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 KJ, Lipson RS, Al-Hadid Q, Whitelegge JP, Clarke SG (June 2010). "Identification of protein N-terminal methyltransferases in yeast and humans". Biochemistry. 49 (25): 5225–35. doi:10.1021/bi100428x. PMC 2890028. PMID 20481588.
  2. ↑ Tooley CE, Petkowski JJ, Muratore-Schroeder TL, Balsbaugh JL, Shabanowitz J, Sabat M, Minor W, Hunt DF, Macara IG (August 2010). "NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein". Nature. 466 (7310): 1125–8. doi:10.1038/nature09343. PMC 2939154. PMID 20668449.
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