An isomerase that catalyzes the conversion of chorismic acid to prephenic acid. EC 5.4.99.5.
A cyclohexadiene carboxylic acid derived from SHIKIMIC ACID and a precursor for the biosynthesis of UBIQUINONE and the AROMATIC AMINO ACIDS.
An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. EC 4.2.1.51.
An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD. In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosine. EC 1.3.1.12.
An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.
An enzyme that catalyzes the conversion of 2-phospho-D-glycerate to 3-phospho-D-glycerate. EC 5.4.2.1.
A tri-hydroxy cyclohexene carboxylic acid important in biosynthesis of so many compounds that the shikimate pathway is named after it.
An enzyme that catalyzes the formation of 7-phospho-2-keto-3-deoxy-D-arabinoheptonate from phosphoenolpyruvate and D-erythrose-4-phosphate. It is one of the first enzymes in the biosynthesis of TYROSINE and PHENYLALANINE. This enzyme was formerly listed as EC 4.1.2.15.
An enzyme that catalyzes the transfer of phosphate from C-3 of 1,3-diphosphoglycerate to C-2 of 3-phosphoglycerate, forming 2,3-diphosphoglycerate. EC 5.4.2.4.
Six-carbon alicyclic hydrocarbons which contain one or more double bonds in the ring. The cyclohexadienes are not aromatic, in contrast to BENZOQUINONES which are sometimes called 2,5-cyclohexadiene-1,4-diones.
Enzymes that catalyze the cleavage of a phosphorus-oxygen bond by means other than hydrolysis or oxidation. EC 4.6.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
A group of compounds that are derivatives of phenylpyruvic acid which has the general formula C6H5CH2COCOOH, and is a metabolite of phenylalanine. (From Dorland, 28th ed)
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Amino acids containing an aromatic side chain.
The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.
Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.
Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.
An actinomycete from which the antibiotic CHLORTETRACYCLINE is obtained.
A gram-positive organism found in dairy products, fresh and salt water, marine organisms, insects, and decaying organic matter.
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.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
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.
Benzoic acids, salts, or esters that contain an amino group attached to carbon number 2 or 6 of the benzene ring structure.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
Six-carbon alicyclic hydrocarbons.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The space between the inner and outer membranes of a cell that is shared with the cell wall.
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
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.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
An enzyme that catalyzes the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine. Anthranilate is the biosynthetic precursor of tryptophan and numerous secondary metabolites, including inducible plant defense compounds. EC 4.1.3.27.
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)
The rate dynamics in chemical or physical systems.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A mechanism of communication within a system in that the input signal generates an output response which returns to influence the continued activity or productivity of that system.
Alkaloids derived from TYRAMINE combined with 3,4-dihydroxybenzaldehyde via a norbelladine pathway, including GALANTAMINE, lycorine and crinine. They are found in the Amaryllidaceae (LILIACEAE) plant family.
Substituted thioglucosides. They are found in rapeseed (Brassica campestris) products and related cruciferae. They are metabolized to a variety of toxic products which are most likely the cause of hepatocytic necrosis in animals and humans.
An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.
A monocot family within the order Liliales. This family is divided by some botanists into other families such as Convallariaceae, Hyacinthaceae and Amaryllidaceae. Amaryllidaceae, which have inferior ovaries, includes CRINUM; GALANTHUS; LYCORIS; and NARCISSUS and are known for AMARYLLIDACEAE ALKALOIDS.
A plant genus of the family LILIACEAE. Members contain radiatine, vittatine, haemanthamine, lycorenine, dihydrolycorine, lycorine, lycoricidinol and lycoricidine.
An enzyme that catalyzes the activation of sulfate ions by ATP to form adenosine-5'-phosphosulfate and pyrophosphate. This reaction constitutes the first enzymatic step in sulfate utilization following the uptake of sulfate. EC 2.7.7.4.
A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.
A basis of value established for the measure of quantity, weight, extent or quality, e.g. weight standards, standard solutions, methods, techniques, and procedures used in diagnosis and therapy.
Washing liquid obtained from irrigation of the lung, including the BRONCHI and the PULMONARY ALVEOLI. It is generally used to assess biochemical, inflammatory, or infection status of the lung.
Binary classification measures to assess test results. Sensitivity or recall rate is the proportion of true positives. Specificity is the probability of correctly determining the absence of a condition. (From Last, Dictionary of Epidemiology, 2d ed)
A species of gram-negative, aerobic BACTERIA. It is a commensal and pathogen only of humans, and can be carried asymptomatically in the NASOPHARYNX. When found in cerebrospinal fluid it is the causative agent of cerebrospinal meningitis (MENINGITIS, MENINGOCOCCAL). It is also found in venereal discharges and blood. There are at least 13 serogroups based on antigenic differences in the capsular polysaccharides; the ones causing most meningitis infections being A, B, C, Y, and W-135. Each serogroup can be further classified by serotype, serosubtype, and immunotype.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
Washing out of the lungs with saline or mucolytic agents for diagnostic or therapeutic purposes. It is very useful in the diagnosis of diffuse pulmonary infiltrates in immunosuppressed patients.
The statistical reproducibility of measurements (often in a clinical context), including the testing of instrumentation or techniques to obtain reproducible results. The concept includes reproducibility of physiological measurements, which may be used to develop rules to assess probability or prognosis, or response to a stimulus; reproducibility of occurrence of a condition; and reproducibility of experimental results.

