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Literature summary for 2.1.1.244 extracted from
- Novel N-terminal and lysine methyltransferases that target translation elongation factor 1A in yeast and human (2016), Mol. Cell. Proteomics, 15, 164-176 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene EEF1AKMT1, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta DE3 | Homo sapiens |
| gene EFM5, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta DE3 | Saccharomyces cerevisiae |
| gene EFM7, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta DE3 | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | Saccharomyces cerevisiae | enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae | 3 S-adenosyl-L-homocysteine + ? | - |
? |  |
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | Homo sapiens | enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | Saccharomyces cerevisiae ATCC 204508 | enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| additional information | Saccharomyces cerevisiae | the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1 | ? | - |
- |
|
| additional information | Homo sapiens | the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1 | ? | - |
- |
|
| additional information | Saccharomyces cerevisiae ATCC 204508 | the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1 | ? | - |
- |
|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q8WVE0 | - |
- |
| Saccharomyces cerevisiae | P53200 | - |
- |
| Saccharomyces cerevisiae | Q05874 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P53200 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | Q05874 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae | Saccharomyces cerevisiae | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae | Homo sapiens | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Human eEF1A is trimethylated at its N-terminus | Saccharomyces cerevisiae | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Human eEF1A is trimethylated at its N-terminus | Homo sapiens | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | enzyme YLR285W trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Methylation by Efm7 is affected by the conformation of eEF1A. Efm7 is unable to methylate a synthetic peptide corresponding to the N-terminal 10 amino acids of eEF1A (GKEKSHINVV), but methylates full-length eEF1A in vitro. Human eEF1A is trimethylated at its N-terminus | Saccharomyces cerevisiae | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae | Saccharomyces cerevisiae ATCC 204508 | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | enzyme N6AMT2 trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Human eEF1A is trimethylated at its N-terminus | Saccharomyces cerevisiae ATCC 204508 | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A | enzyme YLR285W trimethylates eEF1A at the N-terminal site and at the adjacent lysine 79, protein substrate from Homo sapiens or Saccharomyces cerevisiae. Yeast eEF1A is trimethylated at its N-terminus and dimethylated at lysine 3. Methylation by Efm7 is affected by the conformation of eEF1A. Efm7 is unable to methylate a synthetic peptide corresponding to the N-terminal 10 amino acids of eEF1A (GKEKSHINVV), but methylates full-length eEF1A in vitro. Human eEF1A is trimethylated at its N-terminus | Saccharomyces cerevisiae ATCC 204508 | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| additional information | the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1 | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1 | Homo sapiens | ? | - |
- |
|
| additional information | analysis of methylation sites, method, detailed overview | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | analysis of methylation sites, method, detailed overview | Homo sapiens | ? | - |
- |
|
| additional information | the methyltransferase N6AMT2 is responsible for Lys79 methylation of human eEF1A, but has been previously documented as a putative N(6)-adenine-specific DNA methyltransferase. It is renamed eEF1A-KMT1 | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | analysis of methylation sites, method, detailed overview | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EEF1A lysine methyltransferase 1 | UniProt | Homo sapiens |
| eEF1A-KMT1 | - |
Homo sapiens |
| EEF1AKMT1 | - |
Homo sapiens |
| Efm5 | - |
Saccharomyces cerevisiae |
| Efm7 | - |
Saccharomyces cerevisiae |
| elongation factor methyltransferase 7 | - |
Saccharomyces cerevisiae |
| N-terminal and lysine methyltransferase | - |
Saccharomyces cerevisiae |
| N-terminal and lysine methyltransferase | - |
Homo sapiens |
| N6AMT2 | - |
Homo sapiens |
| YGR001C | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
| 30 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Saccharomyces cerevisiae |
| 7.4 | - |
assay at | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Saccharomyces cerevisiae | |
| S-adenosyl-L-methionine | - |
Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme Efm5 is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in human catalyzed by enzyme N6AMT2, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human. Human enzyme N6AMT2 is the direct orthologue of the yeast Efm5, and Efm5 and N6AMT2 can methylate eEF1A from either species in vitro | Saccharomyces cerevisiae |
| evolution | the enzyme is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in yeast catalyzed by enzymes Efm5 and Efm7, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human. Human enzyme N6AMT2 is the direct orthologue of the yeast Efm5, and Efm5 and N6AMT2 can methylate eEF1A from either species in vitro. Methyltransferases that act on lysine 79 in eEF1A are conserved from yeast to human | Homo sapiens |
| evolution | YLR285W is termed elongation factor methyltransferase 7 (Efm7). This enzyme is a distinct type of eukaryotic N-terminal methyltransferase as, unlike the three other known eukaryotic N-terminal methyltransferases, its substrate does not have an N-terminal [A/P/S]-P-K motif. The N-terminal methylation of eEF1A is also present in human catalyzed by enzyme N6AMT2, this conservation over a large evolutionary distance suggests it to be of functional importance. The trimethylation of Lys79 in eEF1A is conserved from yeast to human | Saccharomyces cerevisiae |
| malfunction | deletion of YLR285W results in the loss of N-terminal and lysine methylation in vivo, whereas overexpression of YLR285W results in an increase of methylation at these sites | Saccharomyces cerevisiae |
| malfunction | loss of eEF1A trimethylation at Lys79 upon knockout of YGR001C | Saccharomyces cerevisiae |
| physiological function | eukaryotic elongation factor 1A (eEF1A) is an essential, highly methylated protein that facilitates translational elongation by delivering aminoacyl-tRNAs to ribosomes. Eukaryotic protein N-terminal methyltransferase from Saccharomyces cerevisiae, YLR285W, methylates eEF1A at a previously undescribed high-stoichiometry N-terminal site and at the adjacent lysine | Saccharomyces cerevisiae |
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