2.1.1.221: tRNA (guanine9-N1)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (guanine9-N1)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.221
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2.1.1.221
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microcephaly
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archaea
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disability
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intellectual
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purine
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stature
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eukarya
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n1-methylation
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monogenic
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puberty
- 2.1.1.221
- microcephaly
- archaea
- disability
-
intellectual
- purine
-
stature
- eukarya
-
n1-methylation
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monogenic
- puberty
Reaction
Synonyms
EC 2.1.1.31, hTRMT10A, m1G9 methyltransferase, m1G9 MTase, m1R9-specific TkTrm10, More, ScTrm10, SPOUT MTase, TK0422p, TkTrm10, Trm10, Trm10p (ambiguous), TRMT10A, Trmt10C, tRNA (guanine-N(1)-)-methyltransferase, tRNA m1G9 methyltransferase, tRNA m1G9 MTase, tRNA m1G9 SPOUT methyltransferase, tRNA m1R9 methyltransferase, tRNA(m1G9/m1A9)-methyltransferase, tRNA(m1G9/m1A9)MTase
ECTree
2.1.1.221 tRNA (guanine9-N1)-methyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.1.1.221 - tRNA (guanine9-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 + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
S-adenosyl-L-methionine + guanine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
S-adenosyl-L-methionine + guanine9 in tRNAAsp
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAAsp
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNACysGCA
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
S-adenosyl-L-methionine + guanine9 in tRNAGlyCCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyCCC
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
S-adenosyl-L-methionine + guanine9 in tRNALeuCAA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuCAA
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALeuGAG
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuGAG
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALysCUU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALysCUU
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe
S-adenosyl-L-methionine + guanine9 in tRNAPhe(G9)
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe(G9)
S-adenosyl-L-methionine + guanine9 in tRNAThrAGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrAGU
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAThrCGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrCGU
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNATrp
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNATrp
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
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?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
TRM10 is required for the catalysis of at least 9 of the 10 m1G modifications observed (tRNA(Trp), tRNA(Pro), tRNA(Val), tRNAi(Met), tRNA(Ile), tRNAICG(Arg), and both tRNAUCU(Arg) species) at position 9 in yeast. It is likely that Trm10p is also responsible for modification of G9 of tRNAAla
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
the enzyme is specific for guanine9 in tRNA, does not catalyse methylation of adenine9 in tRNA
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA
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-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
formation of N1-methylguanine9 in tRNA(Asp) from Thermococcus kodakaraensis that contains a guanosine 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 + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
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-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
tRNA substrate from Thermococcus kodakarensis
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAArg
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
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tRNA substrate from Thermococcus kodakarensis
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
tRNA from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
tRNA from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
tRNA from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
tRNA substrate from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
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tRNA substrate from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
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?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
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?
S-adenosyl-L-methionine + guanine9 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe
tRNA substrate from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe
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tRNA substrate from Saccharomyces cerevisiae
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?
S-adenosyl-L-methionine + guanine9 in tRNAPhe(G9)
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe(G9)
tRNA from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAPhe(G9)
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe(G9)
tRNA from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAPhe(G9)
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAPhe(G9)
tRNA from Saccharomyces cerevisiae
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-
?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
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-
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?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
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?
additional information
?
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substrate specificity analysis in vivo, overview
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?
additional information
?
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substrate specificity analysis and comparison of hTRMT10A and hTRMT10B enzymes, overview. hTRMT10A and hTRMT10B catalyze methylation of different tRNA substrates. hTRMT10A displays robust activity on every tested G9-containing tRNA from either humans or Saccharomyces cerevisiae, similar to Saccharomyces cerevisiae ScTrm10. 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. hTRMT10A and hTRMT10B catalyze methylation of different tRNA substrates. hTRMT10A displays robust activity on every tested G9-containing tRNA from either humans or Saccharomyces cerevisiae, similar to Saccharomyces cerevisiae ScTrm10. 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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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
?
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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
?
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the human Trmt10A enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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the human Trmt10A enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
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?
additional information
?
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there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
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?
additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
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the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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-
additional information
?
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the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
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the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
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?
additional information
?
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the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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additional information
?
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the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218
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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
?
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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
?
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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
?
-
-
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
?
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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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