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acetyl-CoA + AAKKRG
CoA + N-acetyl-AAKKRG
-
-
-
?
acetyl-CoA + ACTH peptide
CoA + ?
-
17 amino acids are identical to the adrenocorticotropin (ACTH) peptide sequence, the ACTH-derived lysines are replaced by arginines to minimize any potential interference by Nalpha-acetylation
-
-
?
acetyl-CoA + actin
?
-
-
-
-
?
acetyl-CoA + an N-terminal-amino acid-[protein]
an N-terminal-Nalpha-acetyl-amino acid-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA
acetyl-CoA + an N-terminal-lysinyl-[androgen receptor]
an N-terminal-Nalpha-acetyl-lysinyl-[androgen receptor] + CoA
-
ARD1 acetylates androgen receptor at lysine 618
-
-
?
acetyl-CoA + an N-terminal-methionyl-[RPM1 protein]
an N-terminal-Nalpha-acetyl-methionyl-[RPM1 protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-methionyl-[SNC1 protein]
an N-terminal-Nalpha-acetyl-methionyl-[SNC1 protein] + CoA
-
NatA specifically acetylates the first met of SNC1 protein
-
-
?
acetyl-CoA + beta-catenin
?
-
-
-
-
?
acetyl-CoA + CAP2
?
-
-
-
-
?
acetyl-CoA + DDDIAAL
CoA + N-acetyl-DDDIAAL
-
-
-
?
acetyl-CoA + DDDIAALRWGRPVGRRRRPVRVYP
CoA + Nalpha-acetyl-DDDIAALRWGRPVGRRRRPVRVYP
-
-
-
?
acetyl-CoA + EEEIAAL
CoA + N-acetyl-EEEIAAL
best substrate
-
-
?
acetyl-CoA + EEEIAALRWGRPVGRRRRPVRVYP
CoA + Nalpha-acetyl-EEEIAALRWGRPVGRRRRPVRVYP
-
-
-
?
acetyl-CoA + GRX3
?
-
-
-
-
?
acetyl-CoA + MEEKVG
CoA + N-acetyl-MEEKVG
-
-
-
?
acetyl-CoA + MLCK
?
-
-
-
-
?
acetyl-CoA + MLGPEGG
CoA + N-acetyl-MLGPEGG
poor substrate
-
-
?
acetyl-CoA + MLGPEGGRWGRPVGRRRRPVRVYP
CoA + Nalpha-acetyl-MLGPEGGRWGRPVGRRRRPVRVYP
-
-
-
?
acetyl-CoA + MSRA
?
-
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
acetyl-CoA + N-terminal L-alanyl-[KVNIK]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[KVNIK]
acetyl-CoA + N-terminal L-alanyl-[RYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[RYFRR]
acetyl-CoA + N-terminal L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-aspartyl-[DDDIAALRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
acetyl-CoA + N-terminal L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-glutamyl-[EEEIAALRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
acetyl-CoA + N-terminal L-methionyl-[LGPEGGRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-methionyl-[LGPEGGRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-methionyl-[LGPEGGRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-methionyl-[MLGPEGGRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-methionyl-[MMP2]
CoA + H+ + N-terminal Nalpha-acetyl-L-methionyl-[MMP2]
matrix metalloproteinase-2, MMP2, with sequence MEALMAR
-
-
?
acetyl-CoA + N-terminal L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
acetyl-CoA + N-terminal L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[SESSSKSRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-seryl-[KLIEY]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[KLIEY]
acetyl-CoA + N-terminal L-seryl-[RVQIS]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[RVQIS]
acetyl-CoA + NTF2
?
-
-
-
-
?
acetyl-CoA + Orc1p
CoA + Nalpha-acetyl-[Orc1p]
acetyl-CoA + PCNP protein
CoA + Nalpha-acetyl-PCNP protein
-
i.e. PEST proteolytic signal-containing nuclear protein
-
-
?
acetyl-CoA + PDC5
?
-
-
-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
acetyl-CoA + peptide
Nalpha-acetylpeptide + CoA
acetyl-CoA + PIL1
?
-
-
-
-
?
acetyl-CoA + POL30
?
-
-
-
-
?
acetyl-CoA + QVATYHRAIKVTVDGPRW
?
-
-
-
-
?
acetyl-CoA + RAD23
?
-
-
-
-
?
acetyl-CoA + RKEQTPVAAKHHVNGNRTVW
?
-
-
-
-
?
acetyl-CoA + RPS12
?
-
-
-
-
?
acetyl-CoA + RUP2
?
