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Your query returned 1 entry. Printable version
EC | 2.3.1.255 | ||||||||||||
Accepted name: | N-terminal amino-acid Nα-acetyltransferase NatA | ||||||||||||
Reaction: | (1) acetyl-CoA + an N-terminal-glycyl-[protein] = an N-terminal-Nα-acetyl-glycyl-[protein] + CoA (2) acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-Nα-acetyl-L-alanyl-[protein] + CoA (3) acetyl-CoA + an N-terminal-L-seryl-[protein] = an N-terminal-Nα-acetyl-L-seryl-[protein] + CoA (4) acetyl-CoA + an N-terminal-L-valyl-[protein] = an N-terminal-Nα-acetyl-L-valyl-[protein] + CoA (5) acetyl-CoA + an N-terminal-L-cysteinyl-[protein] = an N-terminal-Nα-acetyl-L-cysteinyl-[protein] + CoA (6) acetyl-CoA + an N-terminal-L-threonyl-[protein] = an N-terminal-Nα-acetyl-L-threonyl-[protein] + CoA |
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Other name(s): | NAA10 (gene name); NAA15 (gene name); ARD1 (gene name) | ||||||||||||
Systematic name: | acetyl-CoA:N-terminal-Gly/Ala/Ser/Val/Cys/Thr-[protein] Nα-acetyltransferase | ||||||||||||
Comments: | N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine. | ||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||
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