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Literature summary for 5.4.99.5 extracted from

  • Schneider, C.Z.; Parish, T.; Basso, L.A.; Santos, D.S.
    The two chorismate mutases from both Mycobacterium tuberculosis and Mycobacterium smegmatis: biochemical analysis and limited regulation of promoter activity by aromatic amino acids (2008), J. Bacteriol., 190, 122-134.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development Since this enzyme is absent from mammals, it represents a promising target for the development of new antimycobacterial drugs, which are needed to combat Mycobacterium tuberculosis, the causative agent of tuberculosis
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Cloned(Commentary)

Cloned (Comment) Organism
Construction of mycobacterial reporter plasmids is described. In contrast to the studies in Mycobacterium tuberculosis, very little is known of CMs in Mycobacterium smegmatis. Homolouges of Rv1885c and Rv0948c are present in the MSMEG5513 have been recently annotated as potential CMs. Rv1885c protein used as a control for the experiments describing Rv0948c and the two Mycobacterium smegmatis homologues Mycolicibacterium smegmatis
in Mycobacterium smegmatis: homologues of each CM from Mycobacterium tuberculosis are found in Mycobacterium smegmatis, a nonpathogenic species. These homologues (which correspond to ORFs MSMEG5513 and MSMEG2114 respectively) cloned, expressed in Escherichia coli (strains DH5alpha, DH10B and BL21(DE3)), and demonstrate to possess CM activity as their Mycobacterium tuberculosis counterparts Mycolicibacterium smegmatis

Protein Variants

Protein Variants Comment Organism
additional information CM enzymes, which are not precisely annotated in the original genome sequence of Mycobacterium tuberculosis H37Rv and the subsequent reannotation. In the annotation, two ORFs (Rv0948c and Rv1885) with some similarity to CMs, including the well-known monofunctional periplasmic CM from Erwinia herbicola, are found, although these ORFs are described as conserved hypothetical proteins
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Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular Rv0948c, the presence of a cleavable signal peptide in Rv1885c strongly suggests that they are exported
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
11700
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the recombinant protein AroQMs in Escherichia coli Mycolicibacterium smegmatis
17800
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in Escherichia coli for the mature *AroQMs protein Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Chorismate Mycolicibacterium smegmatis
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Prephenate
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?
Chorismate
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Prephenate
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?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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Sequence data for Mycobacterium tuberculosis H37Rv and Mycobacterium leprae TN were obtained from the TubercuList (http://genolist.pasteur.fr/TubercuList/) and Leproma (http://genolist.pasteur.fr/Leproma/) databases; intracellular pathogen, studies of construction of mycobacterial reporter plasmids, organization of Rv0948c and Rv1885c promoter region, analysis of promoter activity
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Mycolicibacterium smegmatis A0QU81 nonpathogenic species, Analysis of promoter activity described
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no activity in Corynebacterium diphtheriae
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-
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no activity in Mycobacterium leprae
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-
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no activity in Nocardia farcinica
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-
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Purification (Commentary)

Purification (Comment) Organism
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Mycolicibacterium smegmatis

Reaction

Reaction Comment Organism Reaction ID
Chorismate = prephenate CMs are extremly versatile enzymes and can be structurally divided into two major groups: the type I or AroH class, which comprises CMs characterized by a trimericpseudo alpha/beta-barrel structure, and the type II or AroQ class, which comprises CMs can also be monofunctional, bifunctional (generally fused to another shikimate pathway member), exported, and/or allosterically regulated Mycolicibacterium smegmatis
Chorismate = prephenate CMs are extremly versatile enzymes and can be strucurally divided into two major groups: the type I or AroH class, which comprises CMs characterized by a trimericpseudo alpha/beta-barrel structure, and the type II or AroQ class, which comprises CMs, can also be monofunctional, bifunctional (generally fused to another shikimate pathway member), exported, and/or allosterically regulated
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
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Mycolicibacterium smegmatis Prephenate
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?
Chorismate
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Prephenate
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?
additional information It is possible that an extracellular biosynthetic pathway from chorismate to phenylalanine exists in Mycobacterium smegmatis, even if the function of such putative route is presently obscure Mycolicibacterium smegmatis ?
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?

Synonyms

Synonyms Comment Organism
chorismate mutase
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Mycolicibacterium smegmatis
chorismate mutase
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Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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assay at Mycolicibacterium smegmatis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
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additional information CM spezific activity in Escherichia coli extracts: Control (M. Tuberculosis) Sp act (U/mg) 0.889 Cloned extract/control 1 AroQMt (Rv0948c) Sp act (U/mg) 127.38 Cloned extract/control 143.28 *AroQMt (Rv1885c) Sp act (U/mg) 94.23 Cloned extract/control 105.9. CM specific activity in Escherichia coli cells expressing either the AroQMt or the *AroQMt protein is determined to be, repectively, 143- and 106-fold higher than the enzyme activity obtained for Escherichia coli cells carrying the pET-23a(+) expression vector Triticum urartu

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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assay at Mycolicibacterium smegmatis