Chorismate Mutase
Chorismic Acid
Prephenate Dehydratase
Prephenate Dehydrogenase
Methylmalonyl-CoA Mutase
Phosphoglycerate Mutase
Shikimic Acid
3-Deoxy-7-Phosphoheptulonate Synthase
Bisphosphoglycerate Mutase
Cyclohexenes
Phosphorus-Oxygen Lyases
Phenylalanine
Hydro-Lyases
Phenylpyruvic Acids
Isomerases
Allosteric Regulation
Aldehyde-Lyases
Intramolecular Transferases
Brevibacterium
Tryptophan
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
Tyrosine
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
ortho-Aminobenzoates
Transaminases
Catalysis
Periplasm
Phosphotransferases
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Amino Acid Sequence
Anthranilate Synthase
Oxidoreductases
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Models, Molecular
Lyases
Cloning, Molecular
Feedback
Encyclopedias as Topic
Hydrogen Bonding
Chromatography, Affinity
Protein Structure, Secondary
Circular Dichroism
Genetic Code
Probing enzyme quaternary structure by combinatorial mutagenesis and selection. (1/112)
Genetic selection provides an effective way to obtain active catalysts from a diverse population of protein variants. We have used this tool to investigate the role of loop sequences in determining the quaternary structure of a domain-swapped enzyme. By inserting random loops of four to seven residues into a dimeric chorismate mutase and selecting for functional variants by genetic complementation, we have obtained and characterized both monomeric and hexameric enzymes that retain considerable catalytic activity. The low percentage of active proteins recovered from these selection experiments indicates that relatively few loop sequences permit a change in quaternary structure without affecting active site structure. The results of our experiments suggest further that protein stability can be an important driving force in the evolution of oligomeric proteins. (+info)Bacillus subtilis chorismate mutase is partially diffusion-controlled. (2/112)
The effect of viscosogens on the enzyme-catalyzed rearrangement of chorismate to prephenate has been studied. The steady-state parameters kcat and kcat/Km for the monofunctional chorismate mutase from Bacillus subtilis (BsCM) decreased significantly with increasing concentrations of glycerol, whereas the 'sluggish' BsCM mutants C75A and C75S were insensitive to changes in microviscosity. The latter results rule out extraneous interactions of the viscosogen as an explanation for the effects observed with the wild-type enzyme. Additional control experiments show that neither viscosogen-induced shifts in the pH-dependence of the enzyme-catalyzed reaction nor small perturbations of the conformational equilibrium of chorismate can account for the observed effects. Instead, BsCM appears to be limited by substrate binding and product release at low and high substrate concentrations, respectively. Analysis of the kinetic data indicates that diffusive transition states are between 30 and 40% rate-determining in these concentration regimes; the chemical step must contribute to the remaining kinetic barrier. The relatively low value of the 'on' rates for chorismate and prephenate (approximately 2 x 106 m-1.s-1) probably reflects the need for a rare conformation of the enzyme, the ligand, or both for successful binding. Interestingly, the chorismate mutase domain of the bifunctional chorismate mutase-prephenate dehydratase from Escherichia coli, which has steady-state kinetic parameters comparable to those of BsCM but has a much less accessible active site, is insensitive to changes in viscosity and the reaction it catalyses is not diffusion-controlled. (+info)Cloning and characterization of an esophageal-gland-specific chorismate mutase from the phytoparasitic nematode Meloidogyne javanica. (3/112)
Root-knot nematodes are obligate plant parasites that alter plant cell growth and development by inducing the formation of giant feeder cells. It is thought that nematodes inject secretions from their esophageal glands into plant cells while feeding, and that these secretions cause giant cell formation. To elucidate the mechanisms underlying the formation of giant cells, a strategy was developed to clone esophageal gland genes from the root-knot nematode Meloidogyne javanica. One clone, shown to be expressed in the nematode's esophageal gland, codes for a potentially secreted chorismate mutase (CM). CM is a key branch-point regulatory enzyme in the shikimate pathway and converts chorismate to prephenate, a precursor of phenylalanine and tyrosine. The shikimate pathway is not found in animals, but in plants, where it produces aromatic amino acids and derivative compounds that play critical roles in growth and defense. Therefore, we hypothesize that this CM is involved in allowing nematodes to parasitize plants. (+info)The aroC gene of Aspergillus nidulans codes for a monofunctional, allosterically regulated chorismate mutase. (4/112)
The cDNA and the chromosomal locus of the aroC gene of Aspergillus nidulans were cloned and is the first representative of a filamentous fungal gene encoding chorismate mutase (EC 5.4.99.5), the enzyme at the first branch point of aromatic amino acid biosynthesis. The aroC gene complements the Saccharomyces cerevisiae aro7Delta as well as the A. nidulans aroC mutation. The gene consists of three exons interrupted by two short intron sequences. The expressed mRNA is 0.96 kilobases in length and aroC expression is not regulated on the transcriptional level under amino acid starvation conditions. aroC encodes a monofunctional polypeptide of 268 amino acids. Purification of this 30-kDa enzyme allowed determination of its kinetic parameters (k(cat) = 82 s(-1), n(H) = 1. 56, [S](0.5) = 2.3 mM), varying pH dependence of catalytic activity in different regulatory states, and an acidic pI value of 4.7. Tryptophan acts as heterotropic activator and tyrosine as negative acting, heterotropic feedback-inhibitor with a K(i) of 2.8 microM. Immunological data, homology modeling, as well as electron microscopy studies, indicate that this chorismate mutase has a dimeric structure like the S. cerevisiae enzyme. Site-directed mutagenesis of a crucial residue in loop220s (Asp(233)) revealed differences concerning the intramolecular signal transduction for allosteric regulation of enzymatic activity. (+info)Prephenate dehydratase from the aphid endosymbiont (Buchnera) displays changes in the regulatory domain that suggest its desensitization to inhibition by phenylalanine. (5/112)
