-L-methionine + guanine37 in tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro
S-adenosyl-L-methionine + guanine37 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(CGG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro(GGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(GGG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
S-adenosyl-L-methionine + guanine37 in tRNAProAGG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAProAGG
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNA(Asp) possessing a G36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNA(Asp) possessing a G36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing a C36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing a C36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing a G36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing a G36G37 sequence
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing an A36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNA(Asp) possessing an A36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing an A36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing an A36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing an U36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing an U36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAPhe possessing an A36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAPhe possessing an A36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAPhe(GAA)
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAPhe(GAA)
-
-
-
-
?
S-adenosyl-L-methionine + inosine37 in yeast tRNAAsp possessing a G36I37 sequence
S-adenosyl-L-homocysteine + N1-methylinosine37 in yeast tRNAAsp possessing a G36I37 sequence
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
additional information
?
-
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
i.e. im-G14, activity of EC 2.1.1.282
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
i.e. im-G14, activity of EC 2.1.1.282
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
i.e. im-G14, activity of EC 2.1.1.282
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
i.e. yW-86, activity of EC 2.1.1.228
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
i.e. yW-86, activity of EC 2.1.1.228
-
-
?
S-adenosyl-L-methionine + 7-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + 7-[(3S)-(3-amino-3-carboxypropyl)]wyosine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine36 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine36 in tRNALeu
-
G36-substituted tRNA substrate Escherichia coli tRNALeu, TrmD shows a 90fold reduced catalytic efficiency, discrimination between the two sequences of G36 and G37
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-
?
S-adenosyl-L-methionine + guanine36 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine36 in tRNALeu
-
G36-substituted tRNA substrate Escherichia coli tRNALeu, Trm5 shows a lack of discrimination between the two sequences of G36 and G37
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-
?
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNA1Leu
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNA1Leu
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-
?
S-adenosyl-L-methionine + guanine37 in Escherichia coli tRNA1Leu
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNA1Leu
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-
?
S-adenosyl-L-methionine + guanine37 in human mitochondrial tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro
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-
-
?
S-adenosyl-L-methionine + guanine37 in human mitochondrial tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro
-
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-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro
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-
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-
?
S-adenosyl-L-methionine + guanine37 in Methanocaldococcus jannaschii tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
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-
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
the enzyme methylates tRNA transcripts possessing an A36G37 sequence as well as tRNA transcripts possessing a G36G37 sequence. tRNA transcripts possessing pyrimidine36G37 are not methylated at all. The modified nucleoside and the position in yeast tRNA(Phe) transcript are confirmed by LC/MS. Nine truncated tRNA molecules are tested to clarify the additional recognition site. The TrmD protein efficiently methylates the micro helix corresponding to the anti-codon arm. Because the disruption of the anti-codon stem causes the complete loss of the methyl group acceptance activity, the anti-codon stem is essential for the recognition. The existence of the D-arm structure inhibits the activity
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?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
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-
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
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-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
methylates the N1 position of guanosine 37 (G37) in selected tRNA transcripts
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
substrate binding stoichiometry to TrmD, dissociation constants, overview
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD recognizes N1 and O6 of G37 and the exocyclic 2-amino group of G37 is important for TrmD, also TrmD requires G36 for synthesis of m1G37
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
the pH-activity profile indicates one proton transfer during the TrmD reaction
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?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
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-
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD catalyzes the N1-methylguanosine (m1G) modification at position 37 in tRNAs with the 36GG37 sequence, using S-adenosyl-L-methionine as the methyl donor
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD catalyzes the N1-methylguanosine (m1G) modification at position 37 in tRNAs with the 36GG37 sequence, using S-adenosyl-L-methionine as the methyl donor
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
methylates the N1 position of guanosine 37 (G37) in selected tRNA transcripts
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-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
tight binding of Trm5 to products
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
Trm5 recognizes N1 and O6 of G37, but the exocyclic 2-amino group of G37 is dispensable for Trm5. Trm5 does not require G36
