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Literature summary extracted from

  • 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 (2019), Acta Biochim. Biophys. Sin. (Shanghai), 51, 960-968 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.255 gene rimI, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis
2.3.1.258 gene rimI, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.255 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 Mycobacterium tuberculosis
2.3.1.258 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 Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.255 additional information
-
 additional information kinetic analysis of wild-type enzyme and enzyme mutant MtRimIC21A4-153 Mycobacterium tuberculosis
2.3.1.258 additional information
-
 additional information kinetic analysis of wild-type enzyme and enzyme mutant MtRimIC21A4-153 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.255 Mycobacterium tuberculosis I6YG32
-
-
2.3.1.255 Mycobacterium tuberculosis ATCC 25618 I6YG32
-
-
2.3.1.255 Mycobacterium tuberculosis H37Rv I6YG32
-
-
2.3.1.258 Mycobacterium tuberculosis I6YG32
-
-
2.3.1.258 Mycobacterium tuberculosis ATCC 25618 I6YG32
-
-
2.3.1.258 Mycobacterium tuberculosis H37Rv I6YG32
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.255 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Mycobacterium tuberculosis
2.3.1.258 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.255 acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
 Mycobacterium tuberculosis CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
 ?
2.3.1.255 acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
 Mycobacterium tuberculosis H37Rv CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
 ?
2.3.1.255 acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
 Mycobacterium tuberculosis ATCC 25618 CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
 ?
2.3.1.255 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) Mycobacterium tuberculosis ?
-
-
2.3.1.255 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) Mycobacterium tuberculosis H37Rv ?
-
-
2.3.1.255 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) Mycobacterium tuberculosis ATCC 25618 ?
-
-
2.3.1.258 additional information the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE) Mycobacterium tuberculosis ?
-
-
2.3.1.258 additional information the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE) Mycobacterium tuberculosis H37Rv ?
-
-
2.3.1.258 additional information the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE) Mycobacterium tuberculosis ATCC 25618 ?
-
-

Subunits

EC Number Subunits Comment Organism
2.3.1.255 More secondary structure prediction of MtRimI, overview Mycobacterium tuberculosis
2.3.1.258 More secondary structure prediction of MtRimI, overview Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.3.1.255 MtRimI
-
 Mycobacterium tuberculosis
2.3.1.255 Nalpha-acetyltransferase
-
 Mycobacterium tuberculosis
2.3.1.255 RimI
-
 Mycobacterium tuberculosis
2.3.1.255 RimI acetyltransferase
-
 Mycobacterium tuberculosis
2.3.1.258 MtRimI
-
 Mycobacterium tuberculosis
2.3.1.258 Nalpha-acetyltransferase
-
 Mycobacterium tuberculosis
2.3.1.258 RimI
-
 Mycobacterium tuberculosis
2.3.1.258 RimI acetyltransferase
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.255 25
-
 assay at Mycobacterium tuberculosis
2.3.1.258 25
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.255 7.5
-
 assay at Mycobacterium tuberculosis
2.3.1.258 7.5
-
 assay at Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.255 acetyl-CoA
-
 Mycobacterium tuberculosis
2.3.1.258 acetyl-CoA
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.255 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 Mycobacterium tuberculosis
2.3.1.255 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 Mycobacterium tuberculosis
2.3.1.255 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 Mycobacterium tuberculosis
2.3.1.258 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 Mycobacterium tuberculosis
2.3.1.258 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 Mycobacterium tuberculosis
2.3.1.258 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 Mycobacterium tuberculosis