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Literature summary for 2.1.1.244 extracted from
- Chemical biology of protein N-terminal methyltransferases (2019), ChemBioChem, 20, 976-984 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| GDP | methylation of eEF1A is increased in the presence of either GDP or GTP, which are known to bind to eEF1A and to induce conformational changes | Saccharomyces cerevisiae |  |
| GTP | methylation of eEF1A is increased in the presence of either GDP or GTP, which are known to bind to eEF1A and to induce conformational changes | Saccharomyces cerevisiae | |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure with PDB IDs 5WCJ | Homo sapiens |
| crystal structures with PDB IDs 2EX4, 5E1B, 5E1M, 5E1O, 5E1D, 5E2B, 5E2A, 5CVD, and 5CVE | Homo sapiens |
| crystal structures with PDB IDs 3CJT, 3CJS, and 3CJR | Escherichia coli |
| crystal structures with PDB IDs 3EGV, 2NXC, and 2NXN | Thermus thermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H140A | the mutant loses the catalytic activity, but retains binding affinity to the peptide substrate | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | development of potent and specific inhibitors, bisubstrate analogues that simultaneously target both binding sites are proven to be an effective strategy to obtain potent and selective inhibitors for many enzymes with two binding sites. Because NTMT1 forms a ternary complex during catalysis, a bisubstrate strategy has been applied to design and synthesize bisubstrate inhibitors by covalently linking a SAM analogue with a peptide substrate to mimic the transition state. NTMT1 bisubstrate inhibitors contain three components: an N-adenosyl-L-methionine (NAM) that replaces the sulfonium ion of SAM with a nitrogen atom, a hexapeptide derived from the N-terminal sequence of NTMT1 substrate, and a linker. The potency of such bisubstrate inhibitors corroborate the Bi Bi mechanism of NTMT1 methylation | Homo sapiens | |
| NAM-C3-GPRRRS | GPKRRS peptide derived from CENP-A is linked through a propylene group | Homo sapiens | |
| NAM-TZ-SPKRIA | - |
Homo sapiens | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | - |
Homo sapiens | 5737 | - |
| mitochondrion | - |
Homo sapiens | 5739 | - |
| nucleus | - |
Homo sapiens | 5634 | - |
| nucleus | dNTMT is mainly located in histones in the nucleus, where the majority of chromatin-bound H2B is methylated | Drosophila melanogaster | 5634 | - |
| ribosome | - |
Homo sapiens | 5840 | - |
| ribosome | - |
Saccharomyces cerevisiae | 5840 | - |
| ribosome | - |
Escherichia coli | 5840 | - |
| ribosome | - |
Thermus thermophilus | 5840 | - |
| ribosome | - |
Drosophila melanogaster | 5840 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] | Saccharomyces cerevisiae | - |
3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] | Homo sapiens | - |
3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] | Saccharomyces cerevisiae ATCC 204508 | - |
3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + N-terminal-[RCC1] | Homo sapiens | - |
3 S-adenosyl-L-homocysteine + ? | - |
? | |
| L-lysyl-[protein] + 3 S-adenosyl-L-methionine | Escherichia coli | - |
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| L-lysyl-[protein] + 3 S-adenosyl-L-methionine | Thermus thermophilus | - |
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| L-lysyl-[protein] + 3 S-adenosyl-L-methionine | Thermus thermophilus DSM 579 | - |
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| L-lysyl-[protein] + 3 S-adenosyl-L-methionine | Thermus thermophilus ATCC 27634 | - |
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| additional information | Drosophila melanogaster | alpha-N-terminal methylation of histone H2B protein in Drosophila melanogaster | ? | - |
- |
|
| additional information | Homo sapiens | human MTase-like protein 13 (METTL13) is a dual MTase for both N-terminal Gly1 and Lys55 of human eEF1A. To date, eEF1A is the only validated biological substrate for METTL13 | ? | - |
- |
|
| additional information | Escherichia coli | PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | ? | - |
- |
|
| additional information | Homo sapiens | substrate of NTMT1 are regulator of chromosome condensation 1 (RCC1), tumor suppressor retinoblastoma1 (RB1), oncoprotein SET (also known as I2PP2A, TAF1a), damaged DNA-binding protein2 (DDB2), poly(ADP-ribose) polymerase3 (PARP3), and centromere proteins A and B | ? | - |
- |
|
| additional information | Thermus thermophilus | the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | ? | - |
- |
|
| additional information | Saccharomyces cerevisiae | YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A | ? | - |
- |
|
| additional information | Thermus thermophilus DSM 579 | the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | ? | - |
- |
|