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)

Background Chorismate mutases of the AroQ homology class are widespread in the Bacteria and the Archaea. Many of these exist as domains that are fused with other aromatic-pathway catalytic domains. Among the monofunctional AroQ proteins, that from Erwinia herbicola was previously shown to have a cleavable signal peptide and located in the periplasmic compartment. Whether or not this might be unique to E. herbicola was unknown. Results The gene coding for the AroQ protein was cloned from Salmonella typhimurium, and the AroQ protein purified from both S. typhimurium and Pseudomonas aeruginosa was shown to have a periplasmic location. The periplasmic chorismate mutases (denoted *AroQ) are shown to be a distinct subclass of AroQ, being about twice the size of cytoplasmic AroQ proteins. The increased size is due to a carboxy-terminal extension of unknown function. In addition, a so-far novel aromatic aminotransferase was shown to be present in the periplasm of P. aeruginosa. Conclusions Our analysis has
An additional stabilizing factor in this enzyme-substrate complex is hydrogen bonding between the lone pair of the oxygen in the vinyl ether system and hydrogen bond donor residues. Not only does this stabilize the complex, but disruption of resonance within the vinyl ether destabilizes the ground state and reduces the energy barrier for this transformation. An alternative view is that electrostatic stabilization of the polarized transition state is of great importance in this reaction. In the chorismate mutase active site, the transition-state analog is stabilized by 12 electrostatic and hydrogen-bonding interactions.[8] This is shown in mutants of the native enzyme in which Arg90 is replaced with citrulline to demonstrate the importance of hydrogen bonding to stabilize the transition state.[9] Other work using chorismate mutase from Bacillus subtilis showed evidence that when a cation was aptly placed in the active site, the electrostatic interactions between it and the negatively charged ...
1COM: The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction.
BioAssay record AID 52148 submitted by ChEMBL: The compound was tested for inhibition of Bacillus subtilis chorismate mutase (BcCM).
The Claisen rearrangement is a carbon-carbon bond-forming, pericyclic reaction of fundamental importance due to its relevance in synthetic and mechanistic investigations of organic and biological chemistry. Despite continued efforts, the molecular origins of the rate acceleration in going from the aqueous phase into the protein is still incompletely understood. In the present work, the rearrangement reactions for allyl-vinyl-ether (AVE), its dicarboxylated variant (AVE-(CO2)2), and the biologically relevant substrate chorismate are investigated in the gas phase, water, and in chorismate mutase. Only the rearrangement of chorismate in the enzyme shows a negative differential barrier when compared to the reaction in water, which leads to the experimentally observed catalytic effect for the enzyme. The molecular origin of this effect is the positioning of AVE-(CO2)2 and chorismate in the protein active site compared to AVE. Furthermore, in going from AVE-(CO2)2 to chorismate, entropic effects due ...
Hi, I have a Yeast question that I hope someone in the group can answer. In bacteria the conversion of chorismate to para-hydroxybenzoate (PHB) is the first step in ubiquinone biosynthesis. The reaction is carried out by the enzyme chorismate pyruvate lyase (CPL) encoded by the ubiC gene. In a search of the literature I have not been able to find any references to a CPL activity in Yeast. Is it known that chorismate is converted directly to PHB in Yeast as part of ubiquinone synthesis, or is the PHB derived from a different pathway? If it is a direct conversion it would seem that petite mutants blocked at this step would have been isolated and described in the literature. Have I missed something or is there a gap in the information on this pathway? Many Thanks, Frank Mondello ...
Pericyclic reactions possess changed reactivities in the excited state compared to the ground state which complement each other, as can be shown by simple frontier molecular orbital analysis. Hence, most molecules that undergo pericyclic reactions feature two different photochemical pathways. In this thesis an investigation of the first nanoseconds after excitation of Diazo Meldrums acid (DMA) is presented. The time-resolved absorption change in the mid-infrared spectral region revealed indeed two reaction pathways after excitation of DMA with at least one of them being a pericyclic reaction (a sigmatropic rearrangement). These two pathways most probably start from different electronic states and make the spectroscopy of DMA especially interesting. Femtochemistry also allows the spectroscopy of very short-lived intermediates, which is discussed in context of the sequential mechanism of the Wolff rearrangement of DMA. An interesting application of pericyclic reactions are also molecular ...
1. Introduction. The main object of the 6cm Activity Ladder is to promote ATV activity on 5.6GHz. Anyone interested in ATV, whether they are members of the British Amateur Television Club or not, are welcome to take part. 2. Eligibility. BATC Contests are open to all licensed radio amateurs who are equipped to transmit pictures by analogue or digital Fast Scan. There is no receive only section. 3. Dates and Times. The competition will run from 0000hrs UTC on 1st June 2021 to 2359hrs UTC on the 31st December 2021. 4. Location. At least one of the stations in each claimed contact must be operating from a location that is not his main station address (this is to prevent stations with fixed 5.6 GHz links between them claiming points every day and distorting the results). Operating locations must be within the terms of your licence. If operating away from your main station, please get the permission of the landowner. It is essential that you adhere to any local and national COVID virus movement and ...