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
Trm5p is responsible for m1G37 methylation of mitochondrial and cytoplasmic tRNAs
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
methyltransferase activity with tRNA isolated from a DELTAtrm5 mutant strain, as well as with a synthetic mitochondrial initiator tRNA (tRNAMetf). N1-Methylguanine is determined by high pressure liquid chromatography analysis
the site of methylation is guanosine 37 in both mitochondrial tRNAMetf and tRNAPhe, determined by primer extension
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
the streptococcal enzyme utilizes a sequential mechanism. Nonsubstrate tRNA species, like tRNAThr(GGT), tRNAPhe, and tRNAAla(TGC), bind the enzyme with similar affinities, suggesting that tRNA specificity is achieved via a postbinding events. The streptococcal TrmD requires the complete tRNA structure since it cannot modify the tRNALeu(CAG) minihelix lacking the D, T, and extra loops of complete tRNA. In addition, and consistent with a requirement for G at positions 36 and 37 in the tRNA, the enzyme methylates yeast tRNAAsp possessing a G36G37 sequence with kinetic values that are indistinguishable from those obtained with substrate tRNALeu(CAG) but does not methylate either tRNAAsp possessing a C36G37 sequence or tRNA(Asp) possessing a C36A37 sequence
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
TrmD catalyzes the N1-methylguanosine (m1G) modification at position 37 in tRNAs with the 36GG37 sequence, using S-adenosyl-L-methionine as the methyl donor
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArg
-
tRNA substrate from Haemophilus influenzae
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArg
-
tRNA substrate from Haemophilus influenzae
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAArgCCG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArgCCG
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAArgCCG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAArgCCG
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
-
Methanococcus jannaschii tRNACys
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACys
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACys
Methanococcus jannaschii tRNACys
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACysGCA
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNACysGCA
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnCUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnCUG
-
the wild-type Thermotoga maritima tRNAGlnCUG transcript is methylated by Haemophilus influenzae TrmD 2.2 to 99fold more efficiently than the Haemophilus influenzae tRNA transcripts
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnCUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnCUG
-
the wild-type Thermotoga maritima tRNAGlnCUG transcript is methylated by Haemophilus influenzae TrmD 2.2 to 99fold more efficiently than the Haemophilus influenzae tRNA transcripts
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAGlnCUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAGlnCUG
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHis(GUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHis(GUG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHis(GUG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHis(GUG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHisGUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHisGUG
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAHisGUG
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAHisGUG
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
Trametes pubescens 927 / 4 GUTat10.1 / TREU927
TbTRM5 is responsible for m1G37 formation in several tRNAs, cytosolic tRNAIle UAU is essentially fully modified at G37
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
TbTRM5 is responsible for m1G37 formation in several tRNAs, cytosolic tRNAIle UAU is essentially fully modified at G37
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
-
Escherichia coli tRNALeu
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
-
tRNA substrate from Haemophilus influenzae
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu
-
tRNA substrate from Haemophilus influenzae
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(CAG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(CAG)
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(CAG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro
the A37 mutant of EctRNAPro is no substrate for the enzyme
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro
-
tRNA substrate from Haemophilus influenzae
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing a G36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing a G36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + guanine37 in yeast tRNAAsp possessing a G36G37 sequence
S-adenosyl-L-homocysteine + N1-methylguanine37 in yeast tRNAAsp possessing a G36G37 sequence
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
-
-
-
?
additional information
?
-
-
no activity with guanine37 in yeast tRNAAsp(GUC) possessing a C36G37 sequence, guanine37 in Haloferax volcanii tRNAGlu(UUC) possessing a C36G37 sequence, guanine37 in yeast tRNAPhe A36U mutant(GAU) possessing a U36G37 sequence, guanine37 in Escherichia coli tRNASer(UGA) possessing a A36G37 sequence
-
-
?
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected. The tRNA recognition mechanism of Aquifex aeolicus TrmD shows that a micro-helix RNA corresponding to the anticodon-arm is the minimal substrate for this enzyme
-
-
-
additional information
?
-
TrmD recognizes the G36pG37 motif preferentially and does not methylate inosine. The TrmD enzyme is tolerant of alterations in tRNA-protein tertiary interactions as long as the core tRNA structure and the G36pG37 are present
-
-
?
additional information
?
-
-
TrmD recognizes the G36pG37 motif preferentially and does not methylate inosine. The TrmD enzyme is tolerant of alterations in tRNA-protein tertiary interactions as long as the core tRNA structure and the G36pG37 are present
-
-
?
additional information
?
-
-
TrmD catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon
-
-
?
additional information
?
-
-
recognition of N1 of G37 in tRNA is essential for translational fidelity in all biological domains, TrmD shows a more rigid requirement of guanosine functional groups. Replacment of functional groups of G37 by guanosine analogues, i.e. deoxyG, 6-thioG, inosine, and 2-aminopurine, in EctRNALeu, to design the optimal substrate for TrmD. All but deoxyG of these analogs probed the Watson-Crick basepairing interface of G37
-
-
?
