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Information on EC 2.1.1.228 - tRNA (guanine37-N1)-methyltransferase
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2.1.1.228 tRNA (guanine37-N1)-methyltransferaseIUBMB Comments
This enzyme is important for the maintenance of the correct reading frame during translation. Unlike TrmD from Escherichia coli, which recognizes the G36pG37 motif preferentially, the human enzyme (encoded by TRMT5) also methylates inosine at position 37 .
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Word Map
- 2.1.1.228
- methyltransferases
-
anticodon
- adomet
- 1-methylguanosine
- drug development
-
n2-guanine
- trmt10a
-
methyl-deficient
-
n1-methylation
-
adomet-dependent
- trmfo
- 1-methyladenine
- 5-methyluridine
-
epitranscriptome
- 7-methylguanine
-
nsun2-mediated
-
spout
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
guanine37 in tRNA
=
+
N1-methylguanine37 in tRNA
Synonyms
At3g56120, aTrm5a methyltransferase, aTrm5a/Taw22-like enzyme, AtTrm5a, bacterial tRNA (guanine37-N1)-methyltransferase, bacterial tRNA-(N1G37) methyltransferase, EcTrmD, HiTrmD, HsTrm5, m1G37 tRNA methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aTrm5a methyltransferase
aTrm5a/Taw22-like enzyme
bacterial tRNA (guanine37-N1)-methyltransferase
bacterial tRNA-(N1G37) methyltransferase
HiTrmD
m1G37 tRNA methyltransferase
m1G37-forming tRNA methyltransferase
Mj-Trm5
MjTrm5
MjTrm5b
PA14_15990
PaTrmD
TAW22
Trm1
TRM5
Trm5a
trm5b
Trm5p
TrmD
TRMT5
tRNA (guanine37-N1)-methyltransferase
tRNA (m1G37) methyltransferase
tRNA (m1G37)-methyltransferase
tRNA methyltransferase
tRNA methyltransferase 5
tRNA methyltransferase D
tRNA(m1G37)methyltransferase
tRNA-(N1G37) methyltransferase
tRNAPhe:imG2 methyltransferase
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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-
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S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
mechanism of N-methylation by the tRNA m1G37 methyltransferase Trm5 involving proton abstraction during docking of G37 in the active site by a general base , E185
S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
substrate recognition and reaction mechanisms, overview
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S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
substrate recognition and reaction mechanisms, overview
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S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
a highly conserved aspartate residue, D275 in Homo sapiens Trm5, in the flexible loop preceding the proposed general base E288 may be involved in the induced-fit movement of the catalytic process
S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
catalytic mechanism in which the role of Mg2+ is to help to increase the nucleophilicity of N1 of G37 and stabilize the negative developing charge on O6 during attack on the methyl sulfonium of S-adenosyl-L-methionine. Substrate binding to EcTrmD is in rapid equilibrium to form the enzyme-tRNA-S-adenosyl-L-methionine complex, a proton abstraction step is rate limiting in methyl transfer
-
S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
mechanism by which TrmD binds the substrate tRNA in an S-adenosyl-L-methionine-dependent manner: The trefoil-knot center, which is structurally conserved among SPOUTMTases, accommodates the adenosine moiety of S-adenosyl-L-methionine by loosening/retightening of the knot. The TrmD-specific regions surrounding the trefoil knot recognize the methionine moiety of S-adenosyl-L-methionine, and thereby establish the entire TrmD structure for global interactions with tRNA and sequential and specific accommodations of G37 and G36, resulting in the synthesis of m1G37-tRNA
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S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
mechanism by which TrmD binds the substrate tRNA in an S-adenosyl-L-methionine-dependent manner: The trefoil-knot center, which is structurally conserved among SPOUTMTases, accommodates the adenosine moiety of S-adenosyl-L-methionine by loosening/retightening of the knot. The TrmD-specific regions surrounding the trefoil knot recognize the methionine moiety of S-adenosyl-L-methionine, and thereby establish the entire TrmD structure for global interactions with tRNA and sequential and specific accommodations of G37 and G36, resulting in the synthesis of m1G37-tRNA
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S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
mechanism by which TrmD binds the substrate tRNA in an S-adenosyl-L-methionine-dependent manner: The trefoil-knot center, which is structurally conserved among SPOUTMTases, accommodates the adenosine moiety of S-adenosyl-L-methionine by loosening/retightening of the knot. The TrmD-specific regions surrounding the trefoil knot recognize the methionine moiety of S-adenosyl-L-methionine, and thereby establish the entire TrmD structure for global interactions with tRNA and sequential and specific accommodations of G37 and G36, resulting in the synthesis of m1G37-tRNA
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine37-N1)-methyltransferase
This enzyme is important for the maintenance of the correct reading frame during translation. Unlike TrmD from Escherichia coli, which recognizes the G36pG37 motif preferentially, the human enzyme (encoded by TRMT5) also methylates inosine at position 37 [4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
-
?