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). The best inhibitors were N-toluene-p-sulphonyl-L-phenylalanine, N-benzenesulphonyl-L-phenylalanine and N-benzloxycarbonyl-L-phenylalanine. Consequently two compounds, N-toluene-sulphonyl-L-p-aminophenylalanine and N-p-aminobenzenesulphonyl-L-phenylalanine, were synthesized for coupling to CNBr-activated Sepharose-4B. The N-toluene-p-sulphonyl-L-p-aminophenylalanine-Sepharose-4B conjugate was shown to bind the enzyme very strongly at pH 7.5. The enzyme was not eluted by various eluents, including 1 M-NaCl, but could be quantitatively recovered by washing with buffer of pH9. Elution was more effective in the presence of 10 mM-1-adamantaneacetic acid, a competitive inhibitor of the enzyme. This affinity-chromatography procedure results in a high degree of purification of the enzyme and can be used to prepare ...
In Escherichia coli, chorismate lyase catalyzes the first step in ubiquinone biosynthesis, the conversion of chorismate to 4-hydroxybenzoate. 4-Hydroxybenzoate is converted to 3-octaprenyl-4-hydroxybenzoate by 4-hydroxybenzoate octaprenyltransferase. These two enzymes are encoded by ubiC and ubiA, respectively, and have been reported to map near one another at 92 min on the E. coli chromosome. We have cloned the ubiCA gene cluster and determined the nucleotide sequence of ubiC and a portion of ubiA. The nucleotide sequence abuts with a previously determined sequence that encodes a large portion of ubiA. ubiC was localized by subcloning, and overproducing plasmids were constructed. Overexpression of ubiC allowed the purification of chorismate lyase to homogeneity, and N-terminal sequence analysis of chorismate lyase unambiguously defined the beginning of the ubiC coding region. Although chorismate lyase showed no significant amino acid sequence similarity to 4-amino-4-deoxychorismate lyase ...
Replacement of two invariant serine residues in chorismate synthase provides evidence that a proton relay system is essential for intermediate formation and catalytic activity ...
Deletion of the I265-F268 and T271-K277 regions in the large lumenally exposed loop of the CP47 protein are known to lead to a loss of photoautotrophic growth. Here, these regions have been investigated by combinatorial mutagenesis and pseudorevertant mapping. No single amino-acid residue in the I265-F268 region was found to be critical for function, but a large hydrophobic residue at position 267 and preferentially an aromatic residue at position 268 appeared to be required for photoautotrophic growth. Starting from an obligate photoheterotrophic mutant lacking the T271-K277 region, photoautotrophic pseudorevertants were generated with short in-frame tandem repeats near the site of the original deletion, partially or fully restoring the length of the original protein. These pseudorevertants were sensitive to oxygen indicating that the T271-K277 region may provide PS II stability and/or protection against oxygen-dependent photoinactivation. Pseudorevertants with much improved photoautotrophic ...
Postdoc in Computational Enzyme Design KTH, School of Engineering Sciences in Chemistry, Biotechnology & Health KTH Royal Institute of Technology in
in the group: January, 2006 (grad); July, 2010 (postdoc) to July 2013. project(s): terpene biosynthesis, organic reaction mechanisms, computational NMR, catalyst design. dissertation title: Theoretical and Experimental Mechanistic Studies on Sesquiterpene Biosynthesis, Oxyanion-Accelerated Pericyclic Reactions, and More. went off to: teach at Butte College and Chico State. ...
2012, Ait-Aissa S, Billaudel B, Poulletier de Gannes F, Ruffie G, Duleu S, Hurtier A, Haro E, Taxile M, Athane A, Geffard M, Wu T, Wiart J, Bodet D, Veyret B, Lagroye I ...
3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase (EC 2.5.1.54) is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme. In enzymology, a DAHP synthase (EC 2.5.1.54) is an enzyme that catalyzes the chemical reaction phosphoenolpyruvate + D-erythrose 4-phosphate + H2O ⇌ {\displaystyle \rightleftharpoons } 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate The three substrates of this enzyme are phosphoenolpyruvate, D-erythrose 4-phosphate, and H2O, whereas its two products are ...
Biosynthesis of the aromatic amino acids tryptophan, tyrosine, and phenylalanine proceeds via a common pathway to chorismate, at which point the pathway branches (CITS:[Jones][1943992]). One branch proceeds to tryptophan, and the other to tyrosine and phenylalanine (CITS:[Jones]). The series of reactions to chorismate, called the shikimate pathway, and the series of reactions from chorismate to tryptophan have been found to be common to all eukaryotes and prokaryotes studied thus far (as reported in (CITS:[1943992])). In contrast, there appears to be two separate routes from chorismate to tyrosine and phenylalanine, only one of which has been found in S. cerevisiae (CITS:[1943992]). Aromatic amino acid biosynthesis in S. cerevisiae is controlled by a combination of feedback inhibition, activation of enzyme activity, and regulation of enzyme synthesis (CITS:[Jones][1943992]). The first step in the tryptophan branch is feedback inhibited by tryptophan, and the first step in the ...
