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Literature summary for 2.3.1.258 extracted from
- Biophysical and functional characterizations of recombinant RimI acetyltransferase from Mycobacterium tuberculosis (2019), Acta Biochim. Biophys. Sin. (Shanghai), 51, 960-968 .
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. |
|---|---|---|---|---|---|---|
| additional information | the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE) | Mycobacterium tuberculosis | ? | - |
- |
 |
| 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 | ? | - |
- |
|
| 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
| Subunits | Comment | Organism |
|---|---|---|
| More | 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 |
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