S-adenosyl-L-methionine + guanine37 in in Escherichia coli tRNALeu(CAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in in Escherichia coli tRNALeu(CAG)
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-
-
-
?
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
-
-
?
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
-
-
?
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)
-
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-
?
S-adenosyl-L-methionine + guanine37 in tRNALeu(UAG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNALeu(UAG)
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?
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
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
-
-
?
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
-
-
?
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 tRNA1Leu
S-adenosyl-L-homocysteine + N1-methylguanine37 in Escherichia coli tRNA1Leu
-
-
-
?
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
S-adenosyl-L-homocysteine + N1-methylguanine37 in human mitochondrial tRNAPro
-
-
-
?
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
S-adenosyl-L-homocysteine + N1-methylguanine37 in Methanocaldococcus jannaschii tRNAPro
-
-
-
?
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
-
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
-
-
-
?
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
-
-
-
-
?
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
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
substrate binding stoichiometry to TrmD, dissociation constants, overview
-
-
?
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
-
-
?
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
-
-
?
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
-
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 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
-
-
?
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
-
-
?
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
?
-
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
?
-
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
?
-
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
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
TrmD luminescence assay development
-
-
-
additional information
?
-
-
TrmD luminescence assay development
-
-
-
additional information
?
-
TrmD luminescence assay development
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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)
-
-
-
additional information
?
-
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)
-
-
-
additional information
?
-
-
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)
-
-
-
additional information
?
-
no activity of Trm5b with 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe (cf. EC 2.1.1.282)
-
-
-
additional information
?
-
-
no activity of Trm5b with 7-[(3S)-(3-amino-3-carboxypropyl)]-4-demethylwyosine37 in tRNAPhe (cf. EC 2.1.1.282)
-
-
-
additional information
?
-
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
-
-
-
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. 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
-
-
-
additional information
?
-
substrate-binding modes of PaTrm5a, and recognition of substrate analogues, overview
-
-
-
additional information
?
-
-
substrate-binding modes of PaTrm5a, and recognition of substrate analogues, 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
?
-
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
?
-
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
-
-
-
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 synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the 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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + guanine37 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
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
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAIleUaU
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAIleUaU
S-adenosyl-L-methionine + guanine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
S-adenosyl-L-methionine + guanine37 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPro(UGG)
-
-
-
?
S-adenosyl-L-methionine + wyosine37 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylwyosine37 in tRNAPhe
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
S-adenosyl-L-methionine + 4-demethylwyosine
S-adenosyl-L-homocysteine + isowyosine
-
-
-
?
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-aminocarboxypropyl-demethylwyosine
S-adenosyl-L-homocysteine + wyosine
-
-
-
?
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 + 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
-
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 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 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
-
-
-
-
?
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
-
-
-
?
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
-
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 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
TbTRM5 is responsible for m1G37 formation in several tRNAs, cytosolic tRNAIle UAU is essentially fully modified at G37
-
-
?
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 + 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
?
-
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 catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to 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
?
-
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
?
-
-
Trm5 catalyzes methyl transfer to synthesize the m1G37 base at the 3' position adjacent to the tRNA anticodon
-
-
?
additional information
?
-
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)
-
-
-
additional information
?
-
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)
-
-
-
additional information
?
