A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 220.127.116.118
View entry in original ENZYME format
View entry in raw text format (no links)
|N-terminal methionine N(alpha)-acetyltransferase NatE.
- Acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-alanyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-seryl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-valyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-threonyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-lysyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-leucyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
- Acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] <=> an N-terminal-N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
- N-terminal-acetylases (NATs) catalyze the covalent attachment of an
acetyl moiety from acetyl-CoA to the free alpha-amino group at the
N-terminus of a protein.
- This irreversible modification neutralizes the positive charge at the
N-terminus, makes the N-terminal residue larger and more hydrophobic,
and prevents its removal by hydrolysis.
- It may also play a role in membrane targeting and gene silencing.
- NatE is found in all eukaryotic organisms and plays an important role
in chromosome resolution and segregation.
- It specifically targets N-terminal L-methionine residues attached to
Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr.
- There is some substrate overlap with EC 18.104.22.1686.
- In addition, the acetylation of Met followed by small residues such
as Ser, Thr, Ala, or Val suggests a kinetic competition between
NatE and EC 22.214.171.124.
- The enzyme also has the activity of EC 126.96.36.199 and autoacetylates
several of its own lysine residues.
- Formerly EC 188.8.131.52.
|PRIAM enzyme-specific profiles||184.108.40.2068|
|KEGG Ligand Database for Enzyme Nomenclature||220.127.116.118|
|IUBMB Enzyme Nomenclature||18.104.22.1688|
|MEDLINE||Find literature relating to 22.214.171.1248|
|Q0IIJ0, NAA50_BOVIN; ||Q6DBY2, NAA50_DANRE; ||Q9GZZ1, NAA50_HUMAN; |
|Q6PGB6, NAA50_MOUSE; ||Q5RF28, NAA50_PONAB; ||Q6GP53, NAA50_XENLA; |
|Q5XGA9, NAA50_XENTR; ||Q08689, NAT5_YEAST; ||Q980R9, NAT_SACS2; |
|Q4JBG0, NAT_SULAC; ||Q976C3, NAT_SULTO; ||I6YG32, RIMI_MYCTU; |
|Q9NHD5, SAN_DROME; |
entries corresponding to 2.3.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-