Buchnera aphidicola, the prokaryotic endosymbiont of aphids, complements dietary deficiencies with the synthesis and provision of several essential amino acids. We have cloned and sequenced a region of the genome of B. aphidicola isolated from Acyrthosiphon pisum which includes the two-domain aroQ/pheA gene. This gene encodes the bifunctional chorismate mutase-prephenate dehydratase protein, which plays a central role in L-phenylalanine biosynthesis. Two changes involved in the overproduction of this amino acid have been detected. First, the absence of an attenuator region suggests a constitutive expression of this gene. Second, the regulatory domain of the Buchnera prephenate dehydratase shows changes in the ESRP sequence, which is involved in the allosteric binding of phenylalanine and is strongly conserved in prephenate dehydratase proteins from practically all known organisms. These changes suggest the desensitization of the enzyme to inhibition by phenylalanine and would permit the bacterial endosymbiont to overproduce phenylalanine. (+info)HARO7 encodes chorismate mutase of the methylotrophic yeast Hansenula polymorpha and is derepressed upon methanol utilization. (6/112)
The HARO7 gene of the methylotrophic, thermotolerant yeast Hansenula polymorpha was cloned by functional complementation. HARO7 encodes a monofunctional 280-amino-acid protein with chorismate mutase (EC 5.4. 99.5) activity that catalyzes the conversion of chorismate to prephenate, a key step in the biosynthesis of aromatic amino acids. The HARO7 gene product shows strong similarities to primary sequences of known eukaryotic chorismate mutase enzymes. After homologous overexpression and purification of the 32-kDa protein, its kinetic parameters (k(cat) = 319.1 s(-1), n(H) = 1.56, [S](0.5) = 16.7 mM) as well as its allosteric regulatory properties were determined. Tryptophan acts as heterotropic positive effector; tyrosine is a negative-acting, heterotropic feedback inhibitor of enzyme activity. The influence of temperature on catalytic turnover and the thermal stability of the enzyme were determined and compared to features of the chorismate mutase enzyme of Saccharomyces cerevisiae. Using the Cre-loxP recombination system, we constructed mutant strains carrying a disrupted HARO7 gene that showed tyrosine auxotrophy and severe growth defects. The amount of the 0.9-kb HARO7 mRNA is independent of amino acid starvation conditions but increases twofold in the presence of methanol as the sole carbon source, implying a catabolite repression system acting on HARO7 expression. (+info)A strategically positioned cation is crucial for efficient catalysis by chorismate mutase. (7/112)
Combinatorial mutagenesis and in vivo selection experiments previously afforded functional variants of the AroH class Bacillus subtilis chorismate mutase lacking the otherwise highly conserved active site residue Arg(90). Here, we present a detailed kinetic and crystallographic study of several such variants. Removing the arginine side chain (R90G and R90A) reduced catalytic efficiency by more than 5 orders of magnitude. Reintroducing a positive charge to the active site through lysine substitutions restored more than a factor of a thousand in k(cat). Remarkably, the lysine could be placed at position 90 or at the more remote position 88 provided a sterically suitable residue was present at the partner site. Crystal structures of the double mutants C88S/R90K and C88K/R90S show that the lysine adopts an extended conformation that would place its epsilon-ammonium group within hydrogen-bonding distance of the ether oxygen of bound chorismate in the transition state. These results provide support for the hypothesis that developing negative charge in the highly polarized transition state is stabilized electrostatically by a strategically placed cation. The implications of this finding for the mechanism of all natural chorismate mutases and for the design of artificial catalysts are discussed. (+info)Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism. (8/112)
Chorismate mutase acts at the first branch-point of aromatic amino acid biosynthesis and catalyzes the conversion of chorismate to prephenate. The results of molecular dynamics simulations of the substrate in solution and in the active site of chorismate mutase are reported. Two nonreactive conformers of chorismate are found to be more stable than the reactive pseudodiaxial chair conformer in solution. It is shown by QM/MM molecular dynamics simulations, which take into account the motions of the enzyme, that when these inactive conformers are bound to the active site, they are rapidly converted to the reactive chair conformer. This result suggests that one contribution of the enzyme is to bind the more prevalent nonreactive conformers and transform them into the active form in a step before the chemical reaction. The motion of the reactive chair conformer in the active site calculated by using the QM/MM potential generates transient structures that are closer to the transition state than is the stable CHAIR conformer. (+info)
The emerging periplasm-localized subclass of AroQ chorismate mutases, by David H. Calhoun, Carol A. Bonner et al.
Chorismate mutase - Wikipedia
RCSB PDB
- 1COM: THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE...
AID 52148 - The compound was tested for inhibition of Bacillus subtilis chorismate mutase (BcCM) - PubChem
Molecular Determinants for Rate Acceleration in the Claisen Rearrangement Reaction - edoc
Chorismate to PHB in Yeast?
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Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and...
Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase. | Journal of Bacteriology
Replacement of two invariant serine residues in chorismate synthase provides evidence that a proton relay system is essential...
Combinatorial mutagenesis and pseudorevertant analysis to charact...: Ingenta Connect
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DAHP synthase - Wikipedia
Tryptophan Biosynthesis (Saccharomyces cerevisiae) - WikiPathways
Pericyclic Analogies
Analysis of a trimeric complex involving chorismate synthase from Bacillus subtilis<...
Structural and functional aspects of pyranose-furanose mutases
Computational Organic Chemistry » Computational Organic Chemistry, Second Edition - whats new in Chapters 5-9
RCSB PDB - 6U60: Crystal structure of prephenate dehydrogenase tyrA from Bacillus anthracis in complex with NAD and L-tyrosine
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CATH Superfamily 3.30.70.260
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Prephenate dehydratase
Schmidt JC; Zalkin H (1969). "Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from ...
