Biochemical and Structural Characterization of the Secreted Chorismate Mutase (Rv1885c) from
 Mycobacterium tuberculosis
 H
 37
 R
 v
 : an *AroQ Enzyme Not Regulated by the Aromatic Amino Acids

Kim, Sook-Kyung; Reddy, Sathyavelu K.; Nelson, Bryant C.; Vasquez, Gregory B.; Davis, A. W.; Howard, Andrew; Patterson, S. Dale; Gilliland, Gary L.; Ladner, Jane E.; Reddy, P.G.

doi:10.1128/jb.00441-06

Cited by 47 publications

(45 citation statements)

References 57 publications

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“…The ScCM of S. cerevisiae and AnCM of Aspergillus nidulans are inhibited by Tyr and Phe and are stimulated by Trp (Krappmann et al, 1999;Schmidheini et al, 1989). Similar to MtbCM (Kim et al, 2006), CM0819 in C. glutamicum is not subject to any regulation by aromatic amino acids. But CM0819 together with chorismate and prephenate regulates DS2098 activity via allosteric inhibition, similar to what was observed for the bifunctional CM from B. subtilis (Jensen & Nester, 1965).…”

Section: Discussionmentioning

confidence: 77%

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Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum

Liu

2009

Microbiology

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Chorismate mutase (CM) catalyses the rearrangement of chorismate to prephenate and is also the first and the key enzyme that diverges the shikimate pathway to either tryptophan (Trp) or phenylalanine (Phe) and tyrosine (Tyr). Corynebacterium glutamicum is one of the most important amino acid producers for the fermentation industry and has been widely investigated. However, the gene(s) encoding CM has

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Section: Discussionmentioning

confidence: 77%

“…There was no observable feedback regulation of CM activity at concentrations of 0.01-10 mM of any of Phe, Trp or Tyr. This is similar to MtbCM from Mycobacterium tuberculosis, which was not subject to feedback regulation by Phe, Trp or Tyr (Kim et al, 2006).…”

Section: Cm0819 Activity Is Not Regulated By Phe Tyr and Trp But Ismentioning

confidence: 78%

Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum

Liu

2009

Microbiology

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“…These enzymes consist of three constitutively expressed subtypes: a monofunctional form (Berlyn and Giles, 1969;Chaudhuri et al, 1987), a bifunctional form found in plants and a multifunctional form of dehydroquinase, which is a large polypeptide (Kleanthous et al, 1990). Kim et al (2006) reported the presence in Mycobacterium tuberculosis of such enzymes which are essential for the biosynthesis of phenylalanine, tyrosine, tryptophan (Garbe et al, 1991), and other aromatic compounds in bacteria and other organisms such as fungi, algae and plants, but they are absent in mammals (Haslam, 1993;Kim et al, 2006). An advantage of the non-occurrence of these enzymes in mammals is the possibility of the development of new drugs (Cole et al, 1998;Camus et al, 2002;Kim et al, 2006).…”

Section: Arob and Aroq: Amino Acid Biosynthesismentioning

confidence: 99%

A description of genes of Corynebacterium pseudotuberculosis useful in diagnostics and vaccine applications

D’Afonseca

Moraes²,

Dorella³

et al. 2008

Genet. Mol. Res.

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ABSTRACT. Corynebacterium pseudotuberculosis, a Gram-positive intracellular pathogen, is the etiological agent of caseous lymphadenitis or CLA. This bacterium infects goats and sheep and causes great economic losses worldwide annually, mainly for goat producers. Despite its importance, CLA is still poorly characterized. However, with advances in the genomic field, many C. pseudotuberculosis genes have already been characterized, mainly those related to virulence such as phospholipase D. Here, we examined the use of the several available genes of C. pseudotuberculosis and reviewed their applications in vaccine construction, more efficient diagnostics for CLA, and control of this disease, among other applications.