-
-
-
-
?
acetyl-CoA + SASEAGVRWGRPVGRRRRP
CoA + Nalpha-acetyl-SASEAGVRWGRPVGRRRRP
-
-
-
?
acetyl-CoA + SESSSKS
CoA + N-acetyl-SESSSKS
-
-
-
?
acetyl-CoA + SESSSKSRWGRPVGRRRRPVRVYP
CoA + Ac-SESSSKSRWGRPVGRRRRPVRVYP
-
high-mobility-group protein A1 sequence
-
-
?
acetyl-CoA + SESSSKSRWGRPVGRRRRPVRVYP
CoA + Nalpha-acetyl-SESSSKSRWGRPVGRRRRPVRVYP
-
-
-
?
acetyl-CoA + silencing facor Sir3p
CoA + Nalpha-acetyl-[silencing factor Sir3p]
acetyl-CoA + SMI1
?
-
-
-
-
?
acetyl-CoA + SNZ2/3
?
-
-
-
-
?
acetyl-CoA + SSGTPT
CoA + N-acetyl-SSGTPT
-
-
-
?
acetyl-CoA + THI20
?
-
-
-
-
?
acetyl-CoA + THI22
?
-
-
-
-
?
acetyl-CoA + THI4
?
-
-
-
-
?
acetyl-CoA + THI6
?
-
-
-
-
?
acetyl-CoA + TIF6
?
-
-
-
-
?
acetyl-CoA + TVHEKKSSRKSEYLLPVAW
?
-
-
-
-
?
acetyl-CoA + VMA6
?
-
-
-
-
?
acetyl-CoA + ZPS1
?
-
-
-
-
?
acetyl-CoA + [histone 2B]
an N-terminal-Nalpha-acetyl-[histone 2B] + CoA
-
-
-
-
?
acetyl-CoA + [iso-1-cytochrome c]
an N-terminal-Nalpha-acetyl-[iso-1-cytochrome c] + CoA
-
-
-
-
?
acetyl-CoA + [Runx2]
[Runx2]-N-terminal-N6-acetyl-L-lysine + CoA
additional information
?
-
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[KVNIK]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[KVNIK]
DP7 peptide (AKVNIK) is a substrate of NatA and is derived from the protein endoded by groES/Rv3418c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[KVNIK]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[KVNIK]
DP7 peptide (AKVNIK) is a substrate of NatA and is derived from the protein endoded by groES/Rv3418c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[KVNIK]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[KVNIK]
DP7 peptide (AKVNIK) is a substrate of NatA and is derived from the protein endoded by groES/Rv3418c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[RYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[RYFRR]
DPC peptide (ARYFRR) is a substrate of NatA and is derived from the sequence of S18 RNA protein rpsRS18 of Salmonella typhimurium
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[RYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[RYFRR]
DPC peptide (ARYFRR) is a substrate of NatA and is derived from the sequence of S18 RNA protein rpsRS18 of Salmonella typhimurium
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[RYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[RYFRR]
DPC peptide (ARYFRR) is a substrate of NatA and is derived from the sequence of S18 RNA protein rpsRS18 of Salmonella typhimurium
-
-
ir
acetyl-CoA + N-terminal L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
-
-
-
ir
acetyl-CoA + N-terminal L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
-
-
-
ir
acetyl-CoA + N-terminal L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
substrate SESS
-
-
?
acetyl-CoA + N-terminal L-seryl-[KLIEY]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[KLIEY]
DP6 peptide (SKLIEY) is a substrate of NatA and is derived from the protein endoded by tsaE/Rv3422c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[KLIEY]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[KLIEY]
DP6 peptide (SKLIEY) is a substrate of NatA and is derived from the protein endoded by tsaE/Rv3422c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[KLIEY]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[KLIEY]
DP6 peptide (SKLIEY) is a substrate of NatA and is derived from the protein endoded by tsaE/Rv3422c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[RVQIS]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[RVQIS]
DP4 peptide (SRVQIS) is a substrate of NatA and is derived from the protein endoded by tsaB/Rv3421c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[RVQIS]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[RVQIS]
DP4 peptide (SRVQIS) is a substrate of NatA and is derived from the protein endoded by tsaB/Rv3421c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[RVQIS]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[RVQIS]
DP4 peptide (SRVQIS) is a substrate of NatA and is derived from the protein endoded by tsaB/Rv3421c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + Orc1p
CoA + Nalpha-acetyl-[Orc1p]
-
-
-
-
?
acetyl-CoA + Orc1p
CoA + Nalpha-acetyl-[Orc1p]
-
Orc1p is the large subunit of the origin recognition complex, ORC. Mechanism for modulating chromaffin function
-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
-
-
-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
-
NatA acetylation is important for function of a set of proteins involved in general groth control
-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
-
acetylates N-terminal Ser, Ala, Gly or Thr residues
-
-
?
acetyl-CoA + peptide
Nalpha-acetylpeptide + CoA
-
-
-
-
?
acetyl-CoA + peptide
Nalpha-acetylpeptide + CoA
-
-
-
-
?
acetyl-CoA + silencing facor Sir3p
CoA + Nalpha-acetyl-[silencing factor Sir3p]
-
-
-
-
?
acetyl-CoA + silencing facor Sir3p
CoA + Nalpha-acetyl-[silencing factor Sir3p]
-
mechanism for modulating chromaffin function
-
-
?
acetyl-CoA + [Runx2]
[Runx2]-N-terminal-N6-acetyl-L-lysine + CoA
-
-
-
-
?
acetyl-CoA + [Runx2]
[Runx2]-N-terminal-N6-acetyl-L-lysine + CoA
NAA10 acetylates Runx2 at Lys225
-
-
?
additional information
?
