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Literature summary extracted from

  • Huang, R.
    Chemical biology of protein N-terminal methyltransferases (2019), ChemBioChem, 20, 976-984 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.1.1.244 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
2.1.1.244 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)

EC Number Crystallization (Comment) Organism
2.1.1.244 crystal structure with PDB IDs 5WCJ Homo sapiens
2.1.1.244 crystal structures with PDB IDs 2EX4, 5E1B, 5E1M, 5E1O, 5E1D, 5E2B, 5E2A, 5CVD, and 5CVE Homo sapiens
2.1.1.244 crystal structures with PDB IDs 3CJT, 3CJS, and 3CJR Escherichia coli
2.1.1.244 crystal structures with PDB IDs 3EGV, 2NXC, and 2NXN Thermus thermophilus
2.1.1.299 crystal structures with PDB IDs 5UBB and 6DUB Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.244 H140A the mutant loses the catalytic activity, but retains binding affinity to the peptide substrate Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.244 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
2.1.1.244 NAM-C3-GPRRRS GPKRRS peptide derived from CENP-A is linked through a propylene group Homo sapiens
2.1.1.244 NAM-TZ-SPKRIA
-
 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.244 cytoplasm
-
 Homo sapiens 5737
-
2.1.1.244 mitochondrion
-
 Homo sapiens 5739
-
2.1.1.244 nucleus
-
 Homo sapiens 5634
-
2.1.1.244 nucleus dNTMT is mainly located in histones in the nucleus, where the majority of chromatin-bound H2B is methylated Drosophila melanogaster 5634
-
2.1.1.244 ribosome
-
 Homo sapiens 5840
-
2.1.1.244 ribosome
-
 Saccharomyces cerevisiae 5840
-
2.1.1.244 ribosome
-
 Escherichia coli 5840
-
2.1.1.244 ribosome
-
 Thermus thermophilus 5840
-
2.1.1.244 ribosome
-
 Drosophila melanogaster 5840
-
2.1.1.299 ribosome
-
 Homo sapiens 5840
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.244 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] Saccharomyces cerevisiae
-
 3 S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.244 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] Homo sapiens
-
 3 S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.244 3 S-adenosyl-L-methionine + N-terminal-[eEF1A] Saccharomyces cerevisiae ATCC 204508
-
 3 S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.244 3 S-adenosyl-L-methionine + N-terminal-[RCC1] Homo sapiens
-
 3 S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.244 L-lysyl-[protein] + 3 S-adenosyl-L-methionine Escherichia coli
-
 3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
 ?
2.1.1.244 L-lysyl-[protein] + 3 S-adenosyl-L-methionine Thermus thermophilus
-
 3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
 ?
2.1.1.244 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
-
 ?
2.1.1.244 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
-
 ?
2.1.1.244 additional information Drosophila melanogaster alpha-N-terminal methylation of histone H2B protein in Drosophila melanogaster ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 additional information Escherichia coli PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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
-
 ?
2.1.1.244 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
-
 ?
2.1.1.244 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
-
 ?
2.1.1.244 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
-
 ?
2.1.1.299 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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.244 Drosophila melanogaster Q6NN40
-
-
2.1.1.244 Escherichia coli P0A8T1
-
-
2.1.1.244 Homo sapiens Q8N6R0
-
-
2.1.1.244 Homo sapiens Q9BV86
-
-
2.1.1.244 Saccharomyces cerevisiae P38340
-
-
2.1.1.244 Saccharomyces cerevisiae Q05874
-
-
2.1.1.244 Saccharomyces cerevisiae ATCC 204508 P38340
-
-
2.1.1.244 Saccharomyces cerevisiae ATCC 204508 Q05874
-
-
2.1.1.244 Thermus thermophilus Q84BQ9
-
-
2.1.1.244 Thermus thermophilus ATCC 27634 Q84BQ9
-
-
2.1.1.244 Thermus thermophilus DSM 579 Q84BQ9
-
-
2.1.1.299 Homo sapiens Q5VVY1
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.244 HeLa cell
-
 Homo sapiens
-
2.1.1.244 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
-
2.1.1.244 MCF-7 cell
-
 Homo sapiens
-
2.1.1.244 MCF-7/LCC9 cell
-
 Homo sapiens
-
2.1.1.244 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
-
2.1.1.299 heart
-
 Homo sapiens
-
2.1.1.299 additional information NTMT2 is predominantly expressed in heart and skeletal muscle tissues Homo sapiens
-
2.1.1.299 skeletal muscle
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.244 3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
-
 Saccharomyces cerevisiae 3 S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.244 3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
-
 Homo sapiens 3 S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.244 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 + ?
-
 ?
2.1.1.244 3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
-
 Saccharomyces cerevisiae ATCC 204508 3 S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.244 3 S-adenosyl-L-methionine + N-terminal-[RCC1]
-
 Homo sapiens 3 S-adenosyl-L-homocysteine + ?
-
 ?
2.1.1.244 L-lysyl-[protein] + 3 S-adenosyl-L-methionine
-
 Escherichia coli 3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
 ?
2.1.1.244 L-lysyl-[protein] + 3 S-adenosyl-L-methionine
-
 Thermus thermophilus 3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
 ?
2.1.1.244 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
-
 ?
2.1.1.244 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
-
 ?
2.1.1.244 additional information alpha-N-terminal methylation of histone H2B protein in Drosophila melanogaster Drosophila melanogaster ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 additional information PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit Escherichia coli ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 additional information the substrate recognition motif is A-K-A/G/K Escherichia coli ?
-
-
2.1.1.244 additional information the substrate recognition motif is X-P-K Drosophila melanogaster ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 additional information the substrate recognition sequence is GKEKTH Homo sapiens ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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 ?
-
-
2.1.1.244 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
-
 ?
2.1.1.244 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
-
 ?
2.1.1.244 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
-
 ?
2.1.1.244 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
-
 ?
2.1.1.299 additional information the substrate recognition motif is X-P-K/R. Although NTMT2 is proposed to be a monomethylase, it can also fully methylate both GPKRIA and PPKRIA peptides, but to a low level. NTMT2 is able to methylate hexamer peptides Homo sapiens ?
-
-
2.1.1.299 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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.244 CG1675
-
 Drosophila melanogaster
2.1.1.244 dNTMT
-
 Drosophila melanogaster
2.1.1.244 Efm7
-
 Saccharomyces cerevisiae
2.1.1.244 elongation factor methyltransferase 7
-
 Saccharomyces cerevisiae
2.1.1.244 FEAT i.e. faint expression in normal tissues, aberrant overexpression in tumors Homo sapiens
2.1.1.244 METTL11A
-
 Homo sapiens
2.1.1.244 METTL13
-
 Homo sapiens
2.1.1.244 METTL13/FEAT
-
 Homo sapiens
2.1.1.244 N-terminal RCC1 methyltransferase
-
 Homo sapiens
2.1.1.244 NNT1
-
 Saccharomyces cerevisiae
2.1.1.244 NRMT1
-
 Homo sapiens
2.1.1.244 Ntm1
-
 Saccharomyces cerevisiae
2.1.1.244 NTMT1
-
 Homo sapiens
2.1.1.244 PrmA
-
 Escherichia coli
2.1.1.244 PrmA
-
 Thermus thermophilus
2.1.1.244 TAE1
-
 Saccharomyces cerevisiae
2.1.1.244 YBR261C
-
 Saccharomyces cerevisiae
2.1.1.244 YLR285W
-
 Saccharomyces cerevisiae
2.1.1.299 METTL11B
-
 Homo sapiens
2.1.1.299 NRMT2
-
 Homo sapiens
2.1.1.299 NTMT2
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.244 S-adenosyl-L-methionine
-
 Homo sapiens
2.1.1.244 S-adenosyl-L-methionine
-
 Saccharomyces cerevisiae
2.1.1.244 S-adenosyl-L-methionine
-
 Escherichia coli
2.1.1.244 S-adenosyl-L-methionine
-
 Thermus thermophilus
2.1.1.244 S-adenosyl-L-methionine
-
 Drosophila melanogaster
2.1.1.299 S-adenosyl-L-methionine
-
 Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.1.1.244 0.00081
-
 pH and temperature not specified in the publication Homo sapiens NAM-TZ-SPKRIA
2.1.1.244 0.00094
-
 pH and temperature not specified in the publication Homo sapiens NAM-C3-GPRRRS