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected
-
-
-
additional information
?
-
TrmD is a bacterial enzyme with a trefoil-knot in the active site, involving three crossings of the protein backbone through a loop. TrmD catalyzes methyl transfer from AdoMet to the N1 of G37 on the 3' side of the tRNA anticodon
-
-
-
additional information
?
-
TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
TrmD can methylate a truncated tRNA, in which T- and D-arms have been deleted, the anticodon-arm region is mainly protected
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
proposed model for the TrmD enzymatic cycle which consists of the AdoMet-binding, tRNA-binding, and methyl transfer stages, overview. Anticodon-branch recognition and detection of position 37, interaction analysis of TrmD with G36 and G37
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer
-
-
-
additional information
?
-
guanosine37-methylation by TRM5 occurs regardless of the nature of the nucleotide at position 36. TRM5 also methylates inosine at position 37. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity. The enzyme does not methylate adenosine37, cytosine37 or uridine37 in tRNA. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity
-
-
?
additional information
?
-
-
guanosine37-methylation by TRM5 occurs regardless of the nature of the nucleotide at position 36. TRM5 also methylates inosine at position 37. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity. The enzyme does not methylate adenosine37, cytosine37 or uridine37 in tRNA. The TRM5 enzyme is sensitive to subtle changes in the tRNA-protein tertiary interaction leading to loss of activity
-
-
?
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
the enzyme is specific for methylation of guanine37 in tRNA. No methylation of tRNAArg(UCU) possessing the sequence U36G37
-
-
?
additional information
?
-
-
the enzyme is specific for methylation of guanine37 in tRNA. No methylation of tRNAArg(UCU) possessing the sequence U36G37
-
-
?
additional information
?
-
-
Trm5 catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon
-
-
?
additional information
?
-
-
recognition of N1 of G37 in tRNA is essential for translational fidelity in all biological domains, Trm5 shows a less rigid requirement of guanosine functional groups. Replacment of functional groups of G37 by guanosine analogues, i.e. deoxyG, 6-thioG, inosine, and 2-aminopurine, in MjtRNACys, to design the optimal substrate for Trm5
-
-
?
additional information
?
-
structure of Trm5 active site bound to tRNA and S-adenosyl-L-methionine, induced fit for active-site assembly, detailed overview. E185 is crucial both for general base catalysis and for the conformational change that precedes catalysis
-
-
?
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA, the enzyme recognizes the overall shape of tRNA, overview. Enzyme-substrate interactions in the catalytic domain, D1 domain ofMjTrm5b transitions, overview
-
-
-
additional information
?
-
the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA, the enzyme recognizes the overall shape of tRNA, overview. Enzyme-substrate interactions in the catalytic domain, D1 domain ofMjTrm5b transitions, overview
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
-
the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
-
-
-
additional information
?
-
radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
-
-
-
additional information
?
-
tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
-
-
-
additional information
?
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the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
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additional information
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radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
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additional information
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tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
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additional information
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the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
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additional information
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radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
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additional information
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tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
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additional information
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the mutant tRNAMet transcripts (G37) are modified with m1G37 modification by the Mj-Trm5 but as less efficiently as cytoplasmic tRNALeu(CAG) transcripts. In contrast, the modification is not detected in the human wild-type tRNAMet transcripts (A37) in the presence of Mj-Trm5. The human cytoplasmic tRNALeu(CAG) transcripts (G37) are modified by the Mj-Trm5, whereas human cytoplasmic tRNAThr transcripts (A37) are not modified in the presence of Mj-Trm5. Marked decrease in the steady-state levels of mutated tRNAMet
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additional information
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radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product
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additional information
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Nanoarchaeum equitans NEQ228 protein displays a dual tRNAPhe:m1G/imG2 methyltransferase activity. Two different types of substrates are used: (1) bulk tRNA, isolated from Salmonella enterica trmDELTA27 mutant containing the unmodified G37 nucleotide leading tothe formation of pm1G, and (2) tRNA, which is isolated from the Saccharomes cerevisiae DELTAtyw2 mutant that contains the imG-14 wyosine derivative leading to formation of pimG2pA dinucleotide and to a lesser extent to pm1G, likely resulting from the small amounts of G37-containing tRNAPhe present in the bulk tRNA isolates from the Scetyw2 mutant
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additional information
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substrate specificity, mass spectrometric analysis confirms the G36G37-containing tRNAs Leu(GAG), Leu(CAG), Leu(UAG), Pro(GGG), Pro(UGG), Pro(CGG), and His(GUG) as PaTrmD substrates, overview. PaTrmD catalyzes m1G formation in synthetic tRNA substrates. PaTrmD catalyzes m1G at position 37 in the tRNA anticodon loop. Preparation of tRNA substrates by in vitro transcription, product determination by mass spectrometry
