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Information on EC 2.1.1.244 - protein N-terminal methyltransferase
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EC Tree
2.1.1.244 protein N-terminal methyltransferaseIUBMB Comments
This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. When the terminal amino acid is L-proline, the enzyme catalyses two successive methylations of its alpha-amino group. When the first amino acid is either L-alanine or L-serine, the enzyme catalyses three successive methylations.
The Pro-Lys in positions 2-3 cannot be exchanged for other amino acids [1,2].
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Word Map
- 2.1.1.244
- methyltransferases
-
rna-dependent
- mtase
-
trimethylation
- dengue
- flavivirus
-
bisubstrate
-
methyltransferase-like
- drug development
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
3
+
=
3
+
3
+
N-terminal-(A,S)PK-[protein]
=
3
+
N-terminal-N,N,N-trimethyl-N-(A,S)PK-[protein]
2
+
=
2
+
2
+
N-terminal-PPK-[protein]
=
2
+
N-terminal-N,N-dimethyl-N-PPK-[protein]
Synonyms
nrmt1, ntmt1, mettl13, n-terminal methyltransferase, protein n-terminal methyltransferase 1, n-terminal rcc1 methyltransferase, mettl11a, ylr285w, ybr261c/tae1, n6amt2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-N-terminal methyltransferase 1
Efm5
Efm7
elongation factor methyltransferase 7
FEAT
i.e. faint expression in normal tissues, aberrant overexpression in tumors
METTL11A
N-terminal and lysine methyltransferase
N-terminal methyltransferase
N-terminal RCC1 methyltransferase
NMT1
-
-
-
-
NNT1
NRMT1
Ntm1
NTMT1
PrmA
protein N-terminal methyltransferase 1
Rkm2
TAE1
YBR261C
YGR001C
YLR285W
METTL11A
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + N-terminal-PPK-[protein] = 2 S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-PPK-[protein]
(2)
-
-
-
3 S-adenosyl-L-methionine + N-terminal-(A,S)PK-[protein] = 3 S-adenosyl-L-homocysteine + N-terminal-N,N,N-trimethyl-N-(A,S)PK-[protein]
(1)
-
-
-
S-adenosyl-L-methionine + N-terminal-(A,S)PK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-(A,S)PK-[protein]
(1a)
-
-
-
S-adenosyl-L-methionine + N-terminal-N,N-dimethyl-N-(A,S)PK-serine-[protein] = S-adenosyl-L-homocysteine + N-terminal-N,N,N-trimethyl-N-(A,S)PK-[protein]
(1c)
-
-
-
S-adenosyl-L-methionine + N-terminal-N-methyl-N-(A,S)PK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-(A,S)PK-[protein]
(1b)
-
-
-
S-adenosyl-L-methionine + N-terminal-N-methyl-N-PPK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-PPK-[protein]
(2b)
-
-
-
S-adenosyl-L-methionine + N-terminal-PPK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-PPK-[protein]
(2a)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:N-terminal-(A,P,S)PK-[protein] methyltransferase
This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. When the terminal amino acid is L-proline, the enzyme catalyses two successive methylations of its alpha-amino group. When the first amino acid is either L-alanine or L-serine, the enzyme catalyses three successive methylations.
The Pro-Lys in positions 2-3 cannot be exchanged for other amino acids [1,2].
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CAS REGISTRY NUMBER
COMMENTARY
9068-28-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + CPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + FPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + HPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + IPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + KPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + LPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + MPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + N-terminal-histone 2B
2 S-adenosyl-L-homocysteine + ?
dimethylation of fruit fly histone 2B by NTMT1 over an N-terminal sequence of 1PPKTSGKAA9
-
-
?
2 S-adenosyl-L-methionine + NPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + PPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + QPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + RPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation and low level trimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + TPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + VPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + WPKRIA
2 S-adenosyl-L-homocysteine + ?
mono- and dimethylation by NTMT1
-
-
?
2 S-adenosyl-L-methionine + YPKRIA
2 S-adenosyl-L-homocysteine + ?
dimethylation by NTMT1
-
-
?
3 (E)-hex-2-en-5-ynyl-S-adenosyl-L-methionine + N-terminal-OLA1
?
-
-
-
?
3 S-adenosyl-L-methionine + APKRIA
3 S-adenosyl-L-homocysteine + ?
trimethylation by NTMT1
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
3 S-adenosyl-L-methionine + GPKRIA
3 S-adenosyl-L-homocysteine + ?
trimethylation by NTMT1
-
-
?