-
N-terminal EEEI is acetylated 3fold more than the DDDI substrate, which again is preferred almost 2fold to SESS, the canonical NatA substrate
-
-
?
additional information
?
-
-
N-terminal EEEI is acetylated 3fold more than the DDDI substrate, which again is preferred almost 2fold to SESS, the canonical NatA substrate
-
-
?
additional information
?
-
enzyme zNaa10 has a predicted N-terminal activity with identical substrate specificity to human Naa10 in vitro
-
-
-
additional information
?
-
-
endogenous HYPK, a Huntingtin (Htt)-interacting protein, is a stable interactor of NatA, the C terminus of hNaa15p of NatA specifically interacts directly with HYPK, no interaction with hNaa25p of hNatB and hNaa35p of hNatC
-
-
?
additional information
?
-
enzyme variant ARD1131 has no autoacetylation activity
-
-
?
additional information
?
-
-
N-terminal acetyltransferase Naa10/ARD1 does not acetylate lysine residues
-
-
?
additional information
?
-
Naa10 undergoes autoacetylation at lysine K136
-
-
?
additional information
?
-
lysine acetyltransferase (KAT) activity of recombinant human ARD1/NAA10, overview. Arrest defective 1 (ARD1) is the only enzyme known so far to exhibit both N-terminal acetyltransferase (NAT) and N-terminal lysine acetyltransferase (KAT) activities. Only the monomeric rhARD1/NAA10 form, but not by the oligomeric form, can acetylate lysine residues of substrate proteins
-
-
-
additional information
?
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
additional information
?
-
no activity with an MMP2 mutated at the acetylytion site of Naa10
-
-
-
additional information
?
-
recombinant hARD1/NAA10 exhibits KAT activity, which disappears soon in vitro due to enzyme oligomerization, which results in the loss of KAT activity. While oligomeric recombinant hARD1/NAA10 loses its ability for lysine acetylation, its monomeric form clearly exhibits lysine acetylation activity in vitro. Assay optimization, under optimal conditions, hARD1/NAA10 retains its KAT activity, overview
-
-
-
additional information
?
-
substrates are SESS24 or EEEI24. The ability of NAA10-V111G to acetylate the acidic N-termini EEEI24 is highly reduced compared to wild-type enzyme
-
-
-
additional information
?
-
-
substrates are SESS24 or EEEI24. The ability of NAA10-V111G to acetylate the acidic N-termini EEEI24 is highly reduced compared to wild-type enzyme
-
-
-
additional information
?
-
ARD1 and NAT1 constitute an N-acetyltransferase complex where ARD1 holds the enzymatic activity of the complex. The ARD1-NAT1 complex mediates N-terminal acetylation of nascent polypeptides that emerge from ribosomes after translation. ARD1 may also acetylate the internal lysine residues of proteins
-
-
?
additional information
?
-
acetylation of alpha-tubulin
-
-
-
additional information
?
-
acetylation of alpha-tubulin
-
-
-
additional information
?
-
acetylation of alpha-tubulin
-
-
-
additional information
?
-
acetylation of alpha-tubulin
-
-
-
additional information
?
-
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 acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins. The NatB substrate peptide MERYFRR is a poor substrate for RimI. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed against peptide representing N-terminus of GroES
-
-
-
additional information
?
-
-
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 acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins. The NatB substrate peptide MERYFRR is a poor substrate for RimI. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed against peptide representing N-terminus of GroES
-
-
-
additional information
?
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE). RimIMtb acetylates DP9 (NatE substrate) 18fold better than DPC (NatA substrate)
-
-
-
additional information
?
-
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE). RimIMtb acetylates DP9 (NatE substrate) 18fold better than DPC (NatA substrate)
-
-
-
additional information
?
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE). RimIMtb acetylates DP9 (NatE substrate) 18fold better than DPC (NatA substrate)
-
-
-
additional information
?
-
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 acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins. The NatB substrate peptide MERYFRR is a poor substrate for RimI. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed against peptide representing N-terminus of GroES
-
-
-
additional information
?
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE). RimIMtb acetylates DP9 (NatE substrate) 18fold better than DPC (NatA substrate)
-
-
-
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 acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins. The NatB substrate peptide MERYFRR is a poor substrate for RimI. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed against peptide representing N-terminus of GroES
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additional information
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both proteins ARD1 and NAT1 are required for the N-terminal acetyltransferase activity of the ARD1-NAT1 complex
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additional information
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typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
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typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
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typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. 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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