Prephenic acid
C10H10O6 Helmut Goerisch (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700-3705. doi: ... It is biosynthesized by a [3,3]-sigmatropic Claisen rearrangement of chorismate. Prephenic acid is an example of achiral ( ... "Thermodynamics of the Conversion of Chorismate to Prephenate: Experimental Results and Theoretical Predictions". J. Phys. Chem ...
Prephenate dehydrogenase
"InterPro." Bifunctional Chorismate Mutase/prephenate Dehydrogenase T-protein (IPR008244). InterPro, n.d. Web. 24 Apr. 2014. ... prephenate dehydrogenase is fused with the enzyme chorismate mutase. This fusion is not found in plants or animals. As of late ... and chorismate mutase---prephenate dehydrogenase. This enzyme participates in phenylalanine, tyrosine and tryptophan ...
Shikimate pathway
Prephenic acid is then synthesized by a Claisen rearrangement of chorismate by chorismate mutase. Prephenate is oxidatively ... Helmut Goerisch (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700. doi:10.1021/ ... Then 5-enolpyruvylshikimate-3-phosphate is transformed into chorismate by a chorismate synthase. ... The pathway starts with two substrates, phosphoenol pyruvate and erythrose-4-phosphate, and ends with chorismate, a substrate ...
Shikimic acid
Prephenic acid is then synthesized by a Claisen rearrangement of chorismate by chorismate mutase. Prephenate is oxidatively ... Goerisch, H. (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700-3705. doi:10.1021/ ... Then 5-enolpyruvylshikimate-3-phosphate is transformed into chorismate by a chorismate synthase. ... "Shikimate and chorismate biosynthesis". Department of Chemistry, Queen Mary University of London.. ...
Enzyme kinetics
Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3 ... Such cases exist: for example a mutase such as phosphoglucomutase catalyses the transfer of a phospho group from one position ... Enzymes with single-substrate mechanisms include isomerases such as triosephosphateisomerase or bisphosphoglycerate mutase, ...
William Lipscomb
Chorismate mutase (right) catalyzes (speeds up) the production of the amino acids phenylalanine and tyrosine. Fructose-1,6- ... "Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures". Structure. 5 (11): 1437- ...
Aspartate carbamoyltransferase
Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3 ...
Hydrogen-bond catalysis
For instance, the natural enzyme chorismate mutase, which catalyzes the Claisen rearrangement of chorismate, features many ... "New insight into the catalytic mechanism of chorismate mutases from structural studies". Chemistry & Biology. 2 (4): 195-203. ...
Amino acid synthesis
This process is mediated by a phenylalanine (PheA) or tyrosine (TyrA) specific chorismate mutase-prephenate dehydrogenase. PheA ... trpE encodes the first subunit, which binds to chorismate and moves the amino group from the donor to chorismate. trpG encodes ... The rest of the enzymes in the common pathway (conversion of DAHP to chorismate) appear to be synthesized constitutively, ... Phenylalanine, tyrosine, and tryptophan, the aromatic amino acids, arise from chorismate. The first step, condensation of 3- ...
Isochorismate lyase
... is a structural homolog of the chorismate mutase enzyme in E. coli, and actually exhibits non-physiological ... Using the chorismate produced from that metabolic process, first the enzyme PchA will catalyze the reaction of chorismate into ... a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities". The Journal of ... chorismate mutase activity, albeit at a much lower efficiency. IPL also has several homologs found in other organisms, ...
Arogenate dehydratase
ADTs contain an N-terminal transit peptide, a PDT-like domain, and an ACT (Aspartokinase, chorismate mutase, TyrA) domain. ...
ACT domain
The ACT domain is named after three of the proteins that contain it: aspartate kinase, chorismate mutase and TyrA. The ...
Cyanidin
In the synthesis of L-phenylalanine, chorismate undergoes a Claisen rearrangement by a Chorismate mutase enzyme to form ...
Pravindra Kumar
"Structure of Chorismate Mutase-like Domain of DAHPS from Bacillus subtilis Complexed with Novel Inhibitor Reveals ... reported to have opportunities in the development of a new class of antibiotics as the compound clings to the chorismate mutase ...
Synthetic biology
One project demonstrated that an engineered version of Chorismate mutase still had catalytic activity when only 9 amino acids ...
Hydroxyphenylpyruvate synthase
... may refer to: Prephenate dehydrogenase, an enzyme Chorismate mutase, an enzyme This set index ...
Claisen rearrangement
The enzyme chorismate mutase (EC 5.4.99.5) catalyzes the Claisen rearrangement of chorismate to prephenate, a key intermediate ...
JS Chiao
... pathway of aromatic amino acids in Nocardia mediterranei 1994 Cloning vector system for Nocardia spp 1995 Chorismate mutase and ...
Hirschmanniella oryzae
... chorismate mutase and isochorismatase, thought to be interfering on the salicylic acid pathway and thereby altering the defense ...
List of MeSH codes (D08)
2-acetolactate mutase MeSH D08.811.399.520.250 - chorismate mutase MeSH D08.811.399.520.250.500 - prephenate dehydratase MeSH ... phosphoglycerate mutase MeSH D08.811.399.894.200 - amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 - phosphoglucomutase MeSH D08.811.399.520.750.700 - ... D08.811.399.520.250.750 - prephenate dehydrogenase MeSH D08.811.399.520.625 - methylmalonyl-coa mutase MeSH D08.811.399.520.750 ...
Chorismate mutase
... is found at a branch point in the pathway. The enzyme channels the substrate, chorismate to the biosynthesis ... For example, the secondary structure of the chorismate mutase of yeast is very similar to that of E. coli. Chorimate mutase in ... The systematic name of this enzyme class is chorismate pyruvatemutase. Chorismate mutase, also known as hydroxyphenylpyruvate ... chorismate mutase (EC 5.4.99.5) is an enzyme that catalyzes the chemical reaction for the conversion of chorismate to ...
