Protein N-terminal methyltransferase

Protein N-terminal methyltransferase
Identifiers
EC number 2.1.1.244
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Protein N-terminal methyltransferase (EC 2.1.1.244, NMT1 (gene), METTL11A (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:N-terminal-(A,P,S)PK-(protein) methyltransferase.[1][2] This enzyme catalyses the following chemical reaction

(1) 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] (overall reaction)
(1a) S-adenosyl-L-methionine + N-terminal-(A,S)PK-[protein] S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-(A,S)PK-[protein]
(1b) 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]
(1c) 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]
(2) 2 S-adenosyl-L-methionine + N-terminal-PPK-[protein] 2 S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-PPK-[protein] (overall reaction)
(2a) S-adenosyl-L-methionine + N-terminal-PPK-[protein] S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-PPK-[protein]
(2b) S-adenosyl-L-methionine + N-terminal-N-methyl-N-PPK-[protein] S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-PPK-[protein]

This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys.

References

  1. Webb, K.J.; Lipson, R.S.; Al-Hadid, Q.; Whitelegge, J.P.; Clarke, S.G. (2010). "Identification of protein N-terminal methyltransferases in yeast and humans". Biochemistry. 49: 5225–5235. doi:10.1021/bi100428x. PMID 20481588.
  2. Tooley, C.E.; Petkowski, J.J.; Muratore-Schroeder, T.L.; Balsbaugh, J.L.; Shabanowitz, J.; Sabat, M.; Minor, W.; Hunt, D.F.; Macara, I.G. (2010). "NRMT is an α-N-methyltransferase that methylates RCC1 and retinoblastoma protein". Nature. 466: 1125–1128. doi:10.1038/nature09343. PMID 20668449.
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