Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.255 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
Search for more literature for 2.3.1.255

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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]

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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis I6YG32
-
-
Mycobacterium tuberculosis ATCC 25618 I6YG32
-
-
Mycobacterium tuberculosis H37Rv I6YG32
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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]
-
 ?
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]
-
 ?
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]
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Subunits

Subunits Comment Organism
additional information secondary structure prediction of MtRimI, overview Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
MtRimI
-
 Mycobacterium tuberculosis
Nalpha-acetyltransferase
-
 Mycobacterium tuberculosis
RimI
-
 Mycobacterium tuberculosis
RimI acetyltransferase
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
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
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
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