5.4.99.5: chorismate mutase
This is an abbreviated version!
For detailed information about chorismate mutase, go to the full flat file.
Word Map on EC 5.4.99.5
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5.4.99.5
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shikimate
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sieve
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monofunctional
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phloem
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l-phenylalanine
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l-tyrosine
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7-phosphate
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mutases
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t-proteins
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3-deoxy-d-arabino-heptulosonate
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phenylpyruvate
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claisen
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arogenate
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pericyclic
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nonketotic
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hyperglycinemia
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isochorismate
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cyclohexadienyl
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hydroxyphenylpyruvate
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photorespiratory
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preorganization
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drug development
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3-deoxy-d-arabino-heptulosonate-7-phosphate
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meloidogyne
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synthesis
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agriculture
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analysis
- 5.4.99.5
- shikimate
-
sieve
-
monofunctional
- phloem
- l-phenylalanine
- l-tyrosine
- 7-phosphate
- mutases
-
t-proteins
-
3-deoxy-d-arabino-heptulosonate
- phenylpyruvate
-
claisen
- arogenate
-
pericyclic
-
nonketotic
- hyperglycinemia
- isochorismate
-
cyclohexadienyl
- hydroxyphenylpyruvate
-
photorespiratory
-
preorganization
- drug development
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3-deoxy-d-arabino-heptulosonate-7-phosphate
- meloidogyne
- synthesis
- agriculture
- analysis
Reaction
Synonyms
105-MtCM, 90-MtCM, AmtCM1, AmtCM2, aro7, AroA, AroH, AroQ, AtCM1, AtCM2, AtCM3, Bacillus subtilis chorismate mutase, Bphy_7813, BsAroH, BsCM, BsCM_2, BTH_I1596, chorismate mutase, chorismate mutase 1, chorismate mutase-prephenate dehydrogenase, Chorismate mutase/prephenate dehydratase, CM, CM type 2, CM-1, CM-prephenate dehydratase, CM-TyrAp, CM/PDT, CM/PDT/PDHG, CM0819, CM1, CM2, EcCM, EcCM-R, MI-CM-1, MI-CM-2, MjCM, MTB chorismate mutase, MTB CM, MtbCM, MtCM, Mutase, chorismate, Mycobacterium tuberculosis chorismate mutase, Mycobacterium tuberculosis H37Rv chorismate mutase, NC30, P protein, P-protein, PheA, PpCM1, PpCM2, Rv0948c, Rv1885c, SmCM, Tparo7, TtCM, y2828, YCM
ECTree
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Application on EC 5.4.99.5 - chorismate mutase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
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the widespread presence of chorismate mutases in the specialized sedentary endoparasitic nematode species suggests that this multifunctional enzyme may be a key factor in modulating plant parasitism
analysis
As an intramolecular reaction that appears to be catalyzed without intermediate steps, covalent catalysis, or modification of the reaction pathway, the chorismate-prephenate rearrangement has become an important model system for theoretical approaches to the study of enzyme catalysis
drug development
synthesis
synthesis of L-phenylalanine (an important amino acid that is widely used in the production of food flavors and pharmaceuticals) by engineered Escherichia coli. Coexpression of Vitreoscilla hemoglobin gene, driven by a tac promoter, with the genes encoding 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (aroF) and feedback-resistant chorismate mutase/prephenate dehydratase (pheAfbr), leads to increased productivity of L-phenylalanine and decreased demand for aeration by Escherichia coli CICC10245
drug development
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the enzyme serves as a potential target for the development of inhibitors specific to the pathogen
drug development
advantage of the nonoccurance of CMs in human, develop antimicrobial drugs to combat dreaded human pathogens such as Mycobacterium tuberculosis
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
drug development
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MtCM might play a role in host-pathogen interactions, making it an important target for designing inhibitor molecules against the deadly pathogen
drug development
multiple-drug-resistant tuberculoses bacillus and its synergism with HIV-characterization of new enzyme targets and the development of new drugs
drug development
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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
drug development
since vertebrates lack the shikimate pathway for the biosynthesis of aromatic compounds and thus do not possess chorismate mutase activity, the enzyme represents a prime target for the development of antibacterials
drug development
the secretory isozyme is a target for the discovery of anti-tubercular agents
drug development
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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the secretory isozyme is a target for the discovery of anti-tubercular agents
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drug development
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multiple-drug-resistant tuberculoses bacillus and its synergism with HIV-characterization of new enzyme targets and the development of new drugs
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drug development
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advantage of the nonoccurance of CMs in human, develop antimicrobial drugs to combat dreaded human pathogens such as Mycobacterium tuberculosis
-
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
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