Hoffmann, R.; Tantillo, D. J. Angew. Chem. Int. Ed. 2003, 42, 5877-5882: Breaking Down Barriers: The Liaison Between Sigmatropic Shifts, Electrocyclic Reactions and 3-Center Cations. Ponec, R.; Bultinck, P.; Van Damme, S.; Carbo, R.; Tantillo, D. J. Theor. Chem. Acc. 2005, 113, 205-211: Geometric and Electronic Similarities between Transition Structures for Electrocyclizations and Sigmatropic Hydrogen Shifts. Tantillo, D. J. Annu. Rep. Prog. Chem., Sect. B 2006, 102, 269-289: Reaction Mechanisms. Part (ii) Pericyclic Reactions. Tantillo, D. J.; Lee, J. K. Annu. Rep. Prog. Chem., Sect. B 2007, 103, 272-293: Reaction Mechanisms. Pericyclic Reactions. Lee, J. K.; Tantillo, D. J. Annu. Rep. Prog. Chem., Sect. B 2008, 104, 260-283: Reaction Mechanisms. Pericyclic Reactions. Nouri, D. H.; Tantillo, D. J. Tetrahedron 2008, 64, 5672-5679: Sigmatropic Shifts and Cycloadditions on Neutral, Cationic, and Anionic Pentadienyl + Butadiene Potential Energy Surfaces. Tantillo, D. J. Angew. Chem. ...
TY - GEN. T1 - Analysis of a trimeric complex involving chorismate synthase from Bacillus subtilis. AU - Fitzpatrick, Teresa B.. AU - Amrhein, Nikolaus. AU - Macheroux, Peter. PY - 1999. Y1 - 1999. M3 - Conference contribution. SP - 749. EP - 752. BT - Proceedings of the 13th International Symposium. PB - Rudolf Weber. CY - Berlin. ER - ...
Pyranose-Furanose mutases are enzymes that catalyze the isomerization of six-membered pyranose and five-membered furanose forms of a nucleotide-based sugar. In this research, the substrate binding site of three different mutases were investigated; UDP-galactopyranose mutase (UGM), GDP-altro-heptopyranose mutase (GaHM) and UDP-arabinopyranose mutase (UAM). Both UGM and UAM use a UDP-based sugar as the substrate but require different cofactors, flavin adenine dinucleotide (FAD) and Mn2+ respectively, to function. UGM and GaHM use the same cofactor (FAD), but the latter prefers to work with a GDP-based sugar. In this thesis, studies have been conducted on these three mutases using a variety of tools, such as X-ray crystallography, protein modeling, site-directed mutagenesis and kinetic assays, to understand how these enzymes bind their respective substrates. Among these three mutases, UGM is the best-studied enzyme and is a validated drug target in Mycobacteria. Despite this, the structural role of ...
The last chapter is entirely new, and features how the techniques of computational organic chemistry, as discussed in the previous eight chapters, can be employed toward explicating enzymatic reactions. The chapter is not an in-depth survey of all of the activities in computational enzyme action - that would require its own full-length book - but rather its an overview to inspire you. The chapter begins with a brief discussion of enzymatic models, including the Pauling paradigm and Goodmans model. Then computational strategies for addressing the large molecules involved in enzymatic studies are presented including QM/MM, adiabatic mapping, and the use of some very large-scale computations as benchmarks. Next, I present two case studies: of chorismate mutase and of catechol-O-methyltransferase (COMT). The chapter ends with a presentation of the progress in de novo design of enzymes capable of catalyzing specific reactions as developed by Baker and Houk.. ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Bornemann, S., Lowe, D.J. and Thorneley, R.N. (1996). „The transient kinetics of Escherichia coli chorismate synthase: substrate consumption, product formation, phosphate dissociation, and characterization of a flavin intermediate. Biochemistry. 35: 9907-9916. PMID 8703965 ...
Orbital correlation diagrams are all fine and dandy, but they can be put on a much more solid footing by constructing the relevant state correlation diagrams. I have deliberately avoided using the word state up until now. Here, state refers to an electronic state of the system as a whole.4 The simplest expression for an electronic state is given by a Slater determinant, and we will simply abbreviate it to the usual form that the organic chemists do. For example, in the ground state of the reactants, we can write. $$\Psi_1 = \psi_1^2\psi_2^2$$. where the antisymmetrisation is implicit. The use of capital $\Psi$ instead of small $\psi$ emphasises that this is a total electronic state of a system. The subscript 1 indicates that it is the ground state.. The electronic states of the reactants are well-described by single Slater determinants. For a system with 4 MOs and 4 electrons, there are a total of $8!/4!4! = 70$ states, and so theoretically we need to look at $\Psi_1$ through $\Psi_{70}$. ...
Regulation and Cell signalingRegulation and Cell signaling - no subcategoryCell envelope-associated LytR-CpsA-Psr transcriptional attenuators Prephenate dehydratase (EC 4.2.1.51) ...
The Haro 14mm 48 spoke Replacement Wheel is the perfect replacement for F1 / F2 & Backtrail X1, featuring Haro 48 hole single wall black anodized alloy rim and 14mm sealed mechanism hubs.
Vans and Haro Bikes will be joining forces to bring together an apparel capsule collection and a couple pairs of Vans Era & Sk8 His. In honor of this joint venture, legendary BMX rider Dennis McCoy sits and discusses the evolution of Haro and what the company means to BMX. Take a look at the video and keep an eye out for the collabs to hit stores soon.. ...
One thing I was really looking forward to when switching to Kartys mechanistically organized text was how reactions involving alkenes would be addressed. I expected to see the reactions simply grouped by mechanism; for example, the electrophilic addition reaction mechanisms would be grouped together, as would the pericyclic reaction mechanisms and so on. Instead, I…
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Tyra Banks Lookbook: Tyra Banks wearing Medium Curls with Bangs (1 of 11). Tyra Banks styled her hair in carefree curls and wispy bangs while attending the 2011 New Front Conference.
