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Information on EC 2.3.1.255 - N-terminal amino-acid Nalpha-acetyltransferase NatA and Organism(s) Mycobacterium tuberculosis and UniProt Accession I6YG32
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2.3.1.255 N-terminal amino-acid Nalpha-acetyltransferase NatAIUBMB Comments
N-terminal-acetylases (NATs) catalyse 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 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.
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Word Map
- 2.3.1.255
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auxiliary
- n-acetyltransferase
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n-termini
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ogden
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co-translationally
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n-alpha-acetylation
- hypk
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cotranslation
- medicine
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(3 overall reactions are displayed. Show all (6)>>)
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an N-terminal-glycyl-[protein]
=
an N-terminal-Nalpha-acetyl-glycyl-[protein]
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an N-terminal-L-alanyl-[protein]
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an N-terminal-Nalpha-acetyl-L-alanyl-[protein]
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an N-terminal-L-seryl-[protein]
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an N-terminal-Nalpha-acetyl-L-seryl-[protein]
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Synonyms
naa15, ard1b, hnaa10, naa11, daf-31, n-terminal acetyltransferase a, arrest-defective protein 1, mtrimi, ta0058, n-alpha-acetyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ARD1
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NAA10
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NAA15
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-terminal-Gly/Ala/Ser/Val/Cys/Thr-[protein] Nalpha-acetyltransferase
N-terminal-acetylases (NATs) catalyse 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 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.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
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?
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
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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
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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
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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
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ir
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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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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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)
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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). RimIMtb acetylates DP9 (NatE substrate) 18fold better than DPC (NatA substrate)
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic analysis of wild-type enzyme and enzyme mutant MtRimIC21A4-153
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additional information
additional information
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kinetic analysis of wild-type enzyme and enzyme mutant MtRimIC21A4-153
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
600
about, purified recombinant RimI, NatA substrate N-terminal L-alanyl-[RYFRR], pH 8.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
physiological function
additional information
physiological function
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
physiological function
RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
additional information
structure modeling and molecular docking of RimI, docking of the structure model of MtRimI-Ala-Arg-Tyr-Phe-Arg-Arg (ARYFRR) complex using the crystal structure of the RimI and bisubstrate from Salmonella typhimurium strain LT2 (PDB 2CNM) as template, overview. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
additional information
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structure modeling and molecular docking of RimI, docking of the structure model of MtRimI-Ala-Arg-Tyr-Phe-Arg-Arg (ARYFRR) complex using the crystal structure of the RimI and bisubstrate from Salmonella typhimurium strain LT2 (PDB 2CNM) as template, overview. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
secondary structure prediction of MtRimI, overview
additional information
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secondary structure prediction of MtRimI, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
additional information
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generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme RimI from Escherichia coli by nickel affinity and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene rimI, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Rv3420c or rimI, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hou, M.; Zhuang, J.; Fan, S.; Wang, H.; Guo, C.; Yao, H.; Lin, D.; Liao, X.
Biophysical and functional characterizations of recombinant RimI acetyltransferase from Mycobacterium tuberculosis
Acta Biochim. Biophys. Sin. (Shanghai)
51
960-968
2019
Mycobacterium tuberculosis (I6YG32), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (I6YG32), Mycobacterium tuberculosis H37Rv (I6YG32)
Pathak, D.; Bhat, A.; Sapehia, V.; Rai, J.; Rao, A.
Biochemical evidence for relaxed substrate specificity of Nalpha-acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis
Sci. Rep.
6
28892
2016
Mycobacterium tuberculosis (I6YG32), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (I6YG32), Mycobacterium tuberculosis H37Rv (I6YG32)
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