-
-
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)
-
-
-
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 synthesizes the methylated m1G37 on bacterial tRNAs that contain both G37 and a preceding G36, the 3'-nucleotide of the 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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine
-
Trm5 binding structure, detailed overview
S-adenosyl-L-methionine
binding structure analysis at 2.16 A resolution. PaTrmD shares functionally important amino acid residues involved in cofactor binding (Ser93-Gly96, Gly118, Ile123, Ser137, Gly145), tRNA binding (Gly60, Gly64, Ser203-His206) and catalytic activity (Asp54, Arg159, and Asp174)
S-adenosyl-L-methionine
the AdoMet binding pocket is located between E206, R209, N380, P382, Y198 and R165. Due to the flexibility of D1 domain, a structure model is projected using only D2 and D3 domains, using structure PDB 2YX1 of chain A of Trm5 from Methanococcus jannashii as template
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
KCl
TRM5 enzyme is stimulated 4fold by 100 mM KCl. TRM5 tends to lose all activity in 600 mM KCl
Mg2+
Mn2+
Ni2+
additional information
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+
-
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+
-
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
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
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4-oxo-3,4-dihydrothieno[3,2-d]pyrimidin-2-yl)methyl 2-(furan-2-yl)quinoline-4-carboxylate
-
1-(1H-pyrrol-2-yl)-2-[(thieno[2,3-d]pyrimidin-4-yl)oxy]ethan-1-one
-
1-(2-phenylpyrimidin-4-yl)-N-[(4-propoxyphenyl)methyl]piperidine-4-carboxamide
-
1-(3-chlorophenyl)-5-ethyl-N-(4H-1,2,4-triazol-3-yl)-1H-pyrazole-4-carboxamide
-
1-[(2-chlorophenyl)methyl]-N-(4H-1,2,4-triazol-3-yl)-1H-pyrazole-4-carboxamide
-
1-[7-(3,4-dimethylbenzoyl)-2H-[1,3]dioxolo[4,5-g]quinolin-8-yl]piperidine-4-carboxamide
-
2-((6-(3-amino-1H-pyrazol-5-yl)-1H-indol-1-yl)methyl)-benzamide
-
-
2-((6-(3-amino-1H-pyrazol-5-yl)-1H-indol-1-yl)methyl)-benzonitrile
-
-
2-(1H-inden-2-yl)-5-[2-(1H-indol-3-yl)ethyl]-4-methyl-1H-pyrazolo[4,3-c]pyridine-3,6(2H,5H)-dione
-
2-(5-chlorothiophen-2-yl)-2-oxoethyl (3,4-dimethoxyphenyl)acetate
-
2-(8-fluoro-3,4-dihydroquinolin-1(2H)-yl)-N-(quinolin-5-yl)acetamide
-
2-oxo-2-(2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)ethyl 2-methylquinoline-4-carboxylate
-
2-oxo-2-(2-oxo-2,3-dihydro-1H-benzimidazol-5-yl)ethyl 3-(cyclopropylsulfamoyl)thiophene-2-carboxylate
-
2-oxo-2-(3-sulfamoylanilino)ethyl 2-(furan-2-yl)quinoline-4-carboxylate
-
2-oxo-2-[(quinolin-5-yl)amino]ethyl 1-(5-carbamoylpyridin-2-yl)piperidine-4-carboxylate
-
2-phenyl-7-(quinoline-6-carbonyl)-5,6,7,8-tetrahydropyrazolo[1,5-a]pyrido[4,3-d]pyrimidin-9(1H)-one
-
2-[(3,5-dichloropyridin-2-yl)amino]-2-oxoethyl 5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxylate
-
2-[(5-chloropyridin-2-yl)amino]-2-oxoethyl 2-(furan-2-yl)quinoline-4-carboxylate
-
2-[2-(1-methyl-2-phenyl-2,3-dihydro-1H-indol-3-yl)-2-oxoethyl]-1,3-dioxo-1,2,3,5,6,7-hexahydropyrrolo[1,2-c]pyrimidine-4-carbonitrile
-
2-[2-(4-oxocinnolin-1(4H)-yl)acetamido]-5,6-dihydro-4H-cyclopenta[b]thiophene-3-carboxamide
-
2-[3-(benzenesulfonyl)-7-methyl-4-oxo-1,8-naphthyridin-1(4H)-yl]-N-methyl-N-phenylacetamide
-
2-[5-[2-(methylamino)-1,3-thiazol-4-yl]thiophen-2-yl]acetamide
-
3-(1H-pyrrol-1-yl)-N-[4-[(1,3-thiazol-2-yl)sulfamoyl]phenyl]benzamide
-
3-(4-methoxyphenyl)-7-[(1H-pyrrol-2-yl)methyl]-5,6,7,8-tetrahydro[1,2,4]triazolo[4,3-a]pyrazine
-
3-amino-5-(1-((1-methylpiperidin-2-yl)methyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-((1-methylpiperidin-3-yl)methyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-((2-hydroxypyridin-3-yl)methyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-((6-hydroxypyridin-3-yl)methyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-(4-((4-isopropylpiperazin-1-yl)methyl)-benzyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-(4-(morpholinomethyl)benzyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-(4-(piperidin-1-ylmethyl)benzyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-(pyridin-3-ylmethyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-(pyridin-4-ylmethyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(1-(quinolin-4-ylmethyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-(3-chloro-1-(pyridin-3-ylmethyl)-1H-indol-6-yl)-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-[1-([4-[(4-methylpiperazin-1-yl)methyl]phenyl]methyl)-1H-indol-6-yl]-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-[1-([4-[(pyrrolidin-1-yl)methyl]phenyl]methyl)-1H-indol-6-yl]-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-[1-([5-[(pyrrolidin-1-yl)methyl]pyridin-2-yl]methyl)-1H-indol-6-yl]-1H-pyrazole-4-carbonitrile
