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.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.
A species of gram-positive bacteria that is a common soil and water saprophyte.
Databases devoted to knowledge about specific chemicals.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The meaning ascribed to the BASE SEQUENCE with respect to how it is translated into AMINO ACID SEQUENCE. The start, stop, and order of amino acids of a protein is specified by consecutive triplets of nucleotides called codons (CODON).
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

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 ...
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 ...
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.. ...
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.. ...
1I7S: The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
Hacienda Lopez De Haro Reserva Bodega Classica 2005 reviews, ratings, wine pairings, LCBO, BCLDB, SAQ store stock, price, wine searcher, food pairing Red Wine
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 ...
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 ...
HARO PARQUET 4000 Plank 1-strip Maxim 4V Oak Sauvage brushed naturaLin plus Tongue & Groove plus is a floor from HARO®s parquet range.
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 ...
parkettmanufaktur by HARO PARQUET 4000 Carré Oak Antique Brown Selectiv oleovera Tongue and groove is a floor from HAROs parquet range.
Its always a good day when you can get to see some new Mike Dominguez footage! Im really excited with what Haro has been doing lately and now their Legends team is growing. This video runs thru a day with Dennis McCoy and Mike D. and goes over the release of 1984 Haro Sport Mike Dominguez tribute bike. More backyard vert ramps please!. ...
Latest The Tyra Banks Show review: Love the show, Tyra you are so real, to go without makeup on TV. Please include the mature woman in ...
ID F2PQI4_TRIEC Unreviewed; 323 AA. AC F2PQI4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 11-DEC-2019, entry version 29. DE SubName: Full=Chorismate mutase/prephenate dehydratase {ECO:0000313,EMBL:EGE04152.1}; GN ORFNames=TEQG_03185 {ECO:0000313,EMBL:EGE04152.1}; OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm OS fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton. OX NCBI_TaxID=559882 {ECO:0000313,Proteomes:UP000009169}; RN [1] {ECO:0000313,Proteomes:UP000009169} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313,Proteomes:UP000009169}; RX PubMed=22951933; DOI=10.1128/mBio.00259-12; RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti ...
Phenylalanine (abbreviated as Phe or F) is an alpha-amino acid. The L-isomer is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. It is classified as a nonpolar, aromatic amino acid, because of the hydrophobic nature of the benzyl side chain. L-Phenylalanine (LPA) is an electrically neutral amino acid. It is used in the manufacture of food and drink products and sold as a nutritional supplement for its reputed analgesic and antidepressant effects. Biosynthesis of phenylalanine, tyrosine, and tryptophan proceeds via a common pathway to chorismate, at which point the pathway branches. One branch proceeds to phenylalanine and tyrosine, and the other to tryptophan. The phenylalanine and tyrosine branch has one reaction in common, rearrangement of chorismate to prephenate, at which point, the pathway branches again to either phenylalanine or tyrosine. S. cerevisiae, similar to E. coli, synthesizes phenylalanine and tyrosine via the intermediate 4-hydroxyphenylpyruvate ...
Description: The chemical reactions and pathways resulting in the formation of phenylalanine and tyrosine from other compounds, including chorismate, via the intermediate prephenate.. ...
Ubiquinone (UQ), also called coenzyme Q, and plastoquinone (PQ) are electron carriers in oxidative phosphorylation and photosynthesis, respectively. The quinoid nucleus of ubiquinone is derived from the shikimate pathway; 4-hydroxybenzoate is directly formed from chorismate in bacteria, while it can be formed from either chorismate or tyrosine in yeast. The following biosynthesis of terpenoid moiety involves reactions of prenylation, decarboxylation, and three hydroxylations alternating with three methylations. The order of these reactions are somewhat different between bacteria and yeast. Phylloquinone (vitamin K1), menaquinone (vitamin K2), and tocopherol (vitamin E) are fat-soluble vitamins. Phylloquinone is a compound present in all photosynthetic plants serving as a cofactor for photosystem I-mediated electron transport. Menaquinone is an obligatory component of the electron-transfer pathway in bacteria ...