ಕಿಣ್ವ ಚಲನಶಾಸ್ತ್ರ - ವಿಕಿಪೀಡಿಯ
Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiol. Mol. Biol. Rev. 65 (3): 404-21, table ...
List of EC numbers (EC 5)
2-acetolactate mutase EC 5.4.99.4: 2-methyleneglutarate mutase EC 5.4.99.5: chorismate mutase EC 5.4.99.6: now EC 5.4.4.2 EC ... phosphoglucosamine mutase EC 5.4.2.11: phosphoglycerate mutase EC 5.4.2.12: phosphoglycerate mutase EC 5.4.3.1: deleted EC 5.4. ... benzene mutase EC 5.4.4.2: isochorismate synthase EC 5.4.4.3: 3-(hydroxyamino)phenol mutase EC 5.4.4.4: geraniol isomerase EC ... isobutyryl-CoA mutase EC 5.4.99.14: 4-carboxymethyl-4-methylbutenolide mutase EC 5.4.99.15: (1→4)-a-D-glucan 1-a-D- ...
Isochorismate synthase
Other names for this enzyme include: Isochorismate mutase Menaquinone-specific isochorismate synthase MenF MenF is a gene that ... More specifically it is classified as an intramolecular transferase because it transfers the hydroxy group of chorismate ... Isochorismate synthase catalyzes the irreversible conversion of chorismate to isochorismate: Isochorismate synthase is most ... 5-dihydrochorismate analogues as inhibitors of the chorismate-utilising enzymes". Organic & Biomolecular Chemistry. 7 (11): ...
Shikimic acid
Prephenic acid is then synthesized by a Claisen rearrangement of chorismate by Chorismate mutase.[6][7] ... Helmut Goerisch (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700. doi:10.1021/ ... Then 5-enolpyruvylshikimate-3-phosphate is transformed into chorismate by a chorismate synthase. ... The pathway starts with two substrates, phosphoenol pyruvate and erythrose-4-phosphate and ends with chorismate, a substrate ...
Chorismate mutase - Wikipedia
For example, the secondary structure of the chorismate mutase of yeast is very similar to that of E. coli. Chorimate mutase in ... Chorismate mutase is found at a branch point in the pathway. The enzyme channels the substrate, chorismate to the biosynthesis ... The systematic name of this enzyme class is chorismate pyruvatemutase. Chorismate mutase, also known as hydroxyphenylpyruvate ... chorismate mutase (EC 5.4.99.5) is an enzyme that catalyzes the chemical reaction for the conversion of chorismate to ...
pheA - Bifunctional chorismate mutase/prephenate dehydratase - Escherichia coli O157:H7 - pheA gene & protein
Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to ... IPR008242 Chor_mutase/pphenate_deHydtase. IPR036263 Chorismate_II_sf. IPR036979 CM_dom_sf. IPR002701 CM_II_prokaryot. IPR010952 ... IPR008242 Chor_mutase/pphenate_deHydtase. IPR036263 Chorismate_II_sf. IPR036979 CM_dom_sf. IPR002701 CM_II_prokaryot. IPR010952 ... Chorismate mutasePROSITE-ProRule annotation. ,p>Manual validated information which has been generated by the UniProtKB ...
ARO7 - Chorismate mutase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - ARO7 gene & protein
chorismate mutase activity, aromatic amino acid family biosynthetic process, L-phenylalanine biosynthetic process, tyrosine ... IPR036263 Chorismate_II_sf. IPR008238 Chorismate_mutase_AroQ_euk. IPR037039 CM_AroQ_sf_eucaryotic. ... IPR036263 Chorismate_II_sf. IPR008238 Chorismate_mutase_AroQ_euk. IPR037039 CM_AroQ_sf_eucaryotic. ... chorismate mutase activity Source: SGD ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the function, ...
A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditions | PNAS
Purified Glu198Gly chorismate mutase exhibits a dramatic drop in in vitro chorismate mutase activity. Measurement of chorismate ... bacterial chorismate mutases as e.g., chorismate mutase-prephenate dehydratase of Escherichia coli (P protein) and chorismate ... Chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5) catalyzes the isomerization of chorismate to prephenate within the ... Dependency of activity for Asn194Asp chorismate mutase on pH is similar to that observed for wild-type chorismate mutase under ...
RCSB PDB - 2CHT: CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A...
CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ... We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5), the 1.9-A crystal structure of ... We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5), the 1.9-A crystal structure of ... The B. subtilis chorismate mutase is a homotrimer, with beta-sheets from each monomer packing to form the core of a pseudo- ...
Sequence Similarity
- 1COM: THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF...
Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications ... THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES ... CHORISMATE MUTASE protein, length: 127 (BLAST) Sequence Similarity Cutoff. Rank. Chains in Cluster. Cluster ID / Name. ... The monofunctional chorismate mutase from Bacillus subtilis. ...
Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation...
AID 52148 - The compound was tested for inhibition of Bacillus subtilis chorismate mutase (BcCM) - PubChem
Two components of chorismate mutase in Brevibacterium flavum. - Semantic Scholar
In accord with this suggestion, chorismate mutase as well as DAHP synthetase was insensitive to feedback inhibition by ... All the phenylalanine and tyrosine double auxotrophs defective in chorismate mutase lacked component B but not A. ... DEAE-cellulose or hydroxyapatite column chromatography as well as the disc-gel electrophoretic pattern of chorismate mutase ... In the presence of the reaction substrate, chorismate, the two components associated reversibly to give an active enzyme ...
Subcellular localization of chorismate-mutase isoenzymes in protoplasts from mesophyll and suspension-cultured cells of...
The subcellular locations of two readily discriminated chorismate-mutase (EC 5.4.99.5) isoenzymes from Nicotiana silvestris ... Subcellular localization of chorismate-mutase isoenzymes in protoplasts from mesophyll and suspension-cultured cells of ... Isoenzyme CM-1 is sensitive to feedback inhibition by L-tyrosine and comprises the major fraction of total chorismate mutase in ... The subcellular locations of two readily discriminated chorismate-mutase (EC 5.4.99.5) isoenzymes from Nicotiana silvestris ...
Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and...
Several derivatives of phenylalanine and tyrosine were prepared and tested for inhibition of chorismate mutase-prephenate ... Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and ... Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and ... Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and ...
Genetic consequences of artificial selection on amino acid synthesis: Cysteine synthase and chorismate mutase
The chorismate mutase gene in maize shows strong evidence of selection, with high diversity in teosinte accessions and ... Genetic consequences of artificial selection on amino acid synthesis: Cysteine synthase and chorismate mutase. Davis, Tatum V. ... cysteine synthase and chorismate mutase. One approach to define the importance of a gene is to isolate a mutation and examine ... three segments of the chorismate mutase gene were sequenced in a panel of 14 landraces, the historical intermediate between ...
Structural and functional investigation of a secreted chorismate mutase from the plant-parasitic nematode Heterodera schachtii...
In this article, we present the cloning of Hscm1, a gene for chorismate mutase (CM) from the beet cyst nematode Heterodera ... article{593044, abstract = {In this article, we present the cloning of Hscm1, a gene for chorismate mutase (CM) from the beet ... Structural and functional investigation of a secreted chorismate mutase from the plant-parasitic nematode Heterodera schachtii ... "Structural and Functional Investigation of a Secreted Chorismate Mutase from the Plant-parasitic Nematode Heterodera Schachtii ...
Characterization of a chorismate mutase from the potato cyst nematode Globodera pallida. - Semantic Scholar
A potentially secreted chorismate mutase has been isolated from the potato cyst nematode Globodera pallida. The gene encoding ... The presence of a signal peptide in the deduced amino acid sequence of the G. pallida chorismate mutase and its expression in ... The shikimate pathway, of which chorismate mutase is normally a part, is not found in animals but is present in plants and ... The potential roles of a nematode chorismate mutase are discussed. ...
Mechanistic studies of a chorismate mutase from Bacillus subtilis - Research Collection
A novel noncovalent complex of chorismate mutase and DAHP synthase from Mycobacterium tuberculosis - Research Collection
Searching sequence space for protein catalysts | PNAS
chorismate mutase;. MjCM′,. reengineered CM from Methanococcus jannaschii;. EcCM,. Escherichia coli CM;. WT,. wild type.. ... Specifically, we have constructed large binary-patterned libraries based on the AroQ-class chorismate mutase (CM) from ... helical bundle chorismate mutase with simple binary-patterned modules based on a limited set of four polar and four nonpolar ... Because the chorismate rearrangement is essential for the biosynthesis of tyrosine (Tyr) and phenylalanine (Phe) in bacteria, ...
Integrated metabolome and transcriptome analysis of Magnolia champaca identifies biosynthetic pathways for floral volatile...
Identification and Characterization of Microsatellites in Expressed Sequence Tags and Their Cross Transferability in Different...
ACT domain (IPR002912) | InterPro | EMBL-EBI
Shikimic acid - Wikipedia
Prephenic acid is then synthesized by a Claisen rearrangement of chorismate by Chorismate mutase.[6][7] ... Helmut Goerisch (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700. doi:10.1021/ ... Then 5-enolpyruvylshikimate-3-phosphate is transformed into chorismate by a chorismate synthase. ... The pathway starts with two substrates, phosphoenol pyruvate and erythrose-4-phosphate and ends with chorismate, a substrate ...
NAVER Academic | Effect of cold storage on proteinase and chorismate mutase activities inSolanum tuberosum L. Genotypes...
Protein extracts from each cultivar were assayed for proteinase and chorismate mutase (CM) activities. During cold storage, ... Effect of cold storage on proteinase and chorismate mutase activities inSolanum tuberosum L. Genotypes differing in blackspot ... Protein extracts from each cultivar were assayed for proteinase and chorismate mutase (CM) activities. During cold storage, ...
IUCr) Wheat germ cell-free expression system as a pathway to improve protein yield and solubility for the SSGCID pipeline
talks.cam : Electronic Structure Discussion Group
New/Updated Arabidopsis DNA 20-May-2000
The Effects of Artificial Selection on the Maize Genome | Science
Frontiers | An Enzymatically Hydrolyzed Animal Protein-Based Biostimulant (Pepton) Increases Salicylic Acid and Promotes Growth...
... with an emphasis on its possible role on chorismate-derived hormones (auxin, salicylic acid, and melatonin). Tomato plants ... with an emphasis on its possible role on chorismate-derived hormones (auxin, salicylic acid and melatonin). Tomato plants ... Phe, phenylalanine; PAL, phenylalanine ammonia lyase; ICS, isochorismate synthase; CM, chorismate mutase. ... Chorismate-Derived Hormones. Chorismate-derived hormones, including salicylic acid, auxin, and melatonin were determined by ...
Frontiers | Biosynthesis and Metabolic Fate of Phenylalanine in Conifers | Plant Science
PEP, phosphoenolpyruvate; E4P, erythrose 4-phosphate; CM, chorismate mutase; AS, anthranilate synthase. ... Chorismate may be used by the enzyme anthranilate synthase in the synthesis of Trp or converted to prephenate, which is the ... of aromatic amino acids are channeled from photosynthesis through the shikimate pathway toward the biosynthesis of chorismate, ...
"The emerging periplasm-localized subclass of AroQ chorismate mutases, " by David H. Calhoun, Carol A. Bonner et al.
The periplasmic chorismate mutases (denoted *AroQ) are shown to be a distinct subclass of AroQ, being about twice the size of ... aeruginosa comprises a complete chorismate-to-phenylalanine pathway and accounts for the hidden overflow pathway to ... Background Chorismate mutases of the AroQ homology class are widespread in the Bacteria and the Archaea. Many of these exist as ... The periplasmic chorismate mutases (denoted *AroQ) are shown to be a distinct subclass of AroQ, being about twice the size of ...