| additional information | Saccharomyces cerevisiae ATCC 204508 | YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A | ? | - |
- |
|
| additional information | Thermus thermophilus ATCC 27634 | the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | ? | - |
- |
|
| N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine | Homo sapiens | - |
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine | Drosophila melanogaster | - |
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine | Saccharomyces cerevisiae | - |
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine | Saccharomyces cerevisiae ATCC 204508 | - |
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | Q6NN40 | - |
- |
| Escherichia coli | P0A8T1 | - |
- |
| Homo sapiens | Q8N6R0 | - |
- |
| Homo sapiens | Q9BV86 | - |
- |
| Saccharomyces cerevisiae | P38340 | - |
- |
| Saccharomyces cerevisiae | Q05874 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P38340 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | Q05874 | - |
- |
| Thermus thermophilus | Q84BQ9 | - |
- |
| Thermus thermophilus ATCC 27634 | Q84BQ9 | - |
- |
| Thermus thermophilus DSM 579 | Q84BQ9 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| HeLa cell | - |
Homo sapiens | - |
| HeLa cell | FEAT is observed in the cytoplasm, mitochondria, and nucleus of HeLa cells, as well as in the blood of cancer patients | Homo sapiens | - |
| MCF-7 cell | - |
Homo sapiens | - |
| MCF-7/LCC9 cell | - |
Homo sapiens | - |
| additional information | the NTMT1 gene is expressed in all tissues, and the protein is expressed in most tissues, except spleen, liver, and fallopian tube tissue. NTMT1 is overexpressed in tumor tissues of patients, including colorectal, melanoma, carcinoid, lung, and liver | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] | - |
Saccharomyces cerevisiae | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] | - |
Homo sapiens | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] | specifically, the C-terminal domain is able to methylate peptides derived from the first 15 amino acids of eEF1A, whereas the N-terminal domain is sufficient for methylation of Lys55. High specificity of METTL13 for eEF1A | Homo sapiens | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] | - |
Saccharomyces cerevisiae ATCC 204508 | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| 3 S-adenosyl-L-methionine + N-terminal-[RCC1] | - |
Homo sapiens | 3 S-adenosyl-L-homocysteine + ? | - |
? | |
| L-lysyl-[protein] + 3 S-adenosyl-L-methionine | - |
Escherichia coli | 3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| L-lysyl-[protein] + 3 S-adenosyl-L-methionine | - |
Thermus thermophilus | 3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| L-lysyl-[protein] + 3 S-adenosyl-L-methionine | - |
Thermus thermophilus DSM 579 | 3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| L-lysyl-[protein] + 3 S-adenosyl-L-methionine | - |
Thermus thermophilus ATCC 27634 | 3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| additional information | alpha-N-terminal methylation of histone H2B protein in Drosophila melanogaster | Drosophila melanogaster | ? | - |
- |
|
| additional information | human MTase-like protein 13 (METTL13) is a dual MTase for both N-terminal Gly1 and Lys55 of human eEF1A. To date, eEF1A is the only validated biological substrate for METTL13 | Homo sapiens | ? | - |
- |
|
| additional information | PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | Escherichia coli | ? | - |
- |
|
| additional information | substrate of NTMT1 are regulator of chromosome condensation 1 (RCC1), tumor suppressor retinoblastoma1 (RB1), oncoprotein SET (also known as I2PP2A, TAF1a), damaged DNA-binding protein2 (DDB2), poly(ADP-ribose) polymerase3 (PARP3), and centromere proteins A and B | Homo sapiens | ? | - |
- |
|
| additional information | the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | Thermus thermophilus | ? | - |
- |
|
| additional information | YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | the S-adenosyl-L-methionine-dependent protein methyltransferase EFM7 trimethylates the N-terminal glycine Gly-2 of elongation factor 1-alpha (TEF1 and TEF2), before also catalyzing the mono- and dimethylation of Lys-3. The substrate recognition sequence is GKEKSH. Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A. Efm7 can methylate domain 1 (residues 1-238) of eEF1A, but to a smaller degree of trimethylation. Although yeast Efm7 is not able to methylate the decamer peptide that is derived from yeast N-terminal eEF1A, METTL13 can methylate the 15mer peptide derived from human N-terminal eEF1A | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | the substrate recognition motif is A-K-A/G/K | Escherichia coli | ? | - |
- |
|
| additional information | the substrate recognition motif is X-P-K | Drosophila melanogaster | ? | - |