-
-
3-amino-5-[1-[(pyridin-2-yl)methyl]-1H-indol-6-yl]-1H-pyrazole-4-carbonitrile
-
-
3-methoxy-5-(pyridin-3-ylmethyl)benzyl-1H-pyrazole-4-carboxylate
-
-
3-oxo-N-(5,6,7,8-tetrahydronaphthalen-1-yl)-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
-
3-oxo-N-[1-[4-(1H-1,2,4-triazol-1-yl)phenyl]ethyl]-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
-
3-oxo-N-[[2-(thiophen-2-yl)-1,3-oxazol-4-yl]methyl]-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
-
4-((4-azidobenzyl)oxy)-N-(4-((octylamino)methyl)benzyl)thieno-[2,3-d]pyrimidine-5-carboxamide
-
-
4-(hexyloxy)-N-(4-((octylamino)methyl)benzyl)thieno[2,3-d]-pyrimidine-5-carboxamide
-
-
4-methoxy-N-(4-(morpholinomethyl)benzyl)thieno[2,3-d]-pyrimidine-5-carboxamide
-
-
4-methyl-5-(1-(4-(pyrrolidin-1-ylmethyl)benzyl)-1H-indol-6-yl)-1H-pyrazol-3-amine
-
-
4-oxo-N-(4-((pentylamino)methyl)benzyl)-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
-
-
4-oxo-N-(4-(piperidin-1-ylmethyl)benzyl)-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
4-[3-(8-hydroxyimidazo[1,2-a]pyridin-2-yl)-2,5-dimethyl-1H-pyrrol-1-yl]benzene-1-sulfonamide
-
5,7-dimethyl-N-(4H-1,2,4-triazol-3-yl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
-
5-(1-(4-(piperidin-1-ylmethyl)benzyl)-1H-indol-6-yl)-1H-pyrazol-3-amine
-
-
5-[1-([4-[(pyrrolidin-1-yl)methyl]phenyl]methyl)-1H-indol-6-yl]-1H-pyrazol-3-amine
-
-
5-[2-(1,4-dioxa-8-azaspiro[4.5]decan-8-yl)-2-oxoethyl]-2-(3-fluorophenyl)-7-methyl-3-(1H-pyrrol-1-yl)-2,3,3a,5-tetrahydro-4H-pyrazolo[3,4-d]pyridazin-4-one
-
6-(2-[[(furan-2-yl)methyl]amino]-1,3-thiazol-4-yl)-3,4-dihydroquinolin-2(1H)-one
-
6-[5-(thiophen-2-yl)-1,2,4-oxadiazol-3-yl][1,2,4]triazolo[4,3-a]pyridine
-
ethyl 1-(3-(3-(((1H-pyrazole-4-carbonyl)oxy)methyl)-5-methoxyphenyl)prop-2-yn-1-yl)-1H-pyrazole-4-carboxylate
-
-
glycerol
the Escherichia coli TRmD performs best in the absence of glycerol, its activity decresaing linearly with increasing glycerol concentrations. No activity at 50% glycerol
N-(2-methoxy-5-methylphenyl)-N'-[1,2,4]triazolo[4,3-a]pyridin-3-ylurea
-
N-(3,4-dimethylphenyl)-5,6-dihydro-4H-cyclopenta[d][1,2]oxazole-3-carboxamide
-
N-(3-acetylphenyl)-N2-[5-chloro-2-(pyrrolidin-1-yl)phenyl]glycinamide
-
N-(3-carbamoyl-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-chloropyridine-2-carboxamide
-
N-(3-carbamoylthiophen-2-yl)-2-(pyridin-4-yl)quinoline-4-carboxamide
-
N-(3-cyanothiophen-2-yl)-2-(furan-2-yl)quinoline-4-carboxamide
-
N-(4-((((3s,5s,7s)-adamantan-1-yl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-(((2-(2-(2-aminoethoxy)ethoxy)ethyl)amino)methyl)-benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-(((2-(2-ethoxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-(((2-(2-hydroxyethoxy)ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-(((4-aminobutyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide dihydrochloride
-
-
N-(4-(((5-(1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)pentyl)amino) methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-(((5-aminopentyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-(((7-aminohexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((1,5-dihydroxy-4-oxo-1,4-dihydropyridine-2-carboxamido)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]-pyrimidine-5-carboxamide
-
-
N-(4-((benzyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((benzyl(hexyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((benzyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((benzylamino)methyl)benzyl)-4-(hexyloxy)thieno[2,3-d]-pyrimidine-5-carboxamide
-
-
N-(4-((benzylamino)methyl)benzyl)-4-methoxythieno[2,3-d]-pyrimidine-5-carboxamide
-
-
N-(4-((benzylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((benzylamino)methyl)benzyl)-4-propoxythieno[2,3-d]-pyrimidine-5-carboxamide
-
-