Indonesia berpotensi menghasilkan pelepah kelapa sawit atau Oil Palm Frond (OPF) sebanyak 81,887,936 ton/tahun. Ekstrak cair pelepah kelapa sawit memiliki kandungan karbon 19388 ppm dan nitrogen 142 ppm, serta kandungan glukosa sebesar 53.95 ± 2.86 g/L. Kandungan yang dimiliki tersebut memberikan potensi pelepah sawit sebagai bahan baku dalam mikrobiologi industri. Penelitian ini bertujuan melakukan optimasi produksi asam glutamat menggunakan variasi sumber nitrogen dan konsentrasi sumber nitrogen, variasi konsentrasi biotin, variasi waktu fermentasi dengan dua variasi isolat Brevibacterium flavum dan Bacillus sp. dalam media fermentasi ekstrak cair pelepah kelapa sawit atau Oil Palm Frond (OPF). Hasil fermentasi asam glutamat yang diperoleh pada penelitian ini dapat disimpulkan bahwa perlakuan biotin dengan 0.5% urea yang paling berpengaruh terhadap konsentrasi asam glutatamat. Isolat yang paling berpengaruh adalah Brevibacterium flavum pada jam ke-40 dengan konsentrasi asam glutamat yang ...
This entry represents a motif conserved in many allosteric enzymes involved in amino acid and purine biosynthesis, called the ACT domain as the acronym for aspartate kinase, chorismate mutase, and TyrA (prephenate dehydrogenase). Several crystal structures have been determined for proteins that have ACT domains, such as 3-phosphoglycerate dehydrogenase (3PGDH),15 threonine deaminase (TD),16 acetohydroxyacid synthase III,17 and NikR, a transcriptional regulator involved in nickel uptake. The ACT domain consists of 4 beta-strands and 2 alpha-helices PMID:17350037 ...
Reviewer #3: This study compared the EFMO method with ONIOM method as for the reaction free energy barrier for the Chorismate Mutase. In general, the results are more consistent than that of the ONIOM. This review agrees that the current manuscript is publishable, and expect the authors to explain the possible reasons for: (1) the calculated free energy barrier is much higher than that of the experimentally measured enthalpy change? (2) The authors claimed that the MP2-geometry optimization make it 3.5 kcal/mol lower for the free energy barrier than that of the ONIOM method, however, the listed data of free energy barrier in Table2 is close to each other at the same calculation level. (3) The portability to other enzyme system of EFMO method ...
Aminodeoxychorismate synthase/glutamine amidotransferase ; Bifunctional enzyme that catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine. In the first step, a glutamine amidotransferase generates ammonia that is channelled between the binding sites of glutamine and chorismate and used along with chorismate in the second step, catalyzed by aminodeoxychorismate synthase, to produce ADC. Required for the synthesis of 4-aminobenzoate (PABA), an important component in tetrahydrofolate biosynthesis. Does not possess ADC lyase activity (902 aa ...
Anthranilate synthase catalyses the conversion of chorismate to anthranilate, a key step in tryptophan biosynthesis. A series of 3-(1-carboxy-ethoxy) benzoic acids were synthesised as chorismate analogues, with varying functionality at C-4, the position of the departing hydroxyl group in chorismate. Most of the com In memory of Chris Abell
Abstract :. Design and validation of pericyclic reactions for sensing conformational stretching in polymer materials.. The naphthalene and anthraquinone based fluorescent reporter molecules were synthesized in multistep for monitoring pericyclic reactions in polymers. These reporter molecules were incorporated into polymer backbones by click reactions. The reaction was monitored optically and optimized using organic chemistry characterization techniques. The mechanical force felicitate to bonds to come into proper orientation for claisen reaction to occur. The overall goal of the research is to design, implement, and validate functional groups designed to react specifically within stressed polymer materials to signal the onset of mechanical failure.. Design and synthesis of Novel Alternating sulfone copolymers for biomedical applications. Interest in stimulus-responsive polymers and materials has been increasing in recent years. In particular, efforts to apply these polymers for biomedical ...
Steric effects are important in synthesis. Whilst steric hindrance is well known in hindering reactions, steric effects can also be employed to accelerate reactions, in particular cycloaddition reactions, and even to promote reactions that otherwise do not occur. A survey is included in previous work on steric effects in chemical reactions, principally cycloadditions. This includes a brief discussion on the importance of orientation and solvent effects on Diels-Alder cyclisations and ene reactions. The effect of substituents on the cyclisation of N-allyl furfurylamines has been studied. It was shown that bulky N-protecting groups enhance cyclisation, an effective buttress being the trityl (triphenylmethyl) group. The latter has the added advantage of being particularly easy to remove. A study of some ene reactions has also been carried out and steric acceleration of these processes has also been observed. A novel reaction involving an intermolecular cycloaddition followed by a sterically ...
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring ...
View Notes - Organic Lab Reactions 31 from CHM 2210 at University of Florida. 26 THE CLAISEN REARRANGEMENT allyl 2-carbomethoxy-6-methylphenyl ether (LXXXV) undergoes the para rearrangement when the
Amino Acids and Derivatives,Aromatic amino acids and derivatives,Common Pathway For Synthesis of Aromatic Compounds (DAHP synthase to chorismate),3-dehydroquinate synthase (EC 4.2.3.4 ...
