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Literature summary extracted from

  • Okvist, M.; Dey, R.; Sasso, S.; Grahn, E.; Kast, P.; Krengel, U.
    1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed (2006), J. Mol. Biol., 357, 1483-1499.
    View publication on PubMed

Application

EC Number Application Comment Organism
5.4.99.5 drug development fighting diseases such as tuberculosis. Since vertebrates lack the shikimate pathway for the biosynthesis of aromatic compounds and thus do not possess chorismate mutase activity, this enzyme represents a prime target for the development of antibiotics, fungicides and herbicides Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.5 Escherichia coli strain KA29 Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.5 37.2 kDa. Each asymmetric unit contains a homodimer, corresponding to the two protomers of the biological dimer. *MtCM as a model system for the *AroQ subclass and determined its crystal structure at high resolution, both in its unliganded form and in complex with transition state analog (1S,3S,5R,6R)-6-hydroxy-4-oxabicyco[3.3.1]non-7-ene-1,3-dicarboxylic acid. Heavy-atom derivatives prepared. Successful heavy-atom compounds are lead (II) acetate and thallium (III) acetate Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.99.5 (1S,3S,5R,6R)-6-hydroxy-4-oxabicyclo[3.3.1]non-7-ene-1,3-dicarboxylate endo-oxabicyclic dicarboxylic acid is a good geometric mimic of transition state 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 *MtCM, which has a melting temperature of 48°C, rapidly renatures after heat denaturation, and have subsequently exploited this feature for purifying the enzyme Mycobacterium tuberculosis

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 dimer Each assymmetric unit contains a homodimer, corresponding to the two protomers (A and B) of the biological dimer. The structure of a *MtCM protomer strongly resembles the fold of the EcCM dimer, which consists of two intertwined subunits of three helices each and which comprises two active sites Mycobacterium tuberculosis
5.4.99.5 More Ligand-induced structural changes are shown. Experiments neither show evidence for an equilibrium between the dimer and a *MtCM dimer of an intertwined nature, nor for an equilibrium with a monomer at lower protein concentrations as observed for engineered topology variants of chorismate mutases. The active site of *MtCM is highly similar to the catalytic sites of the other structurally characterized AroQ chorismate mutases Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
5.4.99.5 chorismate mutase
-
 Mycobacterium tuberculosis
5.4.99.5 MtCM
-
 Mycobacterium tuberculosis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.4.99.5 additional information
-
 *MtCM melting temperature of 48°C Mycobacterium tuberculosis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.4.99.5 5 9 the catalytic efficiency (kcat/Km) of *MtCM increases by two orders of magnitude upon decreasing the pH from 9 to 5 Mycobacterium tuberculosis