Haro company is one of the top hair manufacturers & exporters of Vietnam. Ombre color hair is one of our product with top quality. 100% real human hair.
Tyra Banks & Rosario Dawson Celebrate Valentines Day Tyra Banks is celebrating Valentines Day on The Tyra Show this Friday (February 12) with special guests Rosario Dawson and author Eve Ensler! The show will…
Access to contact information is restricted to users who have purchased the conferences Online Proceedings, or received access to the proceedings as part of the conference Registration.. Please click the links below if youd like to purchase Online Proceedings for any of the related conferences: ...
Are you true fan of Tyra Banks?! Get your facts straight about the celebrity, find out why Tyra Banks Weight Gain happened in a first place!
Phone toll free (877) 477-8591, Promo Code - HBC4942 to get the best rate for Tyra Summit A2a Condo in Breckenridge, CO - Swimming Pool - Indoor Pool
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 ...
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. ...
In the synthesis of L-phenylalanine, chorismate undergoes a Claisen rearrangement by a Chorismate mutase enzyme to form ...
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 ...
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 ... Phenylalanine, tyrosine, and tryptophan, the aromatic amino acids, arise from chorismate. The first step, condensation of 3- ... The rest of the enzymes in the common pathway (conversion of DAHP to chorismate) appear to be synthesized constitutively, ...
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 ...
Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiol. Mol. Biol. Rev. 65 (3): 404-21, table ...
1995 Chorismate mutase and 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of the methylotrophic actinomycete ...
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 ...
The compound was tested for inhibition of Bacillus subtilis chorismate mutase (BcCM). ...
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 ...
... and in chorismate mutase. Only the rearrangement of chorismate in the enzyme shows a negative differential barrier when ... 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 to rigidification and ring formation are operative, ... and the biologically relevant substrate chorismate are investigated in the gas phase, water, ...
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 ...
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, ...
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 ...
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- ...
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. ...
The shikimate pathway enzymes DAHP synthase (CgDS, Cg2391) and chorismate mutase (CgCM, Cgl0853) play a key role in the ... Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation ...
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 ...
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 ...
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 ...
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 ...
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 ...
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. ...
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 ...
CHORISMATE MUTASE (ENZYMES); ENZYMATIC REACTIONS + ENZYMATIC REACTION MECHANISM + ENZYMATIC CATALYSIS (BIOCHEMISTRY); ... BACILLUS SUBTILIS (MIKROBIOLOGIE); CHORISMAT-MUTASE (ENZYME); ENZYMREAKTION + ENZYMATISCHER REAKTIONSMECHANISMUS + ENZYMATISCHE ...
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, ...
... chorismate mutase; CS, chorismate synthase; PAL, phenylalanine ammonia lyase; C4H, cinnamate-4-hydroxylase; C3H, p-coumarate-3- ...
Chorismate mutase. EMS-25. R. CACTGAGCGCATGTCTTTTG. EMS-26. F. CGCTCTAGTTTCACATAAGCAGTC. 54. (TCTT)3. 0.7855. Serine/threonine- ...
chorismate mutases. * prephenate dehydrogenases (TyrA). *prephenate dehydratases. *homoserine dehydrogenases. *malate ...
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 ...
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, ...
Chorismate mutase. No expression. ++. ++. Burkholderia pseudomallei. ZP_04891863.1. 267-404. Hemagglutinin-family protein. ...
Enzyme catalysis from linear-scaling DFT: application to chorismate mutase. Greg Lever (TCM). ...
... putative chorismate mutase; F23O10.6; F23O10.7; F23O10.8; F23O10.9; F23O10.10; F23O10.11; F23O10.12; F23O10.13; tRNA-Ala; ...
Chorismate mutase (CM2) Aromatic amino acid biosynthesis 19* AY105062 0.43 Microsomal signal peptidase (SPC25) Peptidase ...
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, ...
PDB reference: putative chorismate mutase, 1xho, r1xhosf Read article Acta Cryst. (2005). D61, 967-975. doi: 10.1107/ ...
