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 | - |
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 | 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 | - |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | Rv0948c, the presence of a cleavable signal peptide in Rv1885c strongly suggests that they are exported | - |
- |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
11700 | - |
the recombinant protein AroQMs in Escherichia coli | Mycolicibacterium smegmatis |
17800 | - |
in Escherichia coli for the mature *AroQMs protein | Mycolicibacterium smegmatis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Chorismate | Mycolicibacterium smegmatis | - |
Prephenate | - |
? | |
Chorismate | - |
- |
Prephenate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
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 | - |
Mycolicibacterium smegmatis | A0QU81 | nonpathogenic species, Analysis of promoter activity described | - |
no activity in Corynebacterium diphtheriae | - |
- |
- |
no activity in Mycobacterium leprae | - |
- |
- |
no activity in Nocardia farcinica | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Mycolicibacterium smegmatis |
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 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Chorismate | - |
Mycolicibacterium smegmatis | Prephenate | - |
? | |
Chorismate | - |
- |
Prephenate | - |
? | |
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 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
chorismate mutase | - |
Mycolicibacterium smegmatis |
chorismate mutase | - |
- |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mycolicibacterium smegmatis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Mycolicibacterium smegmatis |