Any feedback?
Literature summary for 2.1.1.204 extracted from
- DNA methyltransferase homologue TRDMT1 in Plasmodium falciparum specifically methylates endogenous aspartic acid tRNA (2017), Biochim. Biophys. Acta, 1860, 1047-1057 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene DNMT2, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3) | Plasmodium falciparum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of enzyme mutant Pf-NDELTATRDMT1 lacking the N-terminus. The Pf-NDELTATRDMT1 protein consists of motifs specific for both DNA and tRNA methyltransferases, substrate specificity analysis reveals that no DNA methylation activity can be detected, but Pf-NDELTATRDMT1 methylates only tRNA-Asp and very weakly tRNA-Val | Plasmodium falciparum |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Plasmodium falciparum |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Plasmodium falciparum | the DNA methyltransferase homologue TRDMT1 in Plasmodium falciparum specifically methylates endogenous aspartic acid tRNA | ? | - |
- |
|
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | Plasmodium falciparum | - |
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Plasmodium falciparum | Q8IBI4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and dialysis | Plasmodium falciparum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the DNA methyltransferase homologue TRDMT1 in Plasmodium falciparum specifically methylates endogenous aspartic acid tRNA | Plasmodium falciparum | ? | - |
- |
|
| additional information | no activity with DNA and other tRNA substrates. Plasmodium falciparum has two isodecoders for valine tRNA, and the very low activity is seen on valine 1 substrate, whereas no activity can be detected on valine 2 tRNA substrate. Purified Pf-TRDMT1 methylates tRNA-Asp at C38 position | Plasmodium falciparum | ? | - |
- |
|
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | - |
Plasmodium falciparum | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAAsp | assay with tritium-labeled SAM, specific for tRNAAsp | Plasmodium falciparum | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp | - |
? | |
| S-adenosyl-L-methionine + cytosine38 in tRNAVal | assay with tritium-labeled SAM, very low activity | Plasmodium falciparum | S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAVal | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Pf-DNMT2 | - |
Plasmodium falciparum |
| TRDMT1 | - |
Plasmodium falciparum |
| tRNA aspartic acid methyltransferase 1 | - |
Plasmodium falciparum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Plasmodium falciparum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | 8 | assay at | Plasmodium falciparum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Plasmodium falciparum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | phylogenetic analysis revealed that Plasmodium falciparum TRDMT1 clusters into tRNA specific methyltransferase family. The enzyme structure harbors all the essential motifs for C5 DNA methylation activity as well as tRNA methylation | Plasmodium falciparum |
| physiological function | TRDMT1, a conserved homolog of DNA methyltransferase DNMT2, specifically methylates endogenous aspartic acid tRNA, but not DNA. TRDMT1 mediated C38 methylation of aspartic acid tRNA might play a critical role by translational regulation of important proteins and modulate the pathogenicity of the malarial parasite. Methylation of aspartic acid tRNA can modulate Plasmodium falciparum pathogenicity through translational regulation of functionally important proteins. 5-Methyl cytosines are present only on the RNA and not on the DNA of Plasmodium falciparum | Plasmodium falciparum |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
