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Literature summary for 2.1.1.218 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.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.218

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermococcus kodakarensis
expression in Escherichia coli Sulfolobus acidocaldarius

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + adenine9 in tRNA Sulfolobus acidocaldarius
-
 S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
S-adenosyl-L-methionine + adenine9 in tRNA Thermococcus kodakarensis the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius Q4J894
-
-
Thermococcus kodakarensis Q5JD38
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermococcus kodakarensis
-
 Sulfolobus acidocaldarius

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + adenine9 in tRNA
-
 Sulfolobus acidocaldarius S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
S-adenosyl-L-methionine + adenine9 in tRNA the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA Thermococcus kodakarensis S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
S-adenosyl-L-methionine + adenine9 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 Thermococcus kodakarensis S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?
S-adenosyl-L-methionine + adenine9 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) Sulfolobus acidocaldarius S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA
-
 ?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 assay at Thermococcus kodakarensis
50
-
 assay at Sulfolobus acidocaldarius

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Thermococcus kodakarensis
8
-
 assay at Sulfolobus acidocaldarius

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