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Literature summary extracted from

  • Takuma, H.; Ushio, N.; Minoji, M.; Kazayama, A.; Shigi, N.; Hirata, A.; Tomikawa, C.; Ochi, A.; Hori, H.
    Substrate tRNA recognition mechanism of eubacterial tRNA (m1A58) methyltransferase (TrmI) (2015), J. Biol. Chem., 290, 5912-5925.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.220 additional information
-
 additional information kinetics for diverse tRNAPhe variants, overview Thermus thermophilus
2.1.1.220 0.00013
-
 adenine58 in tRNAPhe pH 7.5-8.0, 55°C, wild-type Thermus thermophilus tRNAPhe as substrate Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.220 S-adenosyl-L-methionine + adenine58 in tRNA Thermus thermophilus
-
 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 S-adenosyl-L-methionine + adenine58 in tRNA Thermus thermophilus DSM 7039
-
 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.220 Thermus thermophilus Q8GBB2 HB27
-
2.1.1.220 Thermus thermophilus DSM 7039 Q8GBB2 HB27
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.220 S-adenosyl-L-methionine + adenine58 in tRNA
-
 Thermus thermophilus S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 S-adenosyl-L-methionine + adenine58 in tRNA
-
 Thermus thermophilus DSM 7039 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 S-adenosyl-L-methionine + adenine58 in tRNAGGUThr the tRNA from Thermus thermophilus, that contains C60 instead of U60, is poorly methylated. Nucleoside analysis of tRNAGGUThr from the wild-type strain indicates that less than 50% of tRNAGGUThr contain m1A58 Thermus thermophilus S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 S-adenosyl-L-methionine + adenine58 in tRNAGGUThr the tRNA from Thermus thermophilus, that contains C60 instead of U60, is poorly methylated. Nucleoside analysis of tRNAGGUThr from the wild-type strain indicates that less than 50% of tRNAGGUThr contain m1A58 Thermus thermophilus DSM 7039 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
 ?
2.1.1.220 S-adenosyl-L-methionine + adenine58 in tRNAPhe the Thermus thermophilus tRNAPhe transcript is methylated efficiently by the Thermus thermophilus enzyme, whereas the Saccharomyces cerevisiae tRNAPhe transcript is poorly methylated. Analysis of fourteen chimeric tRNA transcripts derived from these two tRNA reveals that enzyme TrmI recognized the combination of aminoacyl stem, variable region, and T-loop. TrmI methylates deltion transcripts still containing the aminoacyl stem, variable region, and T-arm. Positive sequence determinants are C56, purine 57, A58, and U60. Replacing A58 with inosine and 2-aminopurine completely abrogates methylation, demonstrating that the 6-amino group in A58 is recognized by enzyme TrmI Thermus thermophilus S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNAPhe
-
 ?
2.1.1.220 S-adenosyl-L-methionine + adenine58 in tRNAPhe the Thermus thermophilus tRNAPhe transcript is methylated efficiently by the Thermus thermophilus enzyme, whereas the Saccharomyces cerevisiae tRNAPhe transcript is poorly methylated. Analysis of fourteen chimeric tRNA transcripts derived from these two tRNA reveals that enzyme TrmI recognized the combination of aminoacyl stem, variable region, and T-loop. TrmI methylates deltion transcripts still containing the aminoacyl stem, variable region, and T-arm. Positive sequence determinants are C56, purine 57, A58, and U60. Replacing A58 with inosine and 2-aminopurine completely abrogates methylation, demonstrating that the 6-amino group in A58 is recognized by enzyme TrmI Thermus thermophilus DSM 7039 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNAPhe
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.220 TrmI
-
 Thermus thermophilus
2.1.1.220 tRNA (m1A58) methyltransferase
-
 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.220 55
-
 assay at Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.220 7.5 8 assay at Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.220 S-adenosyl-L-methionine
-
 Thermus thermophilus