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First, NICS(0) values for a series of related intermolecular anionic attack at alkynes show some interesting trends (Table 1). Two of the transition states look like they might be aromatic: the TSs for the 3-exo-dig and the 5-endo-dig reaction have NICS(0) values that are quite negative. However, given the geometry of these TSs, particularly the close proximity of the σ bonds to the ring center, one might be concerned about contamination of these orbitals. So, NICS(0)MOzz computations, which look at the tensor component perpendicular to the ring using just the π-MOs, shows that the 3-exo-dig is likely non-aromatic (NICS(0)MOzz is near zero), the TS for the 4-endo-dig reaction is antiaromatic (NICS(0)MOzz very positive) and the TS for the 5-endo-dig reaction is aromatic (NICS(0)MOzz is very negative. So this last reaction is the first example of an aromatic transition that is not for a pericyclic reaction ...
TY - JOUR. T1 - Augmenting the anisotropic network model with torsional potentials improves PATH performance, enabling detailed comparison with experimental rate data. AU - Chandrasekaran,Srinivas Niranj. AU - Carter,Charles W.. PY - 2017/5/1. Y1 - 2017/5/1. N2 - PATH algorithms for identifying conformational transition states provide computational parameters-time to the transition state, conformational free energy differences, and transition state activation energies-for comparison to experimental data and can be carried out sufficiently rapidly to use in the high throughput mode.These advantages are especially useful for interpreting results from combinatorial mutagenesis experiments. This report updates the previously published algorithm with enhancements that improve correlations between PATH convergence parameters derived from virtual variant structures generated by RosettaBackrub and previously published kinetic data for a complete, four-way combinatorial mutagenesis of a conformational ...
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... 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 ...
Schmidt JC; Zalkin H (1969). "Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from ...
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 ...
"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 ...
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): 3700-3705. 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 ...
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. ... The pathway starts with two substrates, phosphoenol pyruvate and erythrose-4-phosphate and ends with chorismate, a substrate ...
Chorismate mutase is an intramolecular transferase and it catalyzes the conversion of chorismate to prephenate, used as a ... though the rate increases 106 fold in the presence of chorismate mutase. The reaction goes through a chair transition state ... "A strategically positioned cation is crucial for efficient catalysis by chorismate mutase". The Journal of Biological Chemistry ... Sub-categories of this class are: This category (EC 5.4) includes intramolecular transferases (mutases). These isomerases ...
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, ...
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- ...
Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3 ...
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. ...
Chorismate mutase then converts chorismic acid to prephenate via a Claisen rearrangement (1,3-sigmatropic rearrangement). ...
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- ...
... 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, ...
ADTs contain an N-terminal transit peptide, a PDT-like domain, and an ACT (Aspartokinase, chorismate mutase, TyrA) domain. ...
The ACT domain is named after three of the proteins that contain it: aspartate kinase, chorismate mutase and TyrA. The ...
In the synthesis of L-phenylalanine, chorismate undergoes a Claisen rearrangement by a Chorismate mutase enzyme to form ...
"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 ...
One project demonstrated that an engineered version of Chorismate mutase still had catalytic activity when only 9 amino acids ...
The enzyme chorismate mutase catalyzes the Claisen rearrangement of the enol ether called chorismate to prephenate, an ...
... may refer to: Prephenate dehydrogenase, an enzyme Chorismate mutase, an enzyme This set index ...
The enzyme chorismate mutase (EC 5.4.99.5) catalyzes the Claisen rearrangement of chorismate to prephenate, an intermediate in ...
... pathway of aromatic amino acids in Nocardia mediterranei 1994 Cloning vector system for Nocardia spp 1995 Chorismate mutase and ...
... chorismate mutase (CM) and isochorismatase (ICM), thought to be interfering on the salicylic acid pathway and thereby altering ...
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 ...
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, ... phosphoenolpyruvate mutase EC 5.4.2.10: phosphoglucosamine mutase EC 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate- ... 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)-α-D-glucan 1-α-D- ...
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): ...
The 2014 Ju-Jitsu World Championship were the 12th edition of the Ju-Jitsu World Championships, and were held in Paris, France from November 28 to November 30, 2014. 28.11.2014 - Men's and Women's Fighting System, Men's and Women's Jiu-Jitsu (ne-waza), Men's Duo System - Classic 29.11.2014 - Men's and Women's Fighting System, Men's and Women's Jiu-Jitsu (ne-waza), Women's Duo System - Classic 30.11.2014 - Men's Jiu-Jitsu (ne-waza), Mixed Duo System - Classic, Team event Vincent MATCZAK (2014-09-30). "4TH INVITAION TO WORLD CHAMPIONSHIP 2014" (PDF). Retrieved 2019-11-28.[dead link] Online results Official results (PDF) Mixed team event results (PDF) (All articles with dead external links, Articles with dead external links from April 2022, Ju-Jitsu World Championships, 2014 in French sport ...
Bolley L. "Bo" Johnson (born November 15, 1951) is an American politician from the state of Florida. A member of the Democratic Party, Johnson was a member of the Florida House of Representatives, and served as the Speaker of the Florida House of Representatives. Johnson is from Milton, Florida. His father and grandfather served as county commissioners for Santa Rosa County, Florida. Johnson graduated from Milton High School, and became the first member of his family to attend college. He received his bachelor's degree from Florida State University. Johnson volunteered for Mallory Horne when Horne served as the president of the Florida Senate. At the age of 22, Johnson met Lawton Chiles, then a member of the United States Senate, who hired him as a legislative aide in 1973. Johnson was elected to the Florida House of Representatives, representing the 4th district from November 7, 1978 to November 3, 1992. He also served the 1st district from November 3, 1992 to November 8, 1994. He became the ...