3 S-adenosyl-L-methionine + N-terminal-CENP-A
3 S-adenosyl-L-homocysteine + ?
human CENP-A histone, molecular details for CENP-A recognition by NRMT1. State-specific trimethylation of CENP-A by NRMT1
-
-
?
3 S-adenosyl-L-methionine + N-terminal-dimethyl-SPKRIAKRRS-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRRS-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-LPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-LPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-methyl-SPKRIAKRRS-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRRS-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-peptide-[BAP1 protein]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-peptide-[BAP1 protein]
-
i.e. BRCA1 associated protein 1, a DNA repair protein
-
-
?
3 S-adenosyl-L-methionine + N-terminal-peptide-[DDB2 protein]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-peptide-[DDB2 protein]
-
DDB2 is a DNA repair protein
-
-
?
3 S-adenosyl-L-methionine + N-terminal-peptide-[PARP3 protein]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-peptide-[PARP3 protein]
-
i.e. poly-ADP-ribosylase 3, a DNA repair protein
-
-
?
3 S-adenosyl-L-methionine + N-terminal-PPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-PPKRIA-[RCC1]
3 S-adenosyl-L-methionine + N-terminal-RPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-RPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIA-[RCC1]
3 S-adenosyl-L-methionine + N-terminal-SPKRIAKRR-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRR-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIAKRRS-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRRS-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIAKRRSPP-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIAKRRSPP-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-WPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-WPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-YPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-YPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + SPKRIA
3 S-adenosyl-L-homocysteine + ?
trimethylation by NTMT1
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + DPKRIA
S-adenosyl-L-homocysteine + ?
monomethylation by NTMT1
-
-
?
S-adenosyl-L-methionine + EPKRIA
S-adenosyl-L-homocysteine + ?
monomethylation by NTMT1
-
-
?
S-adenosyl-L-methionine + human histone H3
S-adenosyl-L-homocysteine + ?
-
lower activity with histone H3 compared to histone H4
-
-
?
S-adenosyl-L-methionine + human histone H4
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + N-terminal peptide sequence of a protein
S-adenosyl-L-homocysteine + methylated N-terminal peptide sequence of a protein
-
all known substrates of NTMT1 contain the N-terminal consensus sequence XPK (X = S/P/A/G), although NTMT1 can also methylate peptides with X being F, Y, C, M, K, R, N, Q, or H in vitro, substrate specificity of NTMT1, overview. Structural basis for the specific N-terminal methylation of a consensus motif, XPK, by NTMT1, overview. Hexapeptides composed of the first six residues of RCC1, i.e. regulator of chromosome condensation 1, are recognized by the enzyme. The first residue within the consensus sequence of the NTMT1 substrates is anchored through a hydrogen bond with the conserved Asn168 of NTMT1 in a spacious binding pocket, which exposes the substrate's reactive alpha-amino group to S-adenosyl-L-methionine in the complex structures, and this very N-terminal residue can tolerate most residue substitutions except the negatively charged residues D and E. Asp180 and His140 can act as bases to facilitate deprotonation of the target alpha-N-terminal amino group. Catalytic reaction proceeds probably involving a SN1 mechanism, overview
S-adenosyl-L-homocysteine is bound to NTMT1 in an extended conformation. The carboxylate moiety of SAH forms a salt bridge interaction with the highly conserved Arg74, and the ribosyl group stacks with the indole ring of Trp20. In addition, the adenine moiety of SAH is flanked by the hydrophobic side chains of Ile92 and Val137 and interacts with the main chain amide group of Leu119 and the side chain of Gln120 through hydrogen bonding
-
?
S-adenosyl-L-methionine + N-terminal-(A,P,S)PK-[protein]
S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-(A,P,S)PK-[protein]
-
-
-
?
S-adenosyl-L-methionine + N-terminal-CENP-A
S-adenosyl-L-homocysteine + ?
human CENP-A histone
-
-
?
S-adenosyl-L-methionine + N-terminal-histone 2B
S-adenosyl-L-homocysteine + ?
fruit fly histone 2B
-
-
?
S-adenosyl-L-methionine + Ran guanine nucleotide-exchange factor RCC1
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + retinoblastoma protein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + Rpl12ab
?
-
methylation of Rpl12ab at the N-terminal proline residue
-
-
?
S-adenosyl-L-methionine + SET/TAF-I/PHAPII
S-adenosyl-L-homocysteine + ?
-
only the SETalpha splicing variant is a substrate for NRMT, since it begins with the NRMT consensus in contrast to the beta splicing variant
-
-
?