... and Hg-GLAND16 is a putative chorismate mutase (CM), and blastp searches of the non-redundant database resulted in highest ... Two chorismate mutase genes from the root-knot nematode Meloidogyne incognita. Mol Plant Pathol. 2005;6:23-30.View Article ... Meloidogyne javanica chorismate mutase 1 alters plant cell development. Mol Plant Microbe In. 2003;16:123-31.View ArticleGoogle ... Characterization of a chorismate mutase from the potato cyst nematode Globodera pallida. Mol Plant Pathol. 2003;4:43-50.View ...
  • The systematic name of this enzyme class is chorismate pyruvatemutase . (wikipedia.org)
  • The enzyme channels the substrate, chorismate to the biosynthesis of tyrosine and phenylalanine and away from tryptophan . (wikipedia.org)
  • 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. (unibas.ch)
  • 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)
  • [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)
  • 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)
  • 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 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)
  • Chorismate mutase is found at a branch point in the pathway. (wikipedia.org)
  • 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 to rigidification and ring formation are operative, which lead to changes in the rate. (unibas.ch)
  • 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. (unibas.ch)
  • For example, the secondary structure of the chorismate mutase of yeast is very similar to that of E. coli . (wikipedia.org)
  • 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)
  • Genes, reactions, and enzymes of the common aromatic pathway culminating in the synthesis of chorismate, the precursor of phenylalanine, tyrosine, and tryptophan. (asmscience.org)
  • The compounds found active in in vitro study were assessed for their in vivo antitubercular activity in mice models and for their inhibitory action on vital mycobacterial enzymes viz, isocitrate lyase, pantothenate synthetase and chorismate mutase. (biomedcentral.com)
  • Most chorismate mutases in this family look similar to that of Escherichia coli . (wikipedia.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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • Chorismate mutase acts at the first branchpoint of aromatic amino acid biosynthesis and catalyzes the conversion of chorismate to prephenate. (pnas.org)
  • 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)
  • 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)
  • 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)
  • [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)
  • Genetic and biochemical identification of the chorismate mutase from Corynebacterium glutamicum. (semanticscholar.org)
  • Figure 1 illustrates the biochemical relationship of these specificities to divergent transformations beginning with chorismate (CHA) utilization and converging on TYR formation. (biomedcentral.com)
  • Composite of alternative biochemical routes from chorismate (CHA) to L-tyrosine (TYR) in nature. (biomedcentral.com)
  • 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)
  • and Mycobacterium tuberculosis that convert chorismate to salicylate without requirement of an additional lyase such as PchB in P. aeruginosa. (ku.edu)
  • 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)
  • 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)
  • 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)
  • Westfall CS, Xu A, Jez JM (2014) Structural evolution of differential amino acid effector regulation in plant chorismate mutases. (wustl.edu)
  • 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)
  • Under this agreement, Primetime will collaborate with Dr. Prasad Reddy who is a recognized expert in chorismate mutase enzymology. (biospace.com)
  • The structures for the activated and inhibited state of Saccharomyces cerevisiae chorismate mutase also have been described ( 19 , 20 ). (pnas.org)
  • The presence of chorismate mutase increases the rate of the reaction a million fold. (wikipedia.org)
  • 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)
  • Together, the groups will identify and characterize novel inhibitors of chorismate mutase. (biospace.com)
  • The oxabicyclo[2.2.2]octane system was proposed to be a mimic of chorismate (and is similar to transition-state analogues of chorismate mutase inhibitors). (docme.ru)
  • 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)
  • Transition state analogue in chorismate mutase active site of S. cerevisiae . (wikipedia.org)
  • The phenolate type siderophore, such as pyochelin in Pseudomonas aeruginosa, uses salicylate derived from chorismate as a precursor. (ku.edu)
  • 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)
  • The researchers then sequenced those chorismate mutase genes, compared the sequences, and identified unique regions in each sequence. (innovations-report.com)
  • 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)
  • 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)
  • Here the intermediates shown to intervene between chorismate and pristinamycin or chloramphenicol are p -aminochorismate (ADC), p -aminoprephenate (ADP), p -aminophenylpyruvate (APP), and p -aminophenylalanine (APA). (biomedcentral.com)
  • 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)