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Literature summary extracted from

  • Kim, S.K.; Reddy, S.K.; Nelson, B.C.; Vasquez, G.B.; Davis, A.; Howard, A.J.; Patterson, S.; Gilliland, G.L.; Ladner, J.E.; Reddy, P.T.
    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.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
5.4.99.5 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)

EC Number Cloned (Comment) Organism
5.4.99.5 Escherichia coli strains C600lambda lysogen, MZ1, Nova Blue, BL21(DE3) Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.5 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

EC Number Protein Variants Comment Organism
5.4.99.5 D69A site directed mutagenesis constitute the catalytic site Mycobacterium tuberculosis
5.4.99.5 E109A site directed mutagenesis constitute the catalytic site Mycobacterium tuberculosis
5.4.99.5 E109Q site directed mutagenesis constitute the catalytic site Mycobacterium tuberculosis
5.4.99.5 K60A site directed mutagenesis constitute the catalytic site Mycobacterium tuberculosis
5.4.99.5 additional information The results of the mutagenesis and the activity show that Arg49, Lys 60, Arg72, and Arg134 are essential for catalysis Mycobacterium tuberculosis
5.4.99.5 R134A site directed mutagenesis constitute the catalytic site Mycobacterium tuberculosis
5.4.99.5 R49A site directed mutagenesis constitute the catalytic site Mycobacterium tuberculosis
5.4.99.5 R72A site directed mutagenesis constitute the catalytic site Mycobacterium tuberculosis
5.4.99.5 Y105A site directed mutagenesis constitute the catalytic site Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.99.5 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.4.99.5 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
5.4.99.5 0.5
-
 chorismate +/-0.05, substrate chorismate Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.4.99.5 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.4.99.5 18747
-
 2 * 18747, all alpha-helical bundle structure, two monomeric subunits Mycobacterium tuberculosis
5.4.99.5 37000
-
 monomeric molecular mass 18474 Da. Absorbance, liquid chromatography-mass spectrometry Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.5 Chorismate Mycobacterium tuberculosis
-
 Prephenate
-
 ?
5.4.99.5 Chorismate Mycobacterium tuberculosis H37Rv
-
 Prephenate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.5 Mycobacterium tuberculosis P9WIB9
-
-
5.4.99.5 Mycobacterium tuberculosis H37Rv P9WIB9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.5
-
 Mycobacterium tuberculosis

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.99.5 Chorismate = prephenate the active site is formed within a single chain without any contribution from the second chain in a dimer Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.5 Chorismate
-
 Mycobacterium tuberculosis Prephenate
-
 ?
5.4.99.5 Chorismate
-
 Mycobacterium tuberculosis H37Rv Prephenate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.4.99.5 homodimer 2 * 18747, all alpha-helical bundle structure, two monomeric subunits Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
5.4.99.5 chorismate mutase belongs to the *AroQclass of chorismate mutases Mycobacterium tuberculosis
5.4.99.5 MtCM
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.4.99.5 37
-
 at assay Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.4.99.5 60
-
 chorismate +/-4, substrate chorismate Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.99.5 7.5
-
-
 Mycobacterium tuberculosis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.4.99.5 4 7.5
-
 Mycobacterium tuberculosis