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.
Cyclohexanecarboxylic acids are organic compounds consisting of a cyclohexane ring substituted with a carboxylic acid group, typically represented by the structural formula C6H11COOH.
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.
Tetroses are uncommon sugars (monosaccharides) with four carbon atoms, having an aldehyde functional group at the first carbon atom, and forming ring structures in their cyclic forms, primarily found in complex carbohydrates and certain natural products.
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.
Vinyl compounds, in the context of medical materials, refer to synthetic polymers made from vinyl chloride or vinyl acetate monomers, which are used in the production of various medical devices and supplies such as blood bags, intravenous (IV) bags, tubing, and gloves due to their flexibility, transparency, and resistance to chemicals and heat.
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.
Cobamides are a class of compounds that function as cofactors in various enzymatic reactions, containing a corrin ring similar to vitamin B12, but with different substituents on the benzimidazole moiety, and can be found in certain bacteria and archaea.
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.

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)

Chorismate mutase is an important enzyme in the biosynthetic pathway of aromatic amino acids in bacteria, fungi, and plants. This enzyme catalyzes the conversion of chorismate to prephenate, which is a key step in the synthesis of phenylalanine, tyrosine, and tryptophan.

The reaction catalyzed by chorismate mutase is as follows:

chorismate → prephenate

Inhibition of this enzyme has been explored as a potential target for the development of antibiotics and herbicides, as interrupting the synthesis of aromatic amino acids can be lethal to bacteria and plants. In humans, the equivalent reaction is catalyzed by a different set of enzymes, so chorismate mutase inhibitors are not expected to have toxic effects on human cells.

I'm sorry for any confusion, but "Chorismic Acid" is not a recognized term in medical or clinical sciences. It appears that "chorismic acid" is a concept from biochemistry, specifically in the field of amino acid biosynthesis. It is an intermediate compound in the shikimate pathway, which is present in plants and microorganisms but not in animals.

Chorismic acid is a key branchpoint metabolite that leads to the formation of various aromatic amino acids and other important compounds. However, it's not typically mentioned in medical contexts or definitions. If you're looking for information related to its biochemical role, I would be happy to help with that!

Prephenate Dehydratase is not a medical term per se, but rather a biochemical term. It's a type of enzyme involved in the metabolic pathway known as the shikimate pathway, which is responsible for the biosynthesis of aromatic amino acids in bacteria, fungi, and plants.

Prephenate Dehydratase specifically catalyzes the conversion of prephenate to phenylpyruvate and water in this pathway. This reaction is a key step in the synthesis of phenylalanine, one of the aromatic amino acids.

In a medical context, understanding the function of Prephenate Dehydratase may be relevant in fields such as microbiology or plant biochemistry, but it does not have direct clinical significance for human health diagnoses or treatments.

Prephenate Dehydrogenase (PDH) is an enzyme involved in the metabolic pathway known as the shikimate pathway, which is responsible for the biosynthesis of aromatic amino acids in plants, bacteria, and fungi. Specifically, PDH catalyzes the conversion of prephenate to 4-hydroxybenzoate, an important intermediate in the synthesis of various aromatic compounds.

The reaction catalyzed by Prephenate Dehydrogenase is a decarboxylative oxidation and involves the removal of two hydrogen atoms from the prephenate molecule, resulting in the formation of 4-hydroxybenzoate, carbon dioxide, and NADPH. The enzyme plays a crucial role in the biosynthesis of various natural products, including pigments, antibiotics, and other secondary metabolites.

There are several isoforms of Prephenate Dehydrogenase that have been identified, each with distinct properties and functions. The enzyme has been studied extensively as a potential target for the development of herbicides and antibiotics, due to its essential role in the metabolism of plants and bacteria.

Methylmalonyl-CoA mutase is a mitochondrial enzyme that plays a crucial role in the metabolism of certain amino acids and fatty acids. Specifically, it catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, which is an important step in the catabolic pathways of valine, isoleucine, threonine, methionine, odd-chain fatty acids, and cholesterol.

The enzyme requires a cofactor called adenosylcobalamin (vitamin B12) for its activity. In the absence of this cofactor or due to mutations in the gene encoding the enzyme, methylmalonyl-CoA mutase deficiency can occur, leading to the accumulation of methylmalonic acid and other toxic metabolites, which can cause a range of symptoms including vomiting, dehydration, lethargy, hypotonia, developmental delay, and metabolic acidosis. This condition is typically inherited in an autosomal recessive manner and can be diagnosed through biochemical tests and genetic analysis.

Phosphoglycerate Mutase (PGM) is an enzyme that plays a crucial role in the glycolytic pathway, which is a metabolic process that converts glucose into pyruvate, producing ATP and NADH as energy currency for the cell.

The enzyme catalyzes the interconversion of 3-phosphoglycerate (3-PG) and 2-phosphoglycerate (2-PG), which is the ninth step in glycolysis. Specifically, PGM transfers a phosphate group from the third carbon atom to the second carbon atom of 3-PG, resulting in the formation of 2-PG and inorganic phosphate.

There are two types of Phosphoglycerate Mutase isoenzymes in humans, including:

1. Phosphoglycerate Mutase 1 (PGAM1): This is a cytosolic enzyme that is widely expressed in various tissues, including skeletal muscle, heart, brain, and liver.
2. Phosphoglycerate Mutase 2 (PGAM2): This is a muscle-specific isoenzyme that is primarily found in cardiac and skeletal muscles.

Mutations in the PGAM1 gene have been associated with hemolytic anemia, neurodevelopmental disorders, and other metabolic abnormalities, while mutations in the PGAM2 gene have been linked to myopathies and other muscle-related disorders.

