Any feedback?
Literature summary for 2.1.1.221 extracted from
- m1A Post-transcriptional modification in tRNAs (2017), Biomolecules, 7, 20 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure PDB ID 4FMW | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-adenosyl-L-methionine + guanine9 in tRNA | Thermococcus kodakarensis | - |
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? |  |
| S-adenosyl-L-methionine + guanine9 in tRNA | Saccharomyces cerevisiae | - |
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | Schizosaccharomyces pombe | - |
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | Homo sapiens | - |
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | Thermococcus kodakarensis JCM 12380 | - |
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | Schizosaccharomyces pombe ATCC 24843 | - |
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | Schizosaccharomyces pombe 972 | - |
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | Saccharomyces cerevisiae ATCC 204508 | - |
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | Thermococcus kodakarensis ATCC BAA-918 | - |
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q7L0Y3 | - |
- |
| Homo sapiens | Q8TBZ6 | - |
- |
| Saccharomyces cerevisiae | Q12400 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | Q12400 | - |
- |
| Schizosaccharomyces pombe | O14214 | - |
- |
| Schizosaccharomyces pombe 972 | O14214 | - |
- |
| Schizosaccharomyces pombe ATCC 24843 | O14214 | - |
- |
| Thermococcus kodakarensis | Q5JD38 | - |
- |
| Thermococcus kodakarensis ATCC BAA-918 | Q5JD38 | - |
- |
| Thermococcus kodakarensis JCM 12380 | Q5JD38 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the human Trm10C enzyme is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA | Homo sapiens | ? | - |
- |
|
| additional information | the human Trmt10A enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 | Homo sapiens | ? | - |
- |
|
| additional information | the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA | Thermococcus kodakarensis | ? | - |
- |
|
| additional information | the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 | Schizosaccharomyces pombe | ? | - |
- |
|
| additional information | the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA | Thermococcus kodakarensis JCM 12380 | ? | - |
- |
|
| additional information | the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 | Schizosaccharomyces pombe ATCC 24843 | ? | - |
- |
|
| additional information | the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 | Schizosaccharomyces pombe 972 | ? | - |
- |
|
| additional information | the yeast Trm10 enzyme does not exhibit activity on adenine9 residues in tRNA, no activity of EC 2.1.1.218 | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | the Trm10 enzyme from Thermococcus kodakarensis is bifunctional and methylates adenine9 (EC 2.1.1.218) and guanine9 (EC 2.1.1.221) residues in tRNA | Thermococcus kodakarensis ATCC BAA-918 | ? | - |
- |
|
| S-adenosyl-L-methionine + guanine9 in tRNA | - |
Thermococcus kodakarensis | S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | - |
Saccharomyces cerevisiae | S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | - |
Schizosaccharomyces pombe | S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | - |
Homo sapiens | S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | - |
Thermococcus kodakarensis JCM 12380 | S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | - |
Schizosaccharomyces pombe ATCC 24843 | S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | - |
Schizosaccharomyces pombe 972 | S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | - |
Saccharomyces cerevisiae ATCC 204508 | S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine9 in tRNA | - |
Thermococcus kodakarensis ATCC BAA-918 | S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| m1G9 MTase | - |
Saccharomyces cerevisiae |
| m1G9 MTase | - |
Schizosaccharomyces pombe |
| m1G9 MTase | - |
Homo sapiens |
| More | see also EC 2.1.1.218 | Thermococcus kodakarensis |
| More | see also EC 2.1.1.218 | Homo sapiens |
| SPOUT MTase | - |
Thermococcus kodakarensis |
| SPOUT MTase | - |
Saccharomyces cerevisiae |
| SPOUT MTase | - |
Homo sapiens |
| Trm10 | - |
Thermococcus kodakarensis |
| Trm10 | - |
Schizosaccharomyces pombe |
| TRMT10A | - |
Saccharomyces cerevisiae |
| TRMT10A | - |
Homo sapiens |
| Trmt10C | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Thermococcus kodakarensis | |
| S-adenosyl-L-methionine | - |
Saccharomyces cerevisiae | |
| S-adenosyl-L-methionine | - |
Schizosaccharomyces pombe | |
| S-adenosyl-L-methionine | - |
Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein | Thermococcus kodakarensis |
| evolution | aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein | Saccharomyces cerevisiae |
| evolution | aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein | Schizosaccharomyces pombe |
| evolution | aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein | Homo sapiens |
| metabolism | the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms | Thermococcus kodakarensis |
| metabolism | the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms | Saccharomyces cerevisiae |
| metabolism | the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms | Schizosaccharomyces pombe |
| metabolism | the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. The m1A9 MTases belong to the Trm10 subfamily of the SPOUT superfamily. In addition to the m1A9 modification, the Trm10 subfamily of MTases methylates guanosine in some organisms | Homo sapiens |
| additional information | tRNA recognition by Trm10 enzymes, overview | Thermococcus kodakarensis |
| additional information | tRNA recognition by Trm10 enzymes, overview | Saccharomyces cerevisiae |
| additional information | tRNA recognition by Trm10 enzymes, overview | Schizosaccharomyces pombe |
| additional information | tRNA recognition by Trm10 enzymes, overview | Homo sapiens |
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
