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 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Aquifex aeolicus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | - |
- |
- |
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 |
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 | 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 | Comment | Organism |
---|---|---|
multisite-specific tRNA methyltransferase | - |
Aquifex aeolicus |
Trm1 | - |
Aquifex aeolicus |
tRNA (N2,N2-guanine)-dimethyltransferase | - |
Aquifex aeolicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
assay at | Aquifex aeolicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Aquifex aeolicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | binding structure, overview | Aquifex aeolicus |
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 |