N-(4-((butylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
N-(4-((cyclohexylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((decylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((diethylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
-
enzyme-bound crystal structure, overview
N-(4-((dodecylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno-[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((ethyl(octyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((octylamino)methyl)benzyl)-4-moxythieno[2,3-d]-pyrimidine-5-carboxamide
-
-
N-(4-((octylamino)methyl)benzyl)-4-propoxythieno[2,3-d]-pyrimidine-5-carboxamide
-
-
N-(4-(morpholinomethyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-(morpholinomethyl)benzyl)-4-propoxythieno[2,3-d]-pyrimidine-5-carboxamide
-
-
N-([1-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]piperidin-4-yl]methyl)-1H-indole-2-carboxamide
-
N-([2-[(morpholin-4-yl)methyl]phenyl]methyl)-2-(thiophene-2-carbonyl)benzamide
-
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
N-methyl-1-[2-([[2-(pyridin-3-yl)quinazolin-4-yl]amino]methyl)phenyl]methanesulfonamide
-
N-methyl-N-[[2-(pyrrolidin-1-yl)phenyl]methyl]-3-(1H-pyrrol-1-yl)benzamide
-
N-[(3,5-dimethyl-1,2-oxazol-4-yl)methyl]quinoline-6-carboxamide
-
N-[1-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]piperidin-3-yl]-1H-indole-2-carboxamide
-
N-[1-[3-(pyridin-4-yl)-1H-pyrazol-5-yl]piperidin-3-yl]-2-(thiophen-2-yl)acetamide
-
N-[2-oxo-2-[(1,3,5-trimethyl-4,5-dihydro-1H-pyrazol-4-yl)amino]ethyl]-5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxamide
-
N-[3-(pyridin-4-yl)-1,2-oxazol-5-yl]-5,6,7,8-tetrahydronaphthalene-2-sulfonamide
-
N-[3-([1,3]thiazolo[5,4-b]pyridin-2-yl)phenyl]quinoline-2-carboxamide
-
N-[3-[(3-fluoro-4-methylphenyl)carbamoyl]phenyl]-1-([1,3]thiazolo[5,4-b]pyridin-2-yl)piperidine-3-carboxamide
-
N-[4-(2-amino-2-oxoethyl)-1,3-thiazol-2-yl]-3-(3,5-dimethyl-1-phenyl-1H-pyrazol-4-yl)propanamide
-
N-[4-chloro-3-(pyrrolidine-1-sulfonyl)phenyl]-3-oxo-3,4-dihydro-2H-1,4-benzoxazine-6-carboxamide
-
N-[[4-(piperidine-1-carbonyl)phenyl]methyl]-2-(thiophene-2-carbonyl)benzamide
-
[4-(hydroxymethyl)-2,8-diazaspiro[4.5]decan-2-yl][1-(4-methoxyphenyl)cyclohexyl]methanone
-
[5-(furan-2-yl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]methyl pyrazine-2-carboxylate
-
DTT
TrmD has maximal activity below 1 mM DTT and loses 20% of its activity above that value
DTT
TRM5 displays maximal activity above 1 mM DTT and loses 20% of its activity below that value
KCl
TRM5 enzyme is stimulated 4fold by 100 mM KCl. TRM5 tends to lose all activity in 600 mM KCl
N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
enzyme-bound crystal structure, overview
N-(4-((cyclohexyl(ethyl)amino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
enzyme-bound crystal structure, overview
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
enzyme-bound crystal structure, overview
N-(4-((octylamino)methyl)benzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
the binding of AZ51 does not induce the side chain flip of Tyr111 in MtbTrmD, while the corresponding residue Tyr120 in PaTrmD turned 180° to form stacking interactions with the phenyl ring of the inhibitor, enzyme-bound crystal structure, overview
-
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
i.e. AZ51, inhibitor binding induces conformational changes of the wall loop, whereupon the side chain of aromatic ring of Tyr120 flips about 180° and forms stacking interactions with both the phenyl and piperidine rings of AZ51. This feature appears unique to AZ51 and P
-
N-([4-[(4-aminopiperidin-1-yl)methyl]phenyl]methyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-5-carboxamide
-
-
-
S-adenosyl-L-homocysteine
-
an S-adenosyl-L-methionine analogue
sinefungin
an active-site inhibitor and S-adenosyl-L-methionine (SAM) analogue, that binds at the N-terminal dommain in the SAM binding site. Structure analysis of crystallized isolated dimeric NTD, overview
sinefungin
