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Literature summary extracted from

  • Qamra, R.; Prakash, P.; Aruna, B.; Hasnain, S.E.; Mande, S.C.
    The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions (2006), Biochemistry, 45, 6997-7005.
    View publication on PubMed

Application

EC Number Application Comment Organism
5.4.99.5 drug development MtCM might play a role in host-pathogen interactions, making it an important target for designing inhibitor molecules against the deadly pathogen Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.5 overexpressed in Escherichia coli BL21 (DE3). Mycobacterium tuberculosis CMs are believed to have evolved from duplication of an ancestral CM gene, formation of the active site in a single polypeptide chain appears to be a consequence of this duplication event Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.5 of the homodimeric chorismate mutase (Rv1885c). The crystal structure corresponds to the AroQ class CM of Mycobacterium tuberculosis. Determination of the crystal structure of the unique extracytoplasmic MtbCM in complex with its allosteric ligand, L-Trp. Se-Met MtbCM crystallizes in space group C2 in the presence of Trp. The Mycobacterium tuberculosis enzyme is an all-helical protein. Structural comparisons show that CMs from different organisms have envolved into two completely unrelated protein folds, suggesting separate evolutionary origins of the enzyme. On the basis of the structural fold adopted by the protein, CMs have been classified into the AroH and AroQ classes Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.99.5 L-tryptophan allosteric. The Trp at the dimer interface interacts extensively with residues from both subunits. The unexpected gene duplication possibly leads to a different allosteric regulation mechanism than that is known for other CMs Mycobacterium tuberculosis
5.4.99.5 additional information Unlike the other known prokaryotic CMs, the Mycobacterium tuberculosis enzyme exhibits allosteric regulation by aromatic amino acids, a feature limited to the eukaryotic CMs. The active site of MtbCM is seen to be blocked due to the presence of a sulfate ion in the structure. It therefore appears that sulphate acts as an inhibitor of the enzyme by blocking the entry of the substrate into the active site. In MtbCM the allosteric site is close to the active site Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.4.99.5 extracellular Mycobacterium tuberculosis enzyme has been shown to be secreted into the extracellular medium Mycobacterium tuberculosis
-
-
5.4.99.5 additional information Only one of the gene products is secreted into the extracellular space. This observation strongly suggests that while the cytosolic enzyme might have retained its role in the aromatic amino acid synthesis pathway, the secreted enzyme is likely to have evolved a distinct role, such as aiding the bacterium in its pathogenesis 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
-
?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.5
-
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
-
?

Subunits

EC Number Subunits Comment Organism
5.4.99.5 homodimer The regulating Trp ligand is found to be sandwiched between the two monomers in a dimer containing residues 66-68 Mycobacterium tuberculosis
5.4.99.5 More In MtbCM, while one face of helix 3 contributes to residues involved in monomer-monomer contracts and the allosteric site, the other face contributes to residues involved in the interaction with the substrate. The active site in the gene duplicated monomer is occupied by a sulfate ion and is located in the second half of the polypeptide Mycobacterium tuberculosis

Synonyms

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

pH Optimum

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