Shikimic acid is not a medical term per se, but a chemical compound with significance in biochemistry and pharmacology. It is a cyclohexene derivative that plays a crucial role as an intermediate in the biosynthesis of aromatic amino acids (phenylalanine, tyrosine, and tryptophan) in plants and microorganisms.

Medically, shikimic acid is relevant due to its use as a precursor in the synthesis of antiviral drugs such as oseltamivir (Tamiflu), which is used for treating and preventing influenza A and B infections. It's important to note that shikimic acid itself does not have any direct medical applications, but its derivatives can be essential components in pharmaceutical products.

3-Deoxy-7-phosphoheptulonate synthase (DAH7PS) is an enzyme that catalyzes the first step in the synthesis of the aromatic amino acids, phenylalanine, tyrosine, and tryptophan. The reaction it catalyzes is the condensation of erythrose-4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-arabino-hept-2-ulose-7-phosphate (DAHP), also known as 3-deoxy-7-phosphoheptulonate.

The reaction catalyzed by DAH7PS is the first step in the shikimate pathway, which is a seven-step metabolic route used by bacteria, fungi, algae, parasites, and plants to produce aromatic amino acids and other important compounds. Mammals do not have this pathway, so enzymes of the shikimate pathway are potential targets for the development of antibiotics and herbicides.

DAH7PS is a regulatory enzyme in the shikimate pathway, and its activity is feedback inhibited by the aromatic amino acids phenylalanine and tyrosine. This helps to regulate the flow of carbon into the aromatic amino acid biosynthetic pathway based on the needs of the cell.

Bisphosphoglycerate mutase (BPGM) is an enzyme that plays a crucial role in the regulation of oxygen transport in red blood cells. The main function of BPGM is to convert 1,3-bisphosphoglycerate (1,3-BPG) into 2,3-bisphosphoglycerate (2,3-BPG), also known as 2,3-diphosphoglycerate (2,3-DPG).

2,3-BPG is essential for modulating the affinity of hemoglobin for oxygen. By increasing the concentration of 2,3-BPG in red blood cells, BPGM reduces the ability of hemoglobin to bind to oxygen, allowing more oxygen to be released from hemoglobin and made available to tissues, particularly under low-oxygen conditions. This is especially important for individuals living at high altitudes or those with chronic lung diseases who may have impaired oxygen transport.

Defects in the BPGM gene can lead to a rare disorder called 2,3-bisphosphoglycerate deficiency, which results in an increased affinity of hemoglobin for oxygen and reduced oxygen delivery to tissues. This condition is characterized by symptoms such as shortness of breath, fatigue, and headaches, particularly during exercise or at high altitudes.

Cyclohexenes are organic compounds that consist of a six-carbon ring (cyclohexane) with one double bond. The general chemical formula for cyclohexene is C6H10. The double bond can introduce various chemical properties and reactions to the compound, such as electrophilic addition reactions.

Cyclohexenes are used in the synthesis of other organic compounds, including pharmaceuticals, agrochemicals, and materials. Some cyclohexene derivatives also occur naturally, for example, in essential oils and certain plant extracts. However, it is important to note that pure cyclohexene has a mild odor and is considered a hazardous substance, with potential health effects such as skin and eye irritation, respiratory issues, and potential long-term effects upon repeated exposure.

Cyclohexanecarboxylic acids are a type of organic compound that consists of a cyclohexane ring, which is a six-carbon saturated hydrocarbon, substituted with a carboxylic acid group (-COOH). This group contains a carbon atom double bonded to an oxygen atom and single bonded to a hydroxyl group (-OH).

The cyclohexane ring can be in various forms, including the chair, boat, or twist-boat conformations, depending on the orientation of its constituent atoms. The carboxylic acid group can ionize to form a carboxylate anion, which is negatively charged and has a deprotonated hydroxyl group.

Cyclohexanecarboxylic acids have various applications in industry and research, including as intermediates in the synthesis of other chemicals, solvents, and pharmaceuticals. They can also be found naturally in some plants and microorganisms.

Phosphorus-Oxygen Lyases are a class of enzymes that catalyze the breakdown of a substrate containing a phosphorus-oxygen bond, releasing a phosphate group and forming a new double bond in the process. This reaction is typically represented by the general formula:

Substrate-P-O + A acceptor ------> Substrate-O=A + P\_i

where "Substrate-P-O" represents the phosphorus-oxygen bond in the substrate, "A acceptor" is the molecule that accepts the phosphate group, and "P\_i" denotes inorganic phosphate. These enzymes play important roles in various biological processes, such as signal transduction, energy metabolism, and biosynthesis.

Examples of Phosphorus-Oxygen Lyases include:

1. Phospholipase D - catalyzes the hydrolysis of phosphatidylcholine to produce phosphatidic acid and choline.
2. ATP sulfurylase - catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and sulfate, which is an important intermediate in the biosynthesis of sulfur-containing amino acids.
3. Inositol polyphosphate 1-phosphatase - catalyzes the dephosphorylation of inositol polyphosphates, which are involved in intracellular signaling pathways.
4. UDP-glucose pyrophosphorylase - catalyzes the reversible conversion of UDP-glucose and pyrophosphate to glucose-1-phosphate and UTP, playing a crucial role in carbohydrate metabolism.

It is important to note that Phosphorus-Oxygen Lyases are distinct from Phosphoric Monoester Hydrolases, which also catalyze the hydrolysis of phosphorus-oxygen bonds but do not form new double bonds in the process.

Phenylalanine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through diet or supplementation. It's one of the building blocks of proteins and is necessary for the production of various molecules in the body, such as neurotransmitters (chemical messengers in the brain).

Phenylalanine has two forms: L