and isosteric SAM analogue in which the methyl group of SAM is replaced by an amino group and the sulfur by a carbon atom, competitive inhibition with respect to SAM and uncompetitive for tRNA. A set of crystal structures of the homodimeric PaTrmD protein bound to SAM and sinefungin provide the molecular basis for enzyme competitive inhibition and identify the location of the bound divalent ion. Crystal structure of PaTrmD bound to the SAM-competitive inhibitor sinefungin (SFG) is refined at a resolution of 2.45 A. In order to unambiguously locate the divalent ion, a third structure where crystals of PaTrmD are soaked with Mn2+ and SFG is determined. One Mn2+ near each of the bound sinefungin can be built. Mn2+ is coordinated by side-chain carbonyl group of E173', carboxylic groups of E121, D174' and D182' and the nitrogen atom of the sinefungin tail
additional information
-
fragments of S-adenosyl-L-methionine, adenosine and methionine, are selectively inhibitory of TrmD, while they are poor inhibitors for Trm5 from Methanocaldococcus jannaschii
-
additional information
-
fragments of S-adenosyl-L-methionine, adenosine and methionine, are poor inhibitors of Trm5, while they are selectve inhibitors for TrmD from Escherichia coli
-
additional information
-
synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, overview. The tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA
-
additional information
-
development of inhibitors against Mycobacterium abscessus tRNA (m1G37) methyltransferase (TrmD) using fragment-based approaches, inhibitor screening, overview. Determination of inhibitor thermodynamics and binding kinetics
-
additional information
high-throughput small-molecule library inhibitor screening, antibacterial growth inhibitory activities and haemolytic activity of selected TrmD inhibitors, binding affinity confirmed by thermal stability and surface plasmon resonance, overview
-
additional information
-
high-throughput small-molecule library inhibitor screening, antibacterial growth inhibitory activities and haemolytic activity of selected TrmD inhibitors, binding affinity confirmed by thermal stability and surface plasmon resonance, overview
-
additional information
the N-terminal domain is a useful construct to probe the molecular interactions with SAM competitive inhibitors, in the search for molecules with antibiotic activity
-
additional information
-
the N-terminal domain is a useful construct to probe the molecular interactions with SAM competitive inhibitors, in the search for molecules with antibiotic activity
-
additional information
-
synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, nanomolar potency against TrmD in vitro, overview. This tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA. Biochemical structure-activity relationships (SAR) for TrmD inhibitors, the thienopyrimidinone substituent flexibility is critical for potent TrmD inhibition. Analysis of hemolytic activity of the compounds. Effect of side chain length of 15 analogues
-
additional information
-
synthesis of thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism, overview. The tyrosine-flipping mechanism is uniquely found in Pseudomonas aeruginosa TrmD and renders the enzyme inaccessible to the cofactor S-adenosyl-L-methionine (SAM) and probably to the substrate tRNA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycerol
TRM5 performs best between 25 and 30% glycerol, and is less active at lower concentrations. The enzyme retains 45% of its activity in the presence of 50% glycerol
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Methyl-accepting RNA in 13762 mammary adenocarcinoma correlated with low adenine methyltransferase levels.
Carcinogenesis
Chromosome 8 BAC array comparative genomic hybridization and expression analysis identify amplification and overexpression of TRMT12 in breast cancer.
Carcinoma
A human tRNA methyltransferase 9-like protein prevents tumour growth by regulating LIN9 and HIF1-?.
Carcinoma, Hepatocellular
Composition, associated tissue methyltransferase activity, and catabolic end products of transfer RNA from carcinogen-induced hepatoma and normal monkey livers.
Diabetes Mellitus
tRNA methyltransferase homologue gene TRMT10A mutation in young adult-onset diabetes with intellectual disability, microcephaly and epilepsy.
Epilepsy
tRNA methyltransferase 10 homologue A (TRMT10A) mutation in a Chinese patient with diabetes, insulin resistance, intellectual deficiency and microcephaly.
Epilepsy
tRNA methyltransferase homologue gene TRMT10A mutation in young adult-onset diabetes with intellectual disability, microcephaly and epilepsy.