General Information

EC Number General Information Comment Organism
2.1.1.244 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
2.1.1.244 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
2.1.1.244 malfunction mutation and deletion of PrmA causes no growth defects or any distinct phenotype in Escherichia coli Escherichia coli
2.1.1.244 malfunction mutation and deletion of PrmA causes no growth defects or any distinct phenotype in Thermus thermophilus Thermus thermophilus
2.1.1.244 malfunction the activity of the D577A mutant decreases the enzymatic activity by about half Homo sapiens
2.1.1.244 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
2.1.1.244 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
2.1.1.244 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
2.1.1.244 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
2.1.1.244 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
2.1.1.244 additional information substrate recognition and catalytic mechanisms, overview Thermus thermophilus
2.1.1.244 additional information substrate recognition and catalytic mechanisms, overview Drosophila melanogaster
2.1.1.244 additional information substrate recognition and catalytic mechanisms, overview Saccharomyces cerevisiae
2.1.1.244 additional information substrate recognition and catalytic mechanisms, overview. Conformational changes are necessary for the recognition of multiple substrate sites Escherichia coli
2.1.1.244 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
2.1.1.244 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
2.1.1.244 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
2.1.1.244 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
2.1.1.244 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
2.1.1.244 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
2.1.1.244 physiological function PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit Escherichia coli
2.1.1.244 physiological function PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit Thermus thermophilus
2.1.1.299 malfunction the N209I endometrial and P211S lung cancer mutants decrease the trimethylation level of RCC1, whereas the Q144H lung cancer mutant increases the trimethylation level of RCC1 with minimal levels of mono- and dimethylated RCC1. For NTMT2, the V224L breast cancer mutant shows marginal methylation activity for methylation states. Those data infer that methylation levels may play different roles in different cancers Homo sapiens
2.1.1.299 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
2.1.1.299 additional information substrate recognition and catalytic mechanisms, overview Homo sapiens