SynthaseProteinEnzymesEscherichiaEnzyme chorismate mutaseProteins99.5Conversion of chorismate to prephenateSaccharomycesPathwayCatalysisSubstrateAllostericAroQYeastMonofunctionalCatalyzesClaisenGeneInhibitionBiosynthesisAmino acidBACILLUS SUBTILISEnzymologyPyruvatemutaseMycobacteriumReactionCharacterizationGlutamicumBacterialBacteriaSequenceResiduesAeruginosaHeteroderaStructuresPotentially
Synthase12
- Chorismate mutase, also known as hydroxyphenylpyruvate synthase , participates in phenylalanine, tyrosine and tryptophan biosynthesis. (wikipedia.org)
- The shikimate pathway enzymes DAHP synthase (CgDS, Cg2391) and chorismate mutase (CgCM, Cgl0853) play a key role in the biosynthesis of aromatic compounds. (uio.no)
- Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner. (semanticscholar.org)
- Chorismate mutase and 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of the methylotrophic actinomycete Amycolatopsis methanolica. (semanticscholar.org)
- Prior research by the Laboratory has identified a series of selected genes, including two key genes for the synthesis of amino acids, cysteine synthase and chorismate mutase. (umsystem.edu)
- The seven enzymes involved in the shikimate pathway are DAHP synthase , 3-dehydroquinate synthase , 3-dehydroquinate dehydratase , shikimate dehydrogenase , shikimate kinase , EPSP synthase , and chorismate synthase . (wikipedia.org)
- Then 5-enolpyruvylshikimate-3-phosphate is transformed into chorismate by a chorismate synthase . (wikipedia.org)
- In P. aeruginosa, salicylate is derived from chorismate via isochorismate by two enzymes: isochorismate synthase (PchA) and isochorismate-pyruvate lyase (IPL, PchB). (ku.edu)
- PchA is an isochorismate synthase (ICS) in P. aeruginosa that removes the C4 hydroxyl group and adds a hydroxyl group to C2-chorismate. (ku.edu)
- Anthranilate is a common precursor of all these compounds and anthranilate synthase (AS) catalyzes the synthesis of anthranilate from chorismate and Gln. (plantphysiol.org)
- Viola C, Saridakis V, Christendat D. Crystal structure of chorismate synthase from Aquifex aeolicus reveals a novel beta alpha beta sandwich topology. (labome.org)
- Recent mechanistic and structural data supporting novel flavin functionalities in reactions catalyzed by chorismate synthase, type II isopentenyl diphosphate isomerase, UDP-galactopyranose mutase, and alkyl-dihydroxyacetonephosphate synthase are presented in this review. (mdpi.com)
Protein9
- This protein is involved in step 1 of the subpathway that synthesizes prephenate from chorismate. (uniprot.org)
- Studies of the bifunctional chorismate mutase-prephenate dehydrogenase of Escherichia coli (T protein) indicate that ionizing groups are important for the mutase reaction ( 2 ). (pnas.org)
- In contrast, bacterial chorismate mutases as e.g., chorismate mutase-prephenate dehydratase of Escherichia coli (P protein) and chorismate mutase of Salmonella typhimurium have highest catalytic activities at alkaline pH ( 4 , 5 ). (pnas.org)
- Potato tubers (Solanum tuberosum) from genotypes differing in chemical susceptibility to the physiological disorder blackspot bruise (TXA 763-5, Atlantic, Ranger Russet, Russet Burbank, and Lemhi Russet) were stored for eight months at 3 C. Protein extracts from each cultivar were assayed for proteinase and chorismate mutase (CM) activities. (naver.com)
- Here, we examined the effects and mechanism of action of an enzymatically hydrolyzed animal protein-based biostimulant (Pepton) on the root growth of tomato plants, with an emphasis on its possible role on chorismate-derived hormones (auxin, salicylic acid, and melatonin). (frontiersin.org)
- This CRADA is a great example of our strategy to make advancements through collaborative research on robust measurements of affinities of small molecules for chorismate mutase and their inhibition of normal protein function. (biospace.com)
- But Wang and her colleagues cloned the parasitism gene the nematodes use to produce a protein that plays an important role in the infection process, known as chorismate mutase. (innovations-report.com)
- The beta1 domain of protein G can replace the chorismate mutase domain of the T-protein FEBS Letters, 586, 466-471. (unam.mx)
- Bacterial P-protein, a bifunctional enzyme composed of two catalytic domains, chorismate mutase and PDT for biosynthesis of phenylalanine (Phe). (expasy.org)
Enzymes4
- These chorismate mutases are typically bifunctional enzymes, meaning they contain two catalytic capacities in the same polypeptide chain. (wikipedia.org)
- Comparison of the x-ray structures of allosteric chorismate mutase from the yeast Saccharomyces cerevisiae with Escherichia coli chorismate mutase/prephenate dehydratase suggested conserved active sites between both enzymes. (pnas.org)
- Unlike some bacterial enzymes, yeast chorismate mutase has highest activity at acidic pH values. (pnas.org)
- Vanholme B, Kast P, Haegeman A, Jacob J, Grunewald W, Gheysen G. Structural and functional investigation of a secreted chorismate mutase from the plant-parasitic nematode Heterodera schachtii in the context of related enzymes from diverse origins. (ugent.be)
Escherichia2
- Most chorismate mutases in this family look similar to that of Escherichia coli . (wikipedia.org)
- Several derivatives of phenylalanine and tyrosine were prepared and tested for inhibition of chorismate mutase-prephenate dehydrogenase (EC 1.3.1.12) from Escherichia coli K12 (strain JP 232). (biochemj.org)
Enzyme chorismate mutase1
- The CRADA research plan brings together the expertise on the bacterial enzyme chorismate mutase of Dr. Prasad Reddy at NIST, with the medicinal chemistry expertise of Primetime to identify a potent and selective inhibitors of chorismate mutase. (biospace.com)
Proteins3
