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
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2.3.1.258
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auxiliary
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nt-acetylation
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bisubstrate
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n-acetyltransferase
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n-termini
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drug-induced
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tunnel
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chromatid
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sister
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acetylome
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nalpha-terminal
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co-translationally
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medicine
- 2.3.1.258
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auxiliary
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nt-acetylation
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bisubstrate
- n-acetyltransferase
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n-termini
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drug-induced
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tunnel
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chromatid
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sister
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acetylome
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nalpha-terminal
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co-translationally
- medicine
Reaction
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
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Substrates Products
Substrates Products on EC 2.3.1.258 - N-terminal methionine Nalpha-acetyltransferase NatE
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REACTION DIAGRAM
acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-alanyl-[protein] + CoA
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?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
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?
acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-lysyl-[protein] + CoA
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?
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
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best substrate
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?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-L-tyrosyl-[Scc1 protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-L-tyrosyl-[Scc1 protein] + CoA
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?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalany-[protein] + CoA
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?
acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-seryl-[protein] + CoA
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?
acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-threonyl-[protein] + CoA
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?
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
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?
acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-valyl-[protein] + CoA
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?
acetyl-CoA + MLGPEGGRWGRPVGRRRRP
acetyl-CoA + Nalpha-acetyl-MLGPEGGRWGRPVGRRRRP
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acetyl-CoA + MMAA
Nalpha-acetyl-MMAA + CoA
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substrate with highest catalytic efficiency
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acetyl-CoA + N-terminal L-methionyl-[ARYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-methionyl-[ARYFRR]
DP9 peptide (MARYFRR) is a substrate of NatE, a synthetic peptide
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ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
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ir
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
peptide substrate binding structure, overview
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ectopically expressed hNaa50 results, predominantly, in the N-terminal-acetylation of N-terminal Met (iMet) starting N-termini, including iMet-Lys, iMet-Val, iMet-Ala, iMet-Tyr, iMet-Phe, iMet-Leu, iMet-Ser, and iMet-Thr N-termini. Presence of a kinetic competition between Naa50 and Met-aminopeptidases
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additional information
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Naa50p (Nat5/San) displays both protein Nalpha- and Nepsilon-acetyltransferase activity
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additional information
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Naa50p also possesses Nepsilon-autoacetylation activity
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additional information
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Naa50p also possesses Nepsilon-autoacetylation activity
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additional information
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no activity with peptides SESSRRR, SYSMRRR, and DDIARRR
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additional information
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preferably the enzyme acetylates oligopeptides with N-termini Met-Leu-Xxx-Pro. Furthermore, the enzyme autoacetylates lysines 34, 37, and 140 in vitro as well as histone 4
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additional information
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the enzyme acetylates all MXAA peptides except for MPAA
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additional information
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complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
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additional information
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complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
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additional information
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N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
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analysis of substrate preference of RimIMtb: substrate peptide DPC (NatA substrate) is custom synthesized with single residue modifications at its N-terminus to represent substrate specificities of NatE (DP9), NatB (DP10), NatC (DP11), and substrate Leu (DP8) and tested, all the peptides are modified by RimIMtb, substrates and sequences, detailed overview. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES. RimIMtb acetylates DP9 (NatE substrate) 2.1fold better than DPC (NatA substrate). RimIMtb acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins
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additional information
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the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE)
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additional information
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the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE)
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additional information
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the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE)
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additional information
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potential substrates that are less acetylated in strains lacking isoform Naa50 are: vacuolar morphogenesis protein 7, nuclear cap-binding protein subunit 2, 60S ribosomal protein L16-A, aromatic amino acid aminotransferase 1, tRNA guanosine-2'-O-methyltransferase TRM3, low specificity L-threonine aldolase
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additional information
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N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
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N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
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N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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