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additional information
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substrate specificity, mass spectrometric analysis confirms the G36G37-containing tRNAs Leu(GAG), Leu(CAG), Leu(UAG), Pro(GGG), Pro(UGG), Pro(CGG), and His(GUG) as PaTrmD substrates, overview. PaTrmD catalyzes m1G formation in synthetic tRNA substrates. PaTrmD catalyzes m1G at position 37 in the tRNA anticodon loop. Preparation of tRNA substrates by in vitro transcription, product determination by mass spectrometry
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additional information
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TrmD luminescence assay development
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additional information
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TrmD luminescence assay development
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additional information
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TrmD luminescence assay development
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additional information
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substrate specificity, mass spectrometric analysis confirms the G36G37-containing tRNAs Leu(GAG), Leu(CAG), Leu(UAG), Pro(GGG), Pro(UGG), Pro(CGG), and His(GUG) as PaTrmD substrates, overview. PaTrmD catalyzes m1G formation in synthetic tRNA substrates. PaTrmD catalyzes m1G at position 37 in the tRNA anticodon loop. Preparation of tRNA substrates by in vitro transcription, product determination by mass spectrometry
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additional information
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bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
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additional information
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bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
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additional information
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bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
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additional information
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no activity of Trm5b with 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe (cf. EC 2.1.1.282)
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additional information
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no activity of Trm5b with 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe (cf. EC 2.1.1.282)
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additional information
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Pyrococcus abyssi PAB2272 protein displays a dual tRNAPhe:m1G/imG2 methyltransferase activity. Two different types of substrates are used: (1) bulk tRNA, isolated from Salmonella enterica trmDELTA27 mutant containing the unmodified G37 nucleotide leading to the formation of pm1G, and (2) tRNA, which is isolated from the Saccharomes cerevisiae DELTAtyw2 mutant that contains the imG-14 wyosine derivative leading to formation of pimG2pA dinucleotide and to a lesser extent to pm1G, likely resulting from the small amounts of G37-containing tRNAPhe present in the bulk tRNA isolates from the Scetyw2 mutant
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additional information
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structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA. The enzyme recognizes the overall shape of tRNA. PaTrm5a adopts distinct open conformations before and after the binding of tRNA. Enzyme-substrate interactions in the catalytic domain. The anticodon interactions mostly concentrate on the A36-G37-A38 triplet. Proposed reaction mechanism of Trm5a with modified yeast tRNAPhe, overview
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additional information
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substrate-binding modes of PaTrm5a, and recognition of substrate analogues, overview
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additional information
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substrate-binding modes of PaTrm5a, and recognition of substrate analogues, overview
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additional information
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tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
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additional information
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tRNA recognition by Trm5, detailed overview. The structure of positions 33-37 in the anticodon loop is largely altered from the canonical tRNA structure, and the target G37 is flipped out into the catalytic pocket formed by the D2 and D3 domains. The flipped G37 is recognized in a guanosine-specific manner by the side chains of Arg145 and Asn265, and the N1-atom (the methylation atom) of G37 is located next to the methyl moiety of AdoMet. The adequate interaction between D1 and tRNA enables the catalytic D2-D3 to perform the m1G37 methylation. The m1G37 methylation is achieved by a sensor-effector mechanism in which the affinity of Trm5 for tRNA increases only when the sensor (D1) confirms the completion of the L-shape formation and the catalytically competent effector (D2-D3) is recruited to the tRNA
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additional information
?
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Pyrococcus abyssi PAB2272 protein displays a dual tRNAPhe:m1G/imG2 methyltransferase activity. Two different types of substrates are used: (1) bulk tRNA, isolated from Salmonella enterica trmDELTA27 mutant containing the unmodified G37 nucleotide leading to the formation of pm1G, and (2) tRNA, which is isolated from the Saccharomes cerevisiae DELTAtyw2 mutant that contains the imG-14 wyosine derivative leading to formation of pimG2pA dinucleotide and to a lesser extent to pm1G, likely resulting from the small amounts of G37-containing tRNAPhe present in the bulk tRNA isolates from the Scetyw2 mutant
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additional information
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TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
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additional information
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TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
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additional information
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TrmD synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the anticodon
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