... may refer to: Don't Say No (Billy Squier album), a 1981 album by American rock singer Billy Squier, and its title track Don't Say No (Seohyun EP), a 2016 extended play by South Korean pop singer Seohyun, and its title track "Don't Say No" (Tom Tom Club song), from the 1988 album Boom Boom Chi Boom Boom "Don't Say No", by Robbie Williams from the 2005 album Intensive Care "Don't Say No Tonight", a 1985 single by Eugene Wilde This disambiguation page lists articles associated with the title Don't Say No. If an internal link led you here, you may wish to change the link to point directly to the intended article. (Disambiguation pages with short descriptions, Short description is different from Wikidata, All article disambiguation pages, All disambiguation pages, Disambiguation pages ...
A DFT-Based QM-MM Approach Designed for the Treatment of Large Molecular Systems: Application to Chorismate Mutase. ... A DFT-Based QM-MM Approach Designed for the Treatment of Large Molecular Systems: Application to Chorismate Mutase. ...
Chorismate mutase. No expression. ++. ++. Burkholderia pseudomallei. ZP_04891863.1. 267-404. Hemagglutinin-family protein. ...
... chorismate mutase; PPNDH, prephenate dehydratase; PHETA1, phenylalanine transaminase; ASPTA, aspartate transaminase; ASPK, ... Dashed arrows indicate several reactions from the shikimate and chorismate pathways. Abbreviations for reaction names are as ... phosphoglycerate mutase (PGM) and enolase (ENO). Especially here, it is important to state that all these reversible reactions ... phosphoglycerate mutase; ENO, enolase; PPS, phosphoenolpyruvate synthase; LDH, D-lactate dehydrogenase; PFL, pyruvate formate ...
Crystal structure of the cytoplasmic chorismate mutase from Zea mays. Class: plant protein. Keywords: Chorismate mutase, Zea ... Compound: chorismate mutase. Species: Zea mays [TaxId:4577]. Database cross-references and differences (RAF-indexed): *Uniprot ... Compound: chorismate mutase. Species: Zea mays [TaxId:4577]. Database cross-references and differences (RAF-indexed): *Uniprot ...
Chorismate Mutase Enzyme, Catalysis, Chemical reaction, Chorismic acid, Prephenic acid, Phenylalanine, Tyrosine, Shikimic acid ...
Chorismate mutase is one of the essential enzymes in the shikimate pathway and is key to the survival of the organism ...
Zhang, S.; Pohnert, G.; Kongsaeree, P.; Wilson, D. B.; Clardy, J.; Ganem, B.: Chorismate mutase-prephenate dehydratase from ...
Bacillus chorismate mutase-like. L30e-like. L30e-like. e6p5jO1. O:2-82. HTH. 40S ribosomal protein S13 N-terminal domain. 40S ... Bacillus chorismate mutase-like. L30e-like. L30e-like. e6p5jAh1. Ah:2-123. Long alpha-hairpin. Ribosomal protein L29 (L29p). ... Bacillus chorismate mutase-like. L30e-like. L30e-like. e6p5jAC2. AC:274-363. C-terminal helical region in 60S ribosomal protein ...
Structural evolution of differential amino acid effector regulation in plant chorismate mutases. J Biol Chem 289, 28619-28 ...
Bacterial GlnD proteins contain two C-terminal ACT domains (named after aspartate kinase, chorismate mutase and TyrA) that are ...
A novel Meloidogyne incognita chorismate mutase effector suppresses plant immunity by manipulating the salicylic acid pathway ...
A chorismate mutase from the soybean cyst nematode Heterodera glycines shows polymorphisms that correlate with virulence. Mol ... Several nematode effectors from root-knot and cyst nematodes, such as cellulases, pectinases, expansins, chorismate mutase and ...
chorismate mutase. chorismate mutase (EC 5.4.99.5) (TIGR01795). 91%. 114.7. prephenate dehydrogenase (EC 1.3.1.12). 37%. 43.5. ... 4 candidates for cmutase: chorismate mutase. Score. Gene. Description. Similar to. Id.. Cov.. Bits. Other hit. Other id.. Other ... chorismate mutase-like protein. CM_2 (PF01817). 99%. 66.1. lo. PGA1_c16860. anthranilate synthase component 1. Salicylate ... Comment: Chorismate mutase is usually fused to prephenate dehydratase, which makes it difficult to find this activity when it ...
... chorismate mutase-prephenate dehydratase, PDT protein, MtbPDT, chorismate mutase prephenate dehydratase, CM-PDT, AroQ, CM/PDT/ ... Chorismate mutase/prephenate dehydratase, dehydratase, prephenate, monofunctional prephenate dehydratase, P-protein, ...
Chorismate mutase (substance). Code System Preferred Concept Name. Chorismate mutase (substance). Concept Status. Published. ...
Chorismate Mutase - Preferred Concept UI. M0004343. Scope note. An isomerase that catalyzes the conversion of chorismic acid to ... Chorismate pyruvatemutase Previous Indexing:. Cyclohexanecarboxylic Acids (1969-1974). Isomerases (1969-1974). Vinyl Compounds ... Corismato Mutase Descriptor French: Chorismate mutase Entry term(s):. Chorismate Pyruvatemutase. Mutase, Chorismate. ...