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“…We show in the present study that these are both monofunctional CMs of the AroQ class. It should be pointed out that Rv1885c has been recently characterized in detail by others (27,41,45). We also show that homologues of each CM from M. tuberculosis are found in Mycobacterium smegmatis, a nonpathogenic species.…”

Section: Tuberculosis (Tb) a Serious Infectious Disease Caused Bymentioning

confidence: 76%

The Two Chorismate Mutases from both Mycobacterium tuberculosis and Mycobacterium smegmatis : Biochemical Analysis and Limited Regulation of Promoter Activity by Aromatic Amino Acids

et al. 2008

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Chorismate mutase (CM) catalyzes the rearrangement of chorismate to prephenate in the biosynthetic pathway that forms phenylalanine and tyrosine in bacteria, fungi, plants, and apicomplexan parasites. 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. Until recently, two putative open reading frames (ORFs), Rv0948c and Rv1885c, showing low sequence similarity to CMs have been described as "conserved hypothetical proteins" in the M. tuberculosis genome. However, we and others demonstrated that these ORFs are in fact monofunctional CMs of the AroQ structural class and that they are differentially localized in the mycobacterial cell. Since homologues to the M. tuberculosis enzymes are also present in Mycobacterium smegmatis, we cloned the coding sequences corresponding to ORFs MSMEG5513 and MSMEG2114 from the latter. The CM activities of both ORFs was determined, as well as their translational start sites. In addition, we analyzed the promoter activities of three M. tuberculosis loci related to phenylalanine and tyrosine biosynthesis under a variety of conditions using M. smegmatis as a surrogate host. Our results indicate that the aroQ (Rv0948c), *aroQ (Rv1885c), and fbpB (Rv1886c) genes from M. tuberculosis are constitutively expressed or subjected to minor regulation by aromatic amino acids levels, especially tryptophan. Tuberculosis (TB), a serious infectious disease caused byMycobacterium tuberculosis, still remains a public health problem in the world. It has been estimated that one-third of the world's population is latently infected with M. tuberculosis and that almost 9 million new cases and 2 million deaths occur each year (19). The low efficacy of the currently available TB vaccine (Mycobacterium bovis BCG), the emergence of multidrug-resistant strains of M. tuberculosis, and the global spread of human immunodeficiency virus (which increases the risk of TB development) are among the factors underlying the resurgence of TB (24). New drugs and second-generation vaccines are urgently required to control TB, but the complex biology of M. tuberculosis has hindered the development of novel therapeutic tools.M. tuberculosis is a sophisticated intracellular pathogen that can persist for months or years within the human host, and different mechanisms related to its entry, survival, and replication in macrophages are involved in the infection process (51, 56). The bacilli are notably able to interfere with normal macrophage functions, such as antigen presentation and phagosome maturation, residing in a specialized, nonacidified compartment (44). Of particular interest is the fact that important nutrients are restricted or unavailable inside macrophages, so that M. tuberculosis cells are probably subjected to long-term starvation during the early and latent stages of infection (6,36,50). Since many anabolic and catabolic pathways should be specifical...

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Biochemical and Structural Characterization of the Secreted Chorismate Mutase (Rv1885c) from Mycobacterium tuberculosis H ₃₇ R _v : an *AroQ Enzyme Not Regulated by the Aromatic Amino Acids

Cited by 47 publications

References 57 publications

Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum

Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum

A description of genes of Corynebacterium pseudotuberculosis useful in diagnostics and vaccine applications

The Two Chorismate Mutases from both Mycobacterium tuberculosis and Mycobacterium smegmatis : Biochemical Analysis and Limited Regulation of Promoter Activity by Aromatic Amino Acids

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Biochemical and Structural Characterization of the Secreted Chorismate Mutase (Rv1885c) from Mycobacterium tuberculosis H 37 R v : an *AroQ Enzyme Not Regulated by the Aromatic Amino Acids

Cited by 47 publications

References 57 publications

Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum

Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum

A description of genes of Corynebacterium pseudotuberculosis useful in diagnostics and vaccine applications

The Two Chorismate Mutases from both Mycobacterium tuberculosis and Mycobacterium smegmatis : Biochemical Analysis and Limited Regulation of Promoter Activity by Aromatic Amino Acids

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Product

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Biochemical and Structural Characterization of the Secreted Chorismate Mutase (Rv1885c) from Mycobacterium tuberculosis H ₃₇ R _v : an *AroQ Enzyme Not Regulated by the Aromatic Amino Acids