Chorismate Mutase
Chorismic Acid
Prephenate Dehydratase
Prephenate Dehydrogenase
Methylmalonyl-CoA Mutase
Phosphoglycerate Mutase
Shikimic Acid
3-Deoxy-7-Phosphoheptulonate Synthase
Bisphosphoglycerate Mutase
Cyclohexenes
Phosphorus-Oxygen Lyases
Phenylalanine
Hydro-Lyases
Phenylpyruvic Acids
Isomerases
Allosteric Regulation
Aldehyde-Lyases
Intramolecular Transferases
Brevibacterium
Tryptophan
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
Tyrosine
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
ortho-Aminobenzoates
Transaminases
Catalysis
Periplasm
Phosphotransferases
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Amino Acid Sequence
Anthranilate Synthase
Oxidoreductases
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Models, Molecular
Lyases
Cloning, Molecular
Feedback
Amaryllidaceae Alkaloids
Glucosinolates
3-Isopropylmalate Dehydrogenase
Liliaceae
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.
Lycoris
Sulfate Adenylyltransferase
Arabidopsis
Reference Standards
Bronchoalveolar Lavage Fluid
Sensitivity and Specificity
Neisseria meningitidis
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.
Polymerase Chain Reaction
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.
Bronchoalveolar Lavage
Reproducibility of Results
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)
The emerging periplasm-localized subclass of AroQ chorismate mutases, by David H. Calhoun, Carol A. Bonner et al.
Chorismate mutase - Wikipedia
RCSB PDB
- 1COM: THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE...
AID 52148 - The compound was tested for inhibition of Bacillus subtilis chorismate mutase (BcCM) - PubChem
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Chorismate to PHB in Yeast?
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Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and...
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Replacement of two invariant serine residues in chorismate synthase provides evidence that a proton relay system is essential...
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Chorismate mutase
... is found at a branch point in the pathway. The enzyme channels the substrate, chorismate to the biosynthesis ... For example, the secondary structure of the chorismate mutase of yeast is very similar to that of E. coli. Chorimate mutase in ... The systematic name of this enzyme class is chorismate pyruvatemutase. Chorismate mutase, also known as hydroxyphenylpyruvate ... chorismate mutase (EC 5.4.99.5) is an enzyme that catalyzes the chemical reaction for the conversion of chorismate to ...
Prephenate dehydratase
Schmidt JC; Zalkin H (1969). "Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from ...
Prephenic acid
C10H10O6 Helmut Goerisch (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700-3705. doi: ... It is biosynthesized by a [3,3]-sigmatropic Claisen rearrangement of chorismate. Prephenic acid is an example of achiral ( ... "Thermodynamics of the Conversion of Chorismate to Prephenate: Experimental Results and Theoretical Predictions". J. Phys. Chem ...
Prephenate dehydrogenase
"InterPro." Bifunctional Chorismate Mutase/prephenate Dehydrogenase T-protein (IPR008244). InterPro, n.d. Web. 24 Apr. 2014. ... prephenate dehydrogenase is fused with the enzyme chorismate mutase. This fusion is not found in plants or animals. As of late ... and chorismate mutase---prephenate dehydrogenase. This enzyme participates in phenylalanine, tyrosine and tryptophan ...
Shikimate pathway
Prephenic acid is then synthesized by a Claisen rearrangement of chorismate by chorismate mutase. Prephenate is oxidatively ... Helmut Goerisch (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700-3705. 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 ...
Shikimic acid
Prephenic acid is then synthesized by a Claisen rearrangement of chorismate by chorismate mutase. Prephenate is oxidatively ... Goerisch, H. (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700-3705. doi:10.1021/ ... Then 5-enolpyruvylshikimate-3-phosphate is transformed into chorismate by a chorismate synthase. ... The pathway starts with two substrates, phosphoenol pyruvate and erythrose-4-phosphate and ends with chorismate, a substrate ...
Isomerase
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 ...
Enzyme kinetics
Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3 ... Such cases exist: for example, a mutase such as phosphoglucomutase catalyses the transfer of a phospho group from one position ... Enzymes with single-substrate mechanisms include isomerases such as triosephosphateisomerase or bisphosphoglycerate mutase, ...
William Lipscomb
Chorismate mutase (right) catalyzes (speeds up) the production of the amino acids phenylalanine and tyrosine. Fructose-1,6- ... "Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures". Structure. 5 (11): 1437- ...
Aspartate carbamoyltransferase
Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3 ...
Hydrogen-bond catalysis
For instance, the natural enzyme chorismate mutase, which catalyzes the Claisen rearrangement of chorismate, features many ... "New insight into the catalytic mechanism of chorismate mutases from structural studies". Chemistry & Biology. 2 (4): 195-203. ...
Rosavin
Chorismate mutase then converts chorismic acid to prephenate via a Claisen rearrangement (1,3-sigmatropic rearrangement). ...
Amino acid synthesis
This process is mediated by a phenylalanine (PheA) or tyrosine (TyrA) specific chorismate mutase-prephenate dehydrogenase. PheA ... trpE encodes the first subunit, which binds to chorismate and moves the amino group from the donor to chorismate. trpG encodes ... The rest of the enzymes in the common pathway (conversion of DAHP to chorismate) appear to be synthesized constitutively, ... Phenylalanine, tyrosine, and tryptophan, the aromatic amino acids, arise from chorismate. The first step, condensation of 3- ...