Infections
Alteration in tRNA methyltransferase activity in mengovirus infection: host range specificity.
Insulin Resistance
tRNA methyltransferase 10 homologue A (TRMT10A) mutation in a Chinese patient with diabetes, insulin resistance, intellectual deficiency and microcephaly.
Intellectual Disability
Expanding the Phenotype of TRMT10A Mutations: Case Report and a Review of the Existing Cases.
Intellectual Disability
Mutations in the tRNA methyltransferase 1 gene TRMT1 cause congenital microcephaly, isolated inferior vermian hypoplasia and cystic leukomalacia in addition to intellectual disability.
Intellectual Disability
TRMT1-catalyzed tRNA modifications are required for redox homeostasis to ensure proper cellular proliferation and oxidative stress survival.
Intellectual Disability
TRMT10A mutation in a child with diabetes, short stature, microcephaly and hypoplastic kidneys.
Intellectual Disability
tRNA methyltransferase 10 homologue A (TRMT10A) mutation in a Chinese patient with diabetes, insulin resistance, intellectual deficiency and microcephaly.
Intellectual Disability
tRNA methyltransferase homologue gene TRMT10A mutation in young adult-onset diabetes with intellectual disability, microcephaly and epilepsy.
Leukemia
Differences in activity of N2-guanine tRNA methyltransferase II among several inbred strains of mice.
Microcephaly
Expanding the Phenotype of TRMT10A Mutations: Case Report and a Review of the Existing Cases.
Microcephaly
Mutations in the tRNA methyltransferase 1 gene TRMT1 cause congenital microcephaly, isolated inferior vermian hypoplasia and cystic leukomalacia in addition to intellectual disability.
Microcephaly
Pancreatic ?-cell tRNA hypomethylation and fragmentation link TRMT10A deficiency with diabetes.
Microcephaly
TRMT10A mutation in a child with diabetes, short stature, microcephaly and hypoplastic kidneys.
Microcephaly
tRNA methyltransferase 10 homologue A (TRMT10A) mutation in a Chinese patient with diabetes, insulin resistance, intellectual deficiency and microcephaly.
Microcephaly
tRNA methyltransferase homolog gene TRMT10A mutation in young onset diabetes and primary microcephaly in humans.
Microcephaly
tRNA methyltransferase homologue gene TRMT10A mutation in young adult-onset diabetes with intellectual disability, microcephaly and epilepsy.
Neoplasms
A human tRNA methyltransferase 9-like protein prevents tumour growth by regulating LIN9 and HIF1-?.
Neoplasms
A system of RNA modifications and biased codon use controls cellular stress response at the level of translation.
Neoplasms
Methyl-accepting RNA in 13762 mammary adenocarcinoma correlated with low adenine methyltransferase levels.
Neoplasms
Somatic cancer mutations in the DNMT2 tRNA methyltransferase alter its catalytic properties.
Ovarian Neoplasms
Association of tRNA methyltransferase NSUN2/IGF-II molecular signature with ovarian cancer survival.
Ovarian Neoplasms
Ovarian cancer proliferation and apoptosis are regulated by human transfer RNA methyltransferase 9-likevia LIN9.
Retinoblastoma
Ovarian cancer proliferation and apoptosis are regulated by human transfer RNA methyltransferase 9-likevia LIN9.
Starvation
Retrograde nuclear import of tRNA precursors is required for modified base biogenesis in yeast.
Vitamin A Deficiency
The effect of vitamin A deficiency on testicular transfer RNA methyltransferase activity.
