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Literature summary for 2.1.1.215 extracted from

  • Awai, T.; Ochi, A.; Ihsanawati, A.; Sengoku, T.; Hirata, A.; Bessho, Y.; Yokoyama, S.; Hori, H.
    Substrate tRNA recognition mechanism of a multisite-specific tRNA methyltransferase, Aquifex aeolicus Trm1, based on the X-ray crystal structure (2011), J. Biol. Chem., 286, 35236-35246.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.215

Protein Variants

Protein Variants Comment Organism
D130A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
D132A site-directed mutagenesis, inactive mutant Aquifex aeolicus
D84A site-directed mutagenesis, almost inactive mutant Aquifex aeolicus
E113A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
E6A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
F134A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
F140A site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Aquifex aeolicus
F27A site-directed mutagenesis, almost inactive mutant Aquifex aeolicus
H110A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
H219A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Aquifex aeolicus
H274A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
I65A site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Aquifex aeolicus
I85A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
K170A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
K283A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
L60A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
N29A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
R179A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Aquifex aeolicus
R192A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
R31A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Aquifex aeolicus
R36A site-directed mutagenesis, inactive mutant Aquifex aeolicus
R66A site-directed mutagenesis, almost inactive mutant Aquifex aeolicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00017
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutant I85A Aquifex aeolicus
0.00017
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant wild-type enzyme Aquifex aeolicus
0.0002
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutant I65A Aquifex aeolicus
0.0003
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutant E6A Aquifex aeolicus
0.0003
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutant N29A Aquifex aeolicus
0.00067
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutants L60A, F140A, and E113A Aquifex aeolicus
0.0008
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutant F134A Aquifex aeolicus
0.0013
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutant D130A Aquifex aeolicus
0.023
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutant F27A Aquifex aeolicus
0.045
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutant R66A Aquifex aeolicus
0.33
-
 S-adenosyl-L-methionine pH 7.5, 55°C, recombinant mutant D84A Aquifex aeolicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Aquifex aeolicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA Aquifex aeolicus
-
 4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA = 4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA reaction mechanism, overview Aquifex aeolicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
-
 Aquifex aeolicus 4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
 ?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA the T-arm in tRNA is the binding site of Trm1, multisite specificity, tRNA-docking modeling, overview Aquifex aeolicus 4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
 ?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe tRNAPhe from yeast Aquifex aeolicus 4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe
-
 ?
additional information Trm1 catalyzes methyl transfers to class II tRNAs as well as all class I tRNAs, the size and sequence of the variable region are not recognized by Aquifex aeolicus Trm1, all tRNA transcripts are methylated. tRNA recognition mechanism of multisite specific Trm1, Asp132 is a catalytic center, structure-function analysis, overview Aquifex aeolicus ?
-
 ?

Subunits

Subunits Comment Organism
More Trm1 from Aquifex aeolicus contains a zinc-cysteine cluster in the C-terminal domain. The N-terminal domain is a typical catalytic domain of S-adenosyl-L-methionine-dependent methyltransferases. Overall structure, structure comparisons, and structure-function analysis, overview Aquifex aeolicus

Synonyms

Synonyms Comment Organism
multisite-specific tRNA methyltransferase
-
 Aquifex aeolicus
Trm1
-
 Aquifex aeolicus
tRNA (N2,N2-guanine)-dimethyltransferase
-
 Aquifex aeolicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
 assay at Aquifex aeolicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Aquifex aeolicus

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine binding structure, overview Aquifex aeolicus

General Information

General Information Comment Organism
evolution archaeal and eukaryotic tRNA (N2,N2-guanine)-dimethyltransferase, Trm1, produces N2,N2-dimethylguanine at position 26 in tRNA. In contrast, Trm1 from Aquifex aeolicus, a hyper-thermophilic eubacterium, modifies G27 as well as G26. The overall structure of Aquifex aeolicus Trm1 is similar to that of archaeal Trm1, although there is a zinc-cysteine cluster in the C-terminal domain of Aquifex aeolicus Trm1 Aquifex aeolicus