Literature summary for 2.1.1.221 extracted from

Kempenaers, M.; Roovers, M.; Oudjama, Y.; Tkaczuk, K.L.; Bujnicki, J.M.; Droogmans, L.
New archaeal methyltransferases forming 1-methyladenosine or 1-methyladenosine and 1-methylguanosine at position 9 of tRNA (2010), Nucleic Acids Res., 38, 6533-6543.

Search for more literature for 2.1.1.221

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Thermococcus kodakarensis
expression in Escherichia coli	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + guanine9 in tRNA	Saccharomyces cerevisiae	-	S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA	-	?
S-adenosyl-L-methionine + guanine9 in tRNA	Thermococcus kodakarensis	the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA	S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q12400	-	-
Thermococcus kodakarensis	Q5JD38	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Thermococcus kodakarensis
-	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + guanine9 in tRNA	-	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA	-	?
S-adenosyl-L-methionine + guanine9 in tRNA	the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA	Thermococcus kodakarensis	S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA	-	?
S-adenosyl-L-methionine + guanine9 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	Thermococcus kodakarensis	S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA	-	?
S-adenosyl-L-methionine + guanine9 in tRNA	the enzyme is specific for guanine9 in tRNA, does not catalyse methylation of adenine9 in tRNA	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA	-	?

Synonyms

Synonyms	Comment	Organism
TK0422p	-	Thermococcus kodakarensis
Trm10p (ambiguous)	-	Thermococcus kodakarensis
tRNA(m1G9/m1A9)-methyltransferase	-	Thermococcus kodakarensis
tRNA(m1G9/m1A9)MTase	-	Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Saccharomyces cerevisiae
50	-	assay at	Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Thermococcus kodakarensis
8	-	assay at	Saccharomyces cerevisiae

pH Range

pH Minimum	pH Maximum	Comment	Organism
5.5	9.75	the bifunctional 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	Thermococcus kodakarensis

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Release 2023.1 (January 2023)