Isochorismate lyase
... is a structural homolog of the chorismate mutase enzyme in E. coli, and actually exhibits non-physiological ... Using the chorismate produced from that metabolic process, first the enzyme PchA will catalyze the reaction of chorismate into ... a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities". The Journal of ... chorismate mutase activity, albeit at a much lower efficiency. IPL also has several homologs found in other organisms, ...
Arogenate dehydratase
ADTs contain an N-terminal transit peptide, a PDT-like domain, and an ACT (Aspartokinase, chorismate mutase, TyrA) domain. ...
ACT domain
The ACT domain is named after three of the proteins that contain it: aspartate kinase, chorismate mutase and TyrA. The ...
Cyanidin
In the synthesis of L-phenylalanine, chorismate undergoes a Claisen rearrangement by a Chorismate mutase enzyme to form ...
Pravindra Kumar
"Structure of Chorismate Mutase-like Domain of DAHPS from Bacillus subtilis Complexed with Novel Inhibitor Reveals ... reported to have opportunities in the development of a new class of antibiotics as the compound clings to the chorismate mutase ...
Synthetic biology
One project demonstrated that an engineered version of Chorismate mutase still had catalytic activity when only 9 amino acids ...
Enol ether
The enzyme chorismate mutase catalyzes the Claisen rearrangement of the enol ether called chorismate to prephenate, an ...
Hydroxyphenylpyruvate synthase
... may refer to: Prephenate dehydrogenase, an enzyme Chorismate mutase, an enzyme This set index ...
Claisen rearrangement
The enzyme chorismate mutase (EC 5.4.99.5) catalyzes the Claisen rearrangement of chorismate to prephenate, an intermediate in ...
JS Chiao
... pathway of aromatic amino acids in Nocardia mediterranei 1994 Cloning vector system for Nocardia spp 1995 Chorismate mutase and ...
Hirschmanniella oryzae
... chorismate mutase (CM) and isochorismatase (ICM), thought to be interfering on the salicylic acid pathway and thereby altering ...
List of MeSH codes (D08)
2-acetolactate mutase MeSH D08.811.399.520.250 - chorismate mutase MeSH D08.811.399.520.250.500 - prephenate dehydratase MeSH ... phosphoglycerate mutase MeSH D08.811.399.894.200 - amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 - phosphoglucomutase MeSH D08.811.399.520.750.700 - ... D08.811.399.520.250.750 - prephenate dehydrogenase MeSH D08.811.399.520.625 - methylmalonyl-coa mutase MeSH D08.811.399.520.750 ...
List of EC numbers (EC 5)
2-acetolactate mutase EC 5.4.99.4: 2-methyleneglutarate mutase EC 5.4.99.5: chorismate mutase EC 5.4.99.6: Now EC 5.4.4.2, ... 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- ...
Isochorismate synthase
Other names for this enzyme include: Isochorismate mutase Menaquinone-specific isochorismate synthase MenF MenF is a gene that ... More specifically it is classified as an intramolecular transferase because it transfers the hydroxy group of chorismate ... Isochorismate synthase catalyzes the irreversible conversion of chorismate to isochorismate: Isochorismate synthase is most ... 5-dihydrochorismate analogues as inhibitors of the chorismate-utilising enzymes". Organic & Biomolecular Chemistry. 7 (11): ...
2014 Ju-Jitsu World Championships
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 Johnson
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 ...
Don't Say No
... 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. - IQUIBICEN...
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Frontiers | Totoro: Identifying Active Reactions During the Transient State for Metabolic Perturbations
... 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 ...
SCOPe 2.08: Structural Classification of Proteins - extended
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 ...
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ECOD: domain e6p5jN1
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 ...
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Find Research outputs - Manipal Academy of Higher Education, Manipal, India
Finding step cmutase for L-tyrosine biosynthesis in Phaeobacter inhibens BS107
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 ...
4.2.1.51: prephenate dehydratase - BRENDA Enzyme Database
Code System Concept
DeCS
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. ...
Gene P32178 | Protein ARO7 - Overview | canSAR Black
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: ...
DR97 5946 protein (Pseudomonas aeruginosa) - STRING interaction network
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 ...
Proteins and Wave Functions: July 2016
Network Portal - Gene PA0590
Model Search | BioModels
Pre GI: BLASTP Hits
"sequence id","alias","species","description",...
... "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"," ...
Pesquisa | Biblioteca Virtual em Saúde - BRASIL
学术成果 | 晶泰科技
Rao, Niny
99.51
- This enzyme in the enteric bacteria also possesses chorismate mutase ( EC 5.4.99.5 ) activity, and converts chorismate into prephenate. (qmul.ac.uk)
Prephenate dehydrogenase1
- Next, feedback-resistant chorismate mutase/prephenate dehydrogenase, was introduced to promote l-tyrosine synthesis. (bvsalud.org)
Potent inhibitors1
- 2022) , Identification of potent inhibitors against Chorismate synthase of Toxoplasma gondii using molecular dynamics simulations. (uohyd.ac.in)
Effector1
- Westfall CS, Xu A, Jez JM (2014) Structural evolution of differential amino acid effector regulation in plant chorismate mutases. (wustl.edu)
Prephenate1
- 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)
Bacillus2
- 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)
Proteins2
- 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)
PROTEIN1
- 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)
Biosynthesis1
- In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. (bvsalud.org)
Isochorismatase1
- Two enzymes, chorismate mutase and isochorismatase, thought to be involved in the salicyclic acid pathway, were identified. (ilvo.be)
Mycobacterium2
- 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)
Enzyme1
- 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)
Year1
- 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)