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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
0.003
S-adenosyl-L-methionine
pH 7.5, 37°C, recombinant enzyme
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
guanine37 in Methanocaldococcus jannaschii tRNA(Cys)
pH 8.0, 50°C
-
0.078
guanine37 in tRNAArg
-
pH 8.0, temperature not specified in the publication
-
0.36
guanine37 in tRNAGlnG36A, guanine37 in tRNAGlnG36C
-
pH 8.0, temperature not specified in the publication
-
0.17
guanine37 in tRNAGlnG36U
-
pH 8.0, temperature not specified in the publication
-
0.0113
guanine37 in tRNALeu(CAG)
pH and temperature not specified in the publication
-
0.217
guanine37 in tRNALeu(GAG)
pH 7.5, 37°C, recombinant enzyme
-
0.13
guanine37 in tRNAPro
-
pH 8.0, temperature not specified in the publication
-
0.0001
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme P267A
-
0.0003
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme D223A
-
0.0013
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme N265A
-
0.0013
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme Y176A
-
0.0015
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme G205A/G207A
-
0.0018
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme P226A
-
0.003
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme R144A
-
0.0037
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, wild-type enzyme
-
0.0086
guanine37 in Methanocaldococcus jannaschii tRNAPro
pH 8.0, 52°C
-
0.0014
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.0047
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.24
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.34
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.049
guanine37 in tRNALeu
recombinant wild-type enzyme, pH 8.0, 30°C
-
0.093
guanine37 in tRNALeu
recombinant wild-type enzyme, pH 8.0, 37°C
-
0.13
guanine37 in tRNALeu
recombinant wild-type enzyme, pH 8.0, 43°C
-
0.32
guanine37 in tRNALeu
-
pH 8.0, temperature not specified in the publication
-
0.0001
S-adenosyl-L-methionine
pH 8.0, 50°C, mutant enzyme P267A
0.0105
S-adenosyl-L-methionine
pH and temperature not specified in the publication
0.012
S-adenosyl-L-methionine
pH 8.0, 50°C, wild-type enzyme
0.02
S-adenosyl-L-methionine
-
kcat in steady-state phase turnover, pH and temperature not specified in the publication
0.09
S-adenosyl-L-methionine
-
pH and temperature not specified in the publication
0.217
S-adenosyl-L-methionine
pH 7.5, 37°C, recombinant enzyme
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
-
0.12 is kchem in the first rapid burst turnover
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
36.9
guanine37 in Methanocaldococcus jannaschii tRNA(Cys)
pH 8.0, 50°C
-
29
guanine37 in tRNAArg
-
pH 8.0, temperature not specified in the publication
-
130
guanine37 in tRNAGlnG36A
-
pH 8.0, temperature not specified in the publication
-
2
guanine37 in tRNAGlnG36C
-
pH 8.0, temperature not specified in the publication
-
15
guanine37 in tRNAGlnG36U
-
pH 8.0, temperature not specified in the publication
-
9.44
guanine37 in tRNALeu(CAG)
pH and temperature not specified in the publication
-
270.8
guanine37 in tRNALeu(GAG)
pH 7.5, 37°C, recombinant enzyme
-
130
guanine37 in tRNAPro
-
pH 8.0, temperature not specified in the publication
-
0.017
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme P267A
-
0.11
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme D223A
-
0.16
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme N265A
-
0.32
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme G205A/G207A
-
0.51
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme N225A
-
0.53
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme Y176A
-
0.61
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme P226A
-
0.775
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, mutant enzyme R144A
-
11.9
guanine37 in Methanocaldococcus jannaschii tRNACys
pH 8.0, 50°C, wild-type enzyme
-
7.22
guanine37 in Methanocaldococcus jannaschii tRNAPro
pH 8.0, 52°C
-
0.000078
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.022
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
0.07
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
280
guanine37 in tRNAGlnCUG
-
pH 8.0, temperature not specified in the publication
-
5.99
guanine37 in tRNALeu
recombinant wild-type enzyme, pH 8.0, 43°C
-
20.42
guanine37 in tRNALeu
recombinant wild-type enzyme, pH 8.0, 30°C
-
30
guanine37 in tRNALeu
recombinant wild-type enzyme, pH 8.0, 37°C
-
40
guanine37 in tRNALeu
-
pH 8.0, temperature not specified in the publication
-
0.2
S-adenosyl-L-methionine
pH 8.0, 50°C, mutant enzyme P267A
5.83
S-adenosyl-L-methionine
pH and temperature not specified in the publication
12.2
S-adenosyl-L-methionine
pH 8.0, 50°C, wild-type enzyme
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
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
5'-[(2-aminoethyl)thio]-5'-deoxy-adenosine
-
pH not specified in the publication, 37°C
0.014
5'-[(2-aminoethyl)thio]-5'-deoxy-adenosine
-
pH not specified in the publication, 55°C
0.461
6-Chloropurine
-
pH not specified in the publication, 55°C
0.0012
methylthioadenosine
-
pH not specified in the publication, 55°C
0.00049
S-adenosyl-L-homocysteine
-
pH not specified in the publication, 55°C
0.0042
S-adenosyl-L-homocysteine
-
pH not specified in the publication, 37°C
44
S-methyl-L-cysteine
-
pH not specified in the publication, 55°C
0.00033
sinefungin
-
pH not specified in the publication, 55°C
0.00041
sinefungin
versus S-adenosyl-L-methionine, pH 7.5, 37°C, recombinant enzyme
0.0064
sinefungin
versus tRNA, pH 7.5, 37°C, recombinant enzyme
additional information
additional information
inhibition kinetics
-