S-adenosyl-L-methionine + SPKRIAKRRSPPADA
?
substrate peptide consisting of the first 15 amino acids of RCC1. NRMT2 V224L is able to significantly decrease the NRMT1 Km with the RCC1 peptide
-
-
?
S-adenosyl-L-methionine + SSKRAKAKTTKKRP
?
substrate peptide consisting of the first 14 amino acids of MYL9
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
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-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
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
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
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-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
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
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
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
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
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-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
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
-
-
?
3 S-adenosyl-L-methionine + eukaryotic elongation factor 1A
3 S-adenosyl-L-homocysteine + ?
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
-
-
?
3 S-adenosyl-L-methionine + N-terminal-OLA1
3 S-adenosyl-L-homocysteine + ?
i.e. Obg-like ATPase 1 (OLA1) protein, target validation using normal and NTMT1 knockout HEK-293FT cells demonstrates that OLA1, a protein involved in many critical cellular functions, is methylated in vivo by NTMT1
-
-
?
3 S-adenosyl-L-methionine + N-terminal-OLA1
3 S-adenosyl-L-homocysteine + ?
i.e. Obg-like ATPase 1 (OLA1) protein
-
-
?
3 S-adenosyl-L-methionine + N-terminal-PPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-PPKRIA-[RCC1]
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-PPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-PPKRIA-[RCC1]
-
best substrate
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIA-[RCC1]
-
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIA-[RCC1]
-
high activity
-
-
?
3 S-adenosyl-L-methionine + N-terminal-SPKRIA-[RCC1]
3 S-adenosyl-L-homocysteine + N-terminal-trimethyl-SPKRIA-[RCC1]
-
i.e. regulator of chromosome condensation 1
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
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
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[eEF1A]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
-
-
-
?
3 S-adenosyl-L-methionine + N-terminal-[RCC1]
3 S-adenosyl-L-homocysteine + ?
RCC1p and methionine-removed RCC1
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
L-lysyl-[protein] + 3 S-adenosyl-L-methionine
3 H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine
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
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
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
N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + APKQQLSKY
?
synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + APKQQLSKY
?
-
synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + APKQQLSKY
?
-
synthetic peptide, modified Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + PPKQQLSKY
?
synthetic peptide, yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + PPKQQLSKY
?
-
synthetic peptide, yeast protein Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + PPKQQLSKY
?
-
synthetic peptide, Rps25a/Rps25b-derived peptide
-
-
?
S-adenosyl-L-methionine + Ran guanine nucleotide-exchange factor RCC1
S-adenosyl-L-homocysteine + ?
-
NRMT is the predominant alpha-N-methyltransferase for RCC1
-
-
?
S-adenosyl-L-methionine + Ran guanine nucleotide-exchange factor RCC1
S-adenosyl-L-homocysteine + ?
-
substrate docking and mutational analysis of RCC1 defining the NRMT recognition sequence, the first 3 residues Ser-Pro-Lys interact with NRMT, overview
-
-
?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
-
the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66
-
-
?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
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the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66. Utilization of top down mass spectrometry to determine the sites of methylation of Rpl12ab
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S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
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the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66
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?
S-adenosyl-L-methionine + Rpl12ab
S-adenosyl-L-homocysteine + ?
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the yeast Rpl12ab protein is dimethylated at the N-terminal proline residue, trimethylated at Lys-3 by Rkm2, and monomethylated at Arg66. Utilization of top down mass spectrometry to determine the sites of methylation of Rpl12ab
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S-adenosyl-L-methionine + Rps25a
?
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Rps25a and Rps25b differ only at position 104, a threonine residue is present in the former and an alanine residue in the latter
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S-adenosyl-L-methionine + Rps25b
?
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Rps25a and Rps25b differ only at position 104, a threonine residue is present in the former and an alanine residue in the latter
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S-adenosyl-L-methionine + SPKQQLSKY
?
synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide
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S-adenosyl-L-methionine + SPKQQLSKY
?
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synthetic peptide, modified yeast protein Rps25a/Rps25b-derived peptide
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S-adenosyl-L-methionine + SPKQQLSKY
?
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synthetic peptide, modified Rps25a/Rps25b-derived peptide
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?
additional information
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alpha-N-terminal methylation of histone H2B protein in Drosophila melanogaster
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additional information
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the substrate recognition motif is X-P-K
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additional information
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PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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additional information
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the substrate recognition motif is A-K-A/G/K
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additional information
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enzyme substrates have a unique N-terminal motif, Met-(Ala/Pro/Ser)-Pro-Lys. The initiating Met is cleaved, and the exposed alpha-amino group is mono-, di-, or trimethylated
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?
additional information
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the enzyme shows a ternary complex mechanism of catalysis, involving formation of a SAM-enzyme-acceptor complex and direct transfer of the methyl group from SAM to the acceptor protein
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additional information
?
