2.1.1.218: tRNA (adenine9-N1)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (adenine9-N1)-methyltransferase, go to the full flat file.
Reaction
Synonyms
adenosine-specific Trm10, EC 2.1.1.36, hTRMT10B, m1A9 MTase, m1R9-specific TkTrm10, More, SaTrm10, SPOUT MTase, TK0422p, TkTrm10, Trm10, Trm10p (ambiguous), TRMT10B, Trmt10C, tRNA m1A9 methyltransferase, tRNA m1A9 MTase, tRNA m1A9-methyltransferase, tRNA m1R9 methyltransferase, tRNA(m1G9/m1A9)-methyltransferase, tRNA(m1G9/m1A9)MTase
ECTree
2.1.1.218 tRNA (adenine9-N1)-methyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.1.1.218 - tRNA (adenine9-N1)-methyltransferase
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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 + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
S-adenosyl-L-methionine + adenine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAArg
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-
-
?
S-adenosyl-L-methionine + adenine9 in tRNAAsp
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAAsp
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-
-
?
S-adenosyl-L-methionine + adenine9 in tRNAiMet
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAiMet
S-adenosyl-L-methionine + adenine9 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAPhe
tRNA substrate from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + adenine9 in tRNAThr
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAThr
tRNA substrate from Thermococcus kodakarensis
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-
?
S-adenosyl-L-methionine + adenine9 in tRNATrp
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNATrp
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-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
all the T-armless tRNAs possess 1-methyladenosine at position 9. This modification is structurally and functionally important for tRNAs in Ascaris suum mitochondria
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?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
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-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
the Watson-Crick base-pair-disrupting methyl group N1-methyladenine9 is sufficient for cloverleaf folding of human mitochondrial tRNALys
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-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
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-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
the enzyme is specific for adenine9 in tRNA, does not catalyse the methylation of guanine9 in tRNA from Saccharomyces cerevisiae. No m1A is formed in a mutant of the tRNAMeti where position 9 is occupied by a guanosine (tRNAMeti A9G)
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-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA
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-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
formation of N1-methyladenosine9 in tRNAAla from Thermococcus kodakaraensis that contains an adenine at position 9. The enzyme forms approximately the same amount of m1A and m1G when the tRNA of the yeast strain Y16243 is used as substrate. Given that occurrence of A9 and G9 in this tRNA population is almost equal (about 50% each) this result indicates that the enzyme TK0422p does not show any preference for one of these two nucleosides. The ratio m1A/m1G formed from Escherichia coli tRNA is higher than that with tRNA from the yeast Y16243 strain. This is consistent with the fact that there are about two times more tRNAs with A9 than with G9 in Escherichia coli. The enzyme is active in a pH range 5.5-9.75. The intensity of m1A and m1G spots varies greatly as a function of the pH. At pH 5.5, m1A MTase activity of TK0422p is predominant over m1G. At pH 7 or higher, both m1A and m1G are detected, m1G intensity growing with increasing pH
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-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
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-
-
?
S-adenosyl-L-methionine + adenine9 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + adenine9 in tRNAiMet
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAiMet
docking model of tRNAiMet of Sulfolobus acidocaldarius onto SaTrm10-SAH
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-
?
S-adenosyl-L-methionine + adenine9 in tRNAiMet
S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNAiMet
docking model of tRNAiMet of Sulfolobus acidocaldarius onto SaTrm10-SAH
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-
?
additional information
?
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substrate specificity analysis and comparison of hTRMT10A and hTRMT10B enzymes, overview. Purified hTRMT10B lacks m1G9 methyltransferase activity with several tested Saccharomyces cerevisiae and human tRNA substrates. hTRMT10A and hTRMT10B catalyze methylation of different tRNA substrates. hTRMT10B displays only very weak m1G9 activity on two substrates, human tRNAArg and tRNATrp, with no detectible activity on any other G9-containing tRNA. hTRMT10B, and not hTRMT10A, is indeed capable of catalyzing m1A9 methylation on tRNAAsp in vitro, while hTRMT10B has the sole responsibility for generating the m1A9 modification. hTRMT10A displays higher in vitro catalytic rates than hTRMT10B
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additional information
?
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substrate specificity analysis and comparison of hTRMT10A and hTRMT10B enzymes, overview. Purified hTRMT10B lacks m1G9 methyltransferase activity with several tested Saccharomyces cerevisiae and human tRNA substrates. hTRMT10A and hTRMT10B catalyze methylation of different tRNA substrates. hTRMT10B displays only very weak m1G9 activity on two substrates, human tRNAArg and tRNATrp, with no detectible activity on any other G9-containing tRNA. hTRMT10B, and not hTRMT10A, is indeed capable of catalyzing m1A9 methylation on tRNAAsp in vitro, while hTRMT10B has the sole responsibility for generating the m1A9 modification. hTRMT10A displays higher in vitro catalytic rates than hTRMT10B
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additional information
?
-
the human Trm10C enzyme is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA
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-
additional information
?
-
model for substrate tRNA binding by SaTrm10, in silico tRNA-SaTrm10 docking, role of Asp184 and Asp220 in the catalytic mechanism of SaTrm10, tRNA binding mechanism, overview
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-
additional information
?
-
the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221
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-
additional information
?
-
the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221
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additional information
?
-
model for substrate tRNA binding by SaTrm10, in silico tRNA-SaTrm10 docking, role of Asp184 and Asp220 in the catalytic mechanism of SaTrm10, tRNA binding mechanism, overview
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-
additional information
?
-
the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221
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-
additional information
?
-
the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221
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-
additional information
?
-
the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221
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-
additional information
?
-
the archaeal Trm10 enzyme does not exhibit activity on guanine9 residues in tRNA, no activity of EC 2.1.1.221
-
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-
additional information
?
-
the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA
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-
additional information
?
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usage of [alpha-32P]-labeled tRNA substrates. The enzyme shows activity with both guanine9 and adenine9 containing tRNAs for methylation on N1. Bifunctional enzymes (catalyzing both m1A9 and m1G9) share the same rate-determining step for methylation as the monofunctional enzyme, these enzymes would also exhibit a different pattern of pH dependence for the two methylation reactions because of the difference in N1 pKa between adenine versus guanine
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-
additional information
?
-
the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA
-
-
-
additional information
?
-
the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA
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