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Literature summary for 5.4.99.5 extracted from
- Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids (2006), J. Bacteriol., 188, 8638-8648.
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | advantage of the nonoccurance of CMs in human, develop antimicrobial drugs to combat dreaded human pathogens such as Mycobacterium tuberculosis | Mycobacterium tuberculosis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| Escherichia coli strains C600lambda lysogen, MZ1, Nova Blue, BL21(DE3) | Mycobacterium tuberculosis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| Analysis of the structure shows a novel fold topology for the protein with a topologically rearranged helix containing R134. *MtCM does not have an allosteric regulation site | Mycobacterium tuberculosis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D69A | site directed mutagenesis constitute the catalytic site | Mycobacterium tuberculosis |
| E109A | site directed mutagenesis constitute the catalytic site | Mycobacterium tuberculosis |
| E109Q | site directed mutagenesis constitute the catalytic site | Mycobacterium tuberculosis |
| K60A | site directed mutagenesis constitute the catalytic site | Mycobacterium tuberculosis |
| additional information | The results of the mutagenesis and the activity show that Arg49, Lys 60, Arg72, and Arg134 are essential for catalysis | Mycobacterium tuberculosis |
| R134A | site directed mutagenesis constitute the catalytic site | Mycobacterium tuberculosis |
| R49A | site directed mutagenesis constitute the catalytic site | Mycobacterium tuberculosis |
| R72A | site directed mutagenesis constitute the catalytic site | Mycobacterium tuberculosis |
| Y105A | site directed mutagenesis constitute the catalytic site | Mycobacterium tuberculosis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | *MtCM is not regulated by the aromatic amino acids. The x-ray structure of *MtCM does not have an allosteric regulatory site in the protein | Mycobacterium tuberculosis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | A lower Km of 0.5 +/-0.05 mM is obtained with a 27.5 nM protein concentration (11 pmol) whereas a Km of 0.67 +/-0.05 nM is obtained with a 8 nM protein concentration (3.2 pmol) | Mycobacterium tuberculosis | |
| 0.5 | - |
chorismate | +/-0.05, substrate chorismate | Mycobacterium tuberculosis |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | absence of a discrete periplasmic compartment in Mycobacterium tuberculosis. *MtCM is secreted out of the cytoplasm and through the unusual architecture of the mycobacterial cell wall | Mycobacterium tuberculosis | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 18747 | - |
2 * 18747, all alpha-helical bundle structure, two monomeric subunits | Mycobacterium tuberculosis |
| 37000 | - |
monomeric molecular mass 18474 Da. Absorbance, liquid chromatography-mass spectrometry | Mycobacterium tuberculosis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Chorismate | Mycobacterium tuberculosis | - |
Prephenate | - |
? | |
| Chorismate | Mycobacterium tuberculosis H37Rv | - |
Prephenate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | P9WIB9 | - |
- |
| Mycobacterium tuberculosis H37Rv | P9WIB9 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Mycobacterium tuberculosis |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| Chorismate = prephenate | the active site is formed within a single chain without any contribution from the second chain in a dimer | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Chorismate | - |
Mycobacterium tuberculosis | Prephenate | - |
? | |
| Chorismate | - |
Mycobacterium tuberculosis H37Rv | Prephenate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 18747, all alpha-helical bundle structure, two monomeric subunits | Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| chorismate mutase | belongs to the *AroQclass of chorismate mutases | Mycobacterium tuberculosis |
| MtCM | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
at assay | Mycobacterium tuberculosis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 60 | - |
chorismate | +/-4, substrate chorismate | Mycobacterium tuberculosis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Mycobacterium tuberculosis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 7.5 | - |
Mycobacterium tuberculosis |
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