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2.3.1.258: N-terminal methionine Nalpha-acetyltransferase NatE

This is an abbreviated version!
For detailed information about N-terminal methionine Nalpha-acetyltransferase NatE, go to the full flat file.

Word Map on EC 2.3.1.258

Reaction

acetyl-CoA
+
an N-terminal-L-methionyl-L-alanyl-[protein]
=
an N-terminal-Nalpha-acetyl-L-methionyl-L-alanyl-[protein]
 +
CoA

Synonyms

ARD1, EC 2.3.1.88, hNaa50, hNatA, MtRimI, N-terminal acetyltransferase E, NAA10, NAA15, Naa50, Naa50/San, Naa50p, Naa50p (NAT5/SAN) N-terminal acetyltransferase complex, Nalpha-acetyltransferase, NAT, NAT1, NAT5, NAT5/SAN, NatA, NatA/Naa50 complex, NatE, RimI, RimI acetyltransferase, Rv3420c, SAN, ScNaa50, ScNatA, SpNaa50, SpNatA

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.258 N-terminal methionine Nalpha-acetyltransferase NatE

Inhibitors

Inhibitors on EC 2.3.1.258 - N-terminal methionine Nalpha-acetyltransferase NatE

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
competitive product inhibition; product inhibition, competitive versus acetyl-CoA, noncompetitive against peptide substrate well in line with a ternary complex mechanism. The non-competitive inhibition pattern observed when CoA is tested against peptide as variable substrate and at fixed concentrations of acetyl-CoA also rules out a ping-pong mechanism
desulfo-CoA
competitive inhibition; competitive versus acetyl-CoA
HYPK
Q9GZZ1; P41227; Q9BXJ9
UniProt ID Q9NX55, a protein with intrinsic NAA10 catalytic subunit inhibitory activity. HYPK and hNAA50 can bind to hNatA simultaneously to form a tetrameric hNatE/HYPK complex. hNatE displays an about 8.6fold decrease of Km, and an about 1.1fold decrease of kcat, with an overall 7.7fold increase of catalytic efficiency, compared to hNAA50. In the presence HYPK, hNatE displays an about 1.3fold decrease in Km, and an about 3.8fold decrease in kcat, with an overall 2.9fold decrease in catalytic efficiency compared to hNatE alone. The hNatE/HYPK structure reveals a negative cooperative mechanism. Over the HYPK and hNatA interaction interface within the tetrameric complex, polar interactions between HYPK-Glu74 and hNAA15-Tyr158, between the backbone carbonyl of HYPK-Thr100 and hNAA15-Lys687, between the backbone carbonyl of HYPK-Asn129 and hNAA15-Arg697, and between HYPK-Asn129 and hNAA15-Lys696 are observed
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additional information
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