- |
|
| additional information | the substrate recognition motif is X-P-K. YBR261C methylates ribosomal substrates Rp112ab and Rps25a/Rps25b. YBR261C is able to methylate nonamer synthetic peptides, including PPKQQLSKY, which is derived from alpha-N-terminal Rps25a/b and A/S-PKQQLSKY, with Ala or Ser replacing Pro. YBR261C is able to methylate nonamer peptides | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | the substrate recognition motif is X-P-K/R. NTMT1 is able to methylate hexamer peptides. NTMT1 is known to be a trimethylase that catalyzes mono-, di-, and trimethylation. During the process of multiple methylations, the substrate can be released and rebind to NTMT1, which proceeds through a distributive mechanism for multiple methylations | Homo sapiens | ? | - |
- |
|
| additional information | the substrate recognition sequence is GKEKTH | Homo sapiens | ? | - |
- |
|
| additional information | the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | Thermus thermophilus DSM 579 | ? | - |
- |
|
| additional information | the substrate recognition motif is X-P-K. YBR261C methylates ribosomal substrates Rp112ab and Rps25a/Rps25b. YBR261C is able to methylate nonamer synthetic peptides, including PPKQQLSKY, which is derived from alpha-N-terminal Rps25a/b and A/S-PKQQLSKY, with Ala or Ser replacing Pro. YBR261C is able to methylate nonamer peptides | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | YLR285W, also named elongation factor methyltransferase 7 (Efm7), is a dual MTase that installs methyl groups at both N-terminal Gly1 and Lys2 residues of yeast eEF1A protein. Lys2 is methylated only after trimethylation of Gly1. Yeast eEF1A starts with GKEKSHINV and is the only known substrate of Efm7, although there are 35 other yeast proteins with a G-K sequence at their N termini. But Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | the S-adenosyl-L-methionine-dependent protein methyltransferase EFM7 trimethylates the N-terminal glycine Gly-2 of elongation factor 1-alpha (TEF1 and TEF2), before also catalyzing the mono- and dimethylation of Lys-3. The substrate recognition sequence is GKEKSH. Efm7 is not able to methylate the synthetic decamer peptide GKEKSHINVV derived from the N-terminus of eEF1A. Efm7 can methylate domain 1 (residues 1-238) of eEF1A, but to a smaller degree of trimethylation. Although yeast Efm7 is not able to methylate the decamer peptide that is derived from yeast N-terminal eEF1A, METTL13 can methylate the 15mer peptide derived from human N-terminal eEF1A | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
| additional information | the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | Thermus thermophilus ATCC 27634 | ? | - |
- |
|
| N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine | - |
Homo sapiens | N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine | - |
Drosophila melanogaster | N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine | - |
Saccharomyces cerevisiae | N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
| N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine | - |
Saccharomyces cerevisiae ATCC 204508 | N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CG1675 | - |
Drosophila melanogaster |
| dNTMT | - |
Drosophila melanogaster |
| Efm7 | - |
Saccharomyces cerevisiae |
| elongation factor methyltransferase 7 | - |
Saccharomyces cerevisiae |
| FEAT | i.e. faint expression in normal tissues, aberrant overexpression in tumors | Homo sapiens |
| METTL11A | - |
Homo sapiens |
| METTL13 | - |
Homo sapiens |
| METTL13/FEAT | - |
Homo sapiens |
| N-terminal RCC1 methyltransferase | - |
Homo sapiens |
| NNT1 | - |
Saccharomyces cerevisiae |
| NRMT1 | - |
Homo sapiens |
| Ntm1 | - |
Saccharomyces cerevisiae |
| NTMT1 | - |
Homo sapiens |
| PrmA | - |
Escherichia coli |
| PrmA | - |
Thermus thermophilus |
| TAE1 | - |
Saccharomyces cerevisiae |
| YBR261C | - |
Saccharomyces cerevisiae |
| YLR285W | - |
Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Homo sapiens | |
| S-adenosyl-L-methionine | - |
Saccharomyces cerevisiae | |
| S-adenosyl-L-methionine | - |
Escherichia coli | |
| S-adenosyl-L-methionine | - |
Thermus thermophilus | |
| S-adenosyl-L-methionine | - |
Drosophila melanogaster | |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.00081 | - |
pH and temperature not specified in the publication | Homo sapiens | NAM-TZ-SPKRIA | |
| 0.00094 | - |
pH and temperature not specified in the publication | Homo sapiens | NAM-C3-GPRRRS | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | deletion of YBR261C in yeast abolishes N-terminal methylation, which consequently alters the ribosomal profile and leads to defects in both translational efficiency and fidelity. Overexpression of YBR261 validates its involvement in protein synthesis | Saccharomyces cerevisiae |