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the methyltransferases specifically recognizes the N-terminal X-Pro-Lys sequence motif. Localization of methylation sites by top down mass spectrometry using collisionally activated dissociation or electron capture dissociation. The enzyme can also recognize species with N-terminal alanine and serine residues in addition to those with proline residues, but the proline residue in position 1 is a preferred substrate
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?
additional information
?
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the methyltransferases specifically recognizes the N-terminal X-Pro-Lys sequence motif. Localization of methylation sites by top down mass spectrometry using collisionally activated dissociation or electron capture dissociation. The enzyme can also recognize species with N-terminal alanine and serine residues in addition to those with proline residues, but the proline residue in position 1 is a preferred substrate
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?
additional information
?
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the protein N-terminal methyltransferase 1 (NTMT1) methylates the alpha-N-terminal amines of proteins
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additional information
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enzyme NTMT1 catalyzes the transfer of the methyl group from the S-adenosyl-L-methionine to the protein alpha-amine, resulting in formation of S-adenosyl-L-homocysteine and alpha-N-methylated proteins. Inhibition pattern and methylation progress analyses are performed to determine the kinetic mechanism and processivity of NTMT1, the enzyme NTMT1 utilizes a random sequential bi bi mechanism and proceeds in a distributive manner. Residues of RCC1, i.e. regulator of chromosome condensation 1, are recognized by the enzyme. Methylation status of products is analyzed by MALDI-mass spectrometry
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additional information
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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
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additional information
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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
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additional information
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protein N-terminal methyltransferase 1 (NTMT1/NRMT1) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to protein alpha-N-terminal amines. It recognizes a specific motif X-P-K/R (X represents any amino acid other than D/E)
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
?
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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
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additional information
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analysis of methylation sites, method, detailed overview
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additional information
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analysis of methylation sites, method, detailed overview
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additional information
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histone peptide profiling reveals that human NRMT1is highly selective to human CENP-A and fruit fly H2B, which share a common Xaa-Pro-Lys/Arg motif
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additional information
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histone peptide profiling reveals that human NRMT1is highly selective to human CENP-A and fruit fly H2B, which share a common Xaa-Pro-Lys/Arg motif
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additional information
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motif sequence and signal peptide analyses, and activity-based substrate profiling of NTMT1 utilizing (E)-hex-2-en-5-ynyl-S-adenosyl-L-methionine (Hey-SAM) reveals 72 potential targets, overview
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additional information
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NRMT1 exhibits distributive trimethylase activity in vitro. Isozymes NRMT1 and NRMT2 can interact both in vitro and in vivo, modeling of NRMT1 and NRMT2 interactions. The Ser-Pro-Lys consensus sequence of the RCC1 peptide is a preferred substrate for NRMT1
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additional information
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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
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additional information
?
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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
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additional information
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the substrate recognition sequence is GKEKTH
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additional information
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the substrate recognition sequence is GKEKTH
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additional information
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the N-terminal protein methyltransferase catalyzes the modification of two ribosomal protein substrates, Rpl12ab and Rps25a/Rps25b. The yeast RPS25A and RPS25B genes and differ only at a single amino acid residue
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additional information
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the methyltransferases specifically recognizes the N-terminal X-Pro-Lys sequence motif. Localization of methylation sites by top down mass spectrometry using collisionally activated dissociation or electron capture dissociation. The yeast enzyme can also recognize species with N-terminal alanine and serine residues in addition to those with proline residues, although to a lesser extent, the proline residue in position 1 is a preferred substrate
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?
additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
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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
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additional information
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analysis of methylation sites, method, detailed overview
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additional information
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analysis of methylation sites, method, detailed overview
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additional information
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analysis of methylation sites, method, detailed overview
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
?
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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
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additional information
?
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analysis of methylation sites, method, detailed overview
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additional information
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analysis of methylation sites, method, detailed overview
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
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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
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additional information
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the enzyme alpha-N-methylates the small subunit of ribulose-1,5-bisphohate carboxylase/oxygenase
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additional information
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the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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additional information
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the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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additional information
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the substrate recognition motif is M-L/M/K-G/Q. PrmA preferentially methylates free ribosomal protein L11 over an assembled 50S ribosomal subunit
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