Catalyzes the Claisen rearrangement of chorismate to prephenate (PubMed:2646272, PubMed:2187528, PubMed:10894726, PubMed:3 ... Chorismate mutase - Also known as CHMU_YEAST, ARO7, OSM2. ... Catalyzes the Claisen rearrangement of chorismate to prephenate ... Catalyzes the Claisen rearrangement of chorismate to prephenate (PubMed:2646272, PubMed:2187528, PubMed:10894726, PubMed: ...
Putative chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. The joint presence of this enzyme ... Chorismate mutase / prephenate dehydratase; Catalyzes the Claisen rearrangement of chorismate to prephenate and the ... Chorismate mutase / prephenate dehydratase; Catalyzes the Claisen rearrangement of chorismate to prephenate and the ... PchB also catalyzes the nonphysiological Claisen rearrangement of chorismate to prephenate in which the pyruvylenol tail is ...
chorismate mutase (2) * classical simulation (1) * code snippets blog blogger python fortran c cpp cplusplus c++ syntax ...
chorismate mutase (NCBI). 18, 403. PA3199. PA3199. hypothetical protein (NCBI). 18, 390. ...
Chorismate mutase (4) * Malate dehydrogenase, cytoplasmic (4) * Phosphoribosylformylglycinamidine synthase (4) * Aspartate- ... Chorismate synthase (4) * 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (4 ...
chorismate mutase / prephenate dehydrogenase. 1e-08. 60.8. NC_019977:253895:257189. 257189. 258490. 1302. Methanomethylovorans ...
... "bifunctional chorismate mutase/phospho-2-dehydro-3-deoxyheptonate aldolase [Ensembl]. DAHP synthetase I/KDSA, Chorismate mutase ... ","Probable chorismate synthase AroF (5-enolpyruvylshikimate-3-phosphate phospholyase) [Ensembl]. Chorismate synthase [ ... ","chorismate lyase [Ensembl].","protein_coding" "AGT26517","N559_4933","Klebsiella pneumoniae","DNA-directed RNA polymerase ... ","Probable hydroxylaminobenzene mutase Hab [Ensembl].","protein_coding" "CCP45915","prfB","Mycobacterium tuberculosis"," ...
Next, feedback-resistant chorismate mutase/prephenate dehydrogenase, was introduced to promote l-tyrosine synthesis. This ...
Recently, the change in entropy in the enzyme-catalyzed chorismate mutase reaction brought about uncertainty as a result of an ... Understanding the entropic effect in chorismate mutase reaction catalyzed by isochorismate-pyruvate lyase from Pseudomonas ...
... identical to the chorismate mutase domain of the P. stutzeri Aspartate fusion protein) may function predominantly in tyrosine ... As one chorismate mutase is fused to prephenate dehydratase (pheA; Gmet_0862 = GSU2608, 41% identical to the Pseudomonas ...
  • This enzyme in the enteric bacteria also possesses chorismate mutase ( EC 5.4.99.5 ) activity, and converts chorismate into prephenate. (qmul.ac.uk)
  • Next, feedback-resistant chorismate mutase/prephenate dehydrogenase, was introduced to promote l-tyrosine synthesis. (bvsalud.org)
  • 2022) , Identification of potent inhibitors against Chorismate synthase of Toxoplasma gondii using molecular dynamics simulations. (uohyd.ac.in)
  • Westfall CS, Xu A, Jez JM (2014) Structural evolution of differential amino acid effector regulation in plant chorismate mutases. (wustl.edu)
  • Chorismate mutase (CM, EC 5.4.99.5), encoded by ARO7, catalyzes the Claisen rearrangement of chorismate to prephenate in the biosynthesis of the amino acids tyrosine and phenylalanine. (uni-goettingen.de)
  • Structure of chorismate mutase-like domain of DAHPS from Bacillus subtilis complexed with novel inhibitor reveals conformational plasticity of active site. (purdue.edu)
  • The final model revealed that this protein has a Bacillus chorismate mutase-like fold and forms a homotrimer with a hydrophobic cavity in the center of the structure and ligand-binding clefts between two subunits. (semanticscholar.org)
  • They found that the artificial proteins had the same catalytic function as the natural chorismate mutase proteins. (scientificinquirer.com)
  • In this research we characterized two potential H. oryzae effector proteins, chorismate mutase (HoCM) and isochorismatase (HoICM), and inve. (mysciencework.com)
  • For this research, they studied the chorismate mutase family of metabolic enzymes, a type of protein that is important for life in many bacteria, fungi, and plants. (scientificinquirer.com)
  • In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. (bvsalud.org)
  • Two enzymes, chorismate mutase and isochorismatase, thought to be involved in the salicyclic acid pathway, were identified. (ilvo.be)
  • A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis. (nih.gov)
  • Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids. (umd.edu)
  • Utilizing hybrid potentials of quantum mechanics (GAMESS) and molecular mechanics (CHARMM), I investigate enzyme mechanism (e.g., aldose reductase, chorismate mutase and adenynyl cyclase). (nih.gov)
  • This graph shows the total number of publications written about "Methylmalonyl-CoA Mutase" by people in this website by year, and whether "Methylmalonyl-CoA Mutase" was a major or minor topic of these publications. (jefferson.edu)