- View all proteins of this organism that are known to be involved in the subpathway that synthesizes prephenate from chorismate , the pathway prephenate biosynthesis and in Metabolic intermediate biosynthesis . (uniprot.org)
- The periplasmic chorismate mutases (denoted *AroQ) are shown to be a distinct subclass of AroQ, being about twice the size of cytoplasmic AroQ proteins. (cuny.edu)
- The body of pioneering information published by these investigators has identified over 60 cyst nematode and more than 50 root-knot nematode parasitism genes encoding a variety of secretory proteins including cellulose-binding proteins, pectate lyases, chitinases, venom allergen-like proteins, chorismate mutases, novel ubiquitin extension proteins, and signaling peptides. (apsnet.org)
99.55
- In enzymology , chorismate mutase ( EC 5.4.99.5 ) is an enzyme that catalyzes the chemical reaction for the conversion of chorismate to prephenate in the pathway to the production of phenylalanine and tyrosine , also known as the shikimate pathway. (wikipedia.org)
- Chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5 ) catalyzes the isomerization of chorismate to prephenate within the tyrosine and phenylalanine biosynthetic pathway. (pnas.org)
- We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5), the 1.9-A crystal structure of the monofunctional enzyme from Bacillus subtilis. (rcsb.org)
- The subcellular locations of two readily discriminated chorismate-mutase (EC 5.4.99.5) isoenzymes from Nicotiana silvestris Speg. (nih.gov)
- This enzyme in the enteric bacteria also possesses EC 5.4.99.5 activity and converts chorismate into prephenate. (expasy.org)
Conversion of chorismate to prephenate1
- Chorismate mutase acts at the first branchpoint of aromatic amino acid biosynthesis and catalyzes the conversion of chorismate to prephenate. (pnas.org)
Saccharomyces2
Pathway5
- Chorismate mutase is found at a branch point in the pathway. (wikipedia.org)
- The joint presence of *AroQ, cyclohexadienyl dehydratase and aromatic aminotransferase in the periplasmic compartment of P. aeruginosa comprises a complete chorismate-to-phenylalanine pathway and accounts for the "hidden overflow pathway" to phenylalanine described previously. (cuny.edu)
- The pathway starts with two substrates , phosphoenol pyruvate and erythrose-4-phosphate and ends with chorismate , a substrate for the three aromatic amino acids. (wikipedia.org)
- Using a reverse genetic approach and metabolic flux analysis, we provide evidence that the cytosolic chorismate mutase is responsible for directing carbon flux towards cytosolic phenylalanine production via the phenylpyruvate pathway. (purdue.edu)
- Thus, our results complete elucidation of phenylalanine biosynthesis via phenylpyruvate in plants, showing that this pathway splits from the known plastidial arogenate pathway at chorismate, instead of prephenate as previously thought, and the complete pathway is localized in the cytosol. (purdue.edu)
Catalysis1
- D. Burschowsky, A. van Eerde, M. Ökvist, A. Kienhöfer, P. Kast, D. Hilvert & U. Krengel (2014) .Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis. (uio.no)
Substrate4
- The enzyme channels the substrate, chorismate to the biosynthesis of tyrosine and phenylalanine and away from tryptophan . (wikipedia.org)
- The reaction mechanism of chorismate mutase has been investigated by different approaches such as stereochemical studies applying molecular orbital calculations ( 1 , 7 ) and by the examination of isotope effects using labeled substrate ( 8 , 9 ). (pnas.org)
- In an alternative mechanism an acidic residue is proposed to protonate the ether oxygen O7 of the substrate chorismate ( 9 ). (pnas.org)
- PchB can also perform an adventitious pericyclic reaction that rearranges chorismate to prephenate possibly due to the homology to the E. coli chorismate mutase (CM). The primary contribution to lower the activation energy for enzymatic pericyclic reactions is controversial and may be arise from electrostatic stabilization of the transition state, or conformational stabilization of the reactive substrate. (ku.edu)
Allosteric1
- 2017. Evolution of Allosteric Regulation in Chorismate Mutases from Early Plants. (wustl.edu)
AroQ5
- [1] The structures of chorismate mutases vary in different organisms, but the majority belong to the AroQ family and are characterized by an intertwined homodimer of 3-helical subunits. (wikipedia.org)
- Chorimate mutase in the AroQ family are more common in nature and are widely distributed among the prokaryotes. (wikipedia.org)
- Specifically, we have constructed large binary-patterned libraries based on the AroQ-class chorismate mutase (CM) from Methanococcus jannaschii (MjCM′) ( 12 , 13 ) and applied evolutionary strategies to evaluate their catalytic capabilities. (pnas.org)
- The emerging periplasm-localized subclass of AroQ chorismate mutases, " by David H. Calhoun, Carol A. Bonner et al. (cuny.edu)
- Background Chorismate mutases of the AroQ homology class are widespread in the Bacteria and the Archaea. (cuny.edu)
Yeast5
- For example, the secondary structure of the chorismate mutase of yeast is very similar to that of E. coli . (wikipedia.org)
- E. coli and Yeast chorismate mutase have a limited sequence homology, but their active sites contain similar residues. (wikipedia.org)
- We have replaced all critical amino acid residues, Arg-16, Arg-157, Lys-168, Glu-198, Thr-242, and Glu-246, of yeast chorismate mutase by aliphatic amino acid residues. (pnas.org)
- Replacement of Glu-246 in the yeast chorismate mutase by glutamine changes the pH optimum for activity of the enzyme from a narrow to a broad pH range. (pnas.org)
- Yeast chorismate mutase is a monofunctional enzyme with a molecular mass of 60,000 Da and is composed of two identical subunits ( 3 ). (pnas.org)
Monofunctional3
- [1] However, the chorismate mutase of eukaryotic organisms are more commonly monofunctional. (wikipedia.org)