| malfunction | knockdown of NTMT1 results in mitotic defects and sensitizes etoposide and gamma irradiation in breast cancer cell lines such as MCF-7 and LCC9 | Homo sapiens |
| malfunction | mutation and deletion of PrmA causes no growth defects or any distinct phenotype in Escherichia coli | Escherichia coli |
| malfunction | mutation and deletion of PrmA causes no growth defects or any distinct phenotype in Thermus thermophilus | Thermus thermophilus |
| malfunction | the activity of the D577A mutant decreases the enzymatic activity by about half | Homo sapiens |
| metabolism | protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. Functions of methylated glycine, alanine, and serine, overview | Homo sapiens |
| metabolism | protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. Functions of methylated glycine, alanine, and serine, overview | Saccharomyces cerevisiae |
| metabolism | protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. Functions of methylated glycine, alanine, and serine, overview | Drosophila melanogaster |
| metabolism | protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. The alpha-N-terminal methylation has been reported on various N-terminal sequences in prokaryotic proteins. Functions of methylated glycine, alanine, and serine, overview | Escherichia coli |
| metabolism | protein alpha-N-terminal methylation is catalyzed by prokaryotic and eukaryotic protein N-terminal methyltransferases. The prevalent occurrence of this methylation in ribosomes, myosin, and histones implies its function in protein-protein interactions. The alpha-N-terminal methylation has been reported on various N-terminal sequences in prokaryotic proteins. Functions of methylated glycine, alanine, and serine, overview | Thermus thermophilus |
| additional information | substrate recognition and catalytic mechanisms, overview | Thermus thermophilus |
| additional information | substrate recognition and catalytic mechanisms, overview | Drosophila melanogaster |
| additional information | substrate recognition and catalytic mechanisms, overview | Saccharomyces cerevisiae |
| additional information | substrate recognition and catalytic mechanisms, overview. Conformational changes are necessary for the recognition of multiple substrate sites | Escherichia coli |
| additional information | substrate recognition and catalytic mechanisms, overview. Efm7 substrate recognition may require the three-dimensional structure, which is different from the classic linear X-P-K/R motif recognition by other eukaryotic protein NTMTs | Saccharomyces cerevisiae |
| additional information | substrate recognition and catalytic mechanisms, overview. Ligand binding structures are analyzed. NTMT1-catalyzed methylation follows a random sequential Bi Bi mechanism, which involves the formation of a ternary complex with either substrate binding to NTMT1 first. Two highly conserved Asp180 and His140 act as general bases to facilitate deprotonation of the alpha-amino group of the N-terminus to attack SAM to transfer the methyl group | Homo sapiens |
| additional information | substrate recognition and catalytic mechanisms, overview. METTL13 has two distinct MTase domains: N- and C-terminal domains that appear to have different recognition preferences. The C-terminal domain of dual MTase METTL13 is responsible for the a-N-terminal methylation of eEF1A. The unique interaction of Asp577 with the alpha-amino group of Gly1 is required for enzymatic activity | Homo sapiens |
| physiological function | biological significances of NTMT1 in cell mitosis, chromatin segregation, and damaged DNA repair, along with its implications in cancer and aging | Homo sapiens |
| physiological function | dNTMT is mainly located in the nucleus, where the majority of chromatin-bound H2B is methylated. dNTMT recognizes the N-terminal sequence of Drosophila melanogaster H2B (PPKTSG), which conforms to the canonical X-P-K recognition motif for its mammalian orthologues (X=A, P, or S). dNTMT methylation is not processive since monomethylated Pro is accumulated during the methylation reaction. In addition, dART8, a PRMT for H3R2 methylation, negatively regulated H2B N-terminal methylation, thus suggesting crosstalk between methylation on two histone tails | Drosophila melanogaster |
| physiological function | METTL13/FEAT is implicated in tumorigenesis in vivo by suppressing apoptosis. METTL13/FEAT protein is also implied as a tumor suppressor in bladder carcinoma by negatively regulating cell proliferation, migration, and invasion in bladder cancer cells | Homo sapiens |
| physiological function | PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | Escherichia coli |
| physiological function | PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit | Thermus thermophilus |
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