- There are organisms such as Bacillus subtilis whose chorismate mutase have a completely different structure and are monofunctional. (wikipedia.org)
- The monofunctional chorismate mutase of Bacillus subtilis has a shallow pH profile with highest mutase activity between pH 5 and 9 ( 6 ). (pnas.org)
Catalyzes3
- Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. (uniprot.org)
- Chorismate mutase (CM) catalyzes the rearrangement of chorismate to prephenate, which can be either converted to hydroxyphenylpyruvate by prephenate dehydrogenase (PD) or to phenylpyruvate by prephenate dehydratase (PDT). (concordia.ca)
- We also show that an alternative transcription start site of a known plastidial enzyme produces a functional cytosolic prephenate dehydratase that catalyzes the conversion of prephenate to phenylpyruvate, the intermediate step between chorismate mutase and phenylpyruvate aminotransferase. (purdue.edu)
Claisen2
- Prephenic acid is then synthesized by a Claisen rearrangement of chorismate by Chorismate mutase . (wikipedia.org)
- As an example, the QM/MM replica path method is applied to the study of the Claisen rearrangement of chorismate to prephenate which is catalyzed by the Bacillus subtilis isolated, chorismate mutase. (springer.com)
Gene3
- The chorismate mutase gene in maize shows strong evidence of selection, with high diversity in teosinte accessions and essentially no diversity among inbred lines. (umsystem.edu)
- To answer this question, three segments of the chorismate mutase gene were sequenced in a panel of 14 landraces, the historical intermediate between teosinte and inbreds. (umsystem.edu)
- In this article, we present the cloning of Hscm1, a gene for chorismate mutase (CM) from the beet cyst nematode Heterodera schachtii. (ugent.be)
Inhibition2
- Isoenzyme CM-1 is sensitive to feedback inhibition by L-tyrosine and comprises the major fraction of total chorismate mutase in suspension-cultured cells. (nih.gov)
- Chorismate mutase provides a critical function in metabolism of microbes and its inhibition by drugs could yield a new class of antibiotics. (biospace.com)
Biosynthesis1
- Chorismate mutase of Brevibacterium flavum, a common enzyme in phenylalanine and tyrosine biosynthesis, was separted into two different component, A and B, with molecular weights of 250,000 and 25,000, respectively, by ammonium sulfate fractionation or gel-filtration. (semanticscholar.org)
Amino acid1
- Westfall CS, Xu A, Jez JM (2014) Structural evolution of differential amino acid effector regulation in plant chorismate mutases. (wustl.edu)
BACILLUS SUBTILIS3
- Among these domains, the most common is chorismate mutase located in the N terminus, such as the DAHPSs from Bacillus subtilis and Listeria monocytogenes (Light et al. (springer.com)
- Structural Studies of Chorismate Mutase Type II (CM_2) from Bacillus Subtilis. (iitr.ac.in)
- Structure of chorismate mutase-like domain of DAHPS from Bacillus subtilis complexed with novel inhibitor reveals conformational plasticity of active site. (purdue.edu)
Enzymology1
- Under this agreement, Primetime will collaborate with Dr. Prasad Reddy who is a recognized expert in chorismate mutase enzymology. (biospace.com)
Pyruvatemutase1
- The systematic name of this enzyme class is chorismate pyruvatemutase . (wikipedia.org)
Mycobacterium1
- and Mycobacterium tuberculosis that convert chorismate to salicylate without requirement of an additional lyase such as PchB in P. aeruginosa. (ku.edu)
Reaction1
- The presence of chorismate mutase increases the rate of the reaction a million fold. (wikipedia.org)
Characterization2
- Characterization of a chorismate mutase from the potato cyst nematode Globodera pallida. (semanticscholar.org)
- Cloning and characterization of an esophageal-gland-specific chorismate mutase from the phytoparasitic nematode Meloidogyne javanica. (semanticscholar.org)
Glutamicum1
- Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum. (semanticscholar.org)
Bacterial1
- Hg-GLAND1 is a putative GCN5-related N-acetyltransferase (GNAT), Hg-GLAND13 is a putative invertase (INV), and Hg-GLAND16 is a putative chorismate mutase (CM), and blastp searches of the non-redundant database resulted in highest similarity to bacterial sequences. (biomedcentral.com)
Bacteria1
- [2] [nb 1] Chorismate mutase is only found in fungi, bacteria, and higher plants. (wikipedia.org)
Sequence1
- The researchers then sequenced those chorismate mutase genes, compared the sequences, and identified unique regions in each sequence. (innovations-report.com)
Residues1
- Large degenerate libraries were prepared by replacing all secondary structure units in a dimeric, helical bundle chorismate mutase with simple binary-patterned modules based on a limited set of four polar and four nonpolar residues. (pnas.org)
Aeruginosa1
- The phenolate type siderophore, such as pyochelin in Pseudomonas aeruginosa, uses salicylate derived from chorismate as a precursor. (ku.edu)
Heterodera1
- Bekal S, Niblack TL, Lambert KN (2003) A chorismate mutase from the soybean cyst nematode Heterodera glycines shows polymorphisms that correlate with virulence. (springer.com)
Structures1
- He used X-ray diffraction to solve the three-dimensional structures of carboxypeptidase A, aspartate carbamoyltransferase, leucine aminopeptidase, HaeIII methyltransferase convalently complexed to DNA, human interferon beta, chorismate mutase and fructose-1,6-bisphosphatase. (asbmb.org)
Potentially2
- A potentially secreted chorismate mutase has been isolated from the potato cyst nematode Globodera pallida. (semanticscholar.org)
- Dr. Reddy of the Biomolecular Measurement Division of the National Institute of Standards and Technology added, "Given what we know about the structure and function of chorismate mutase, this enzyme provides a potentially new target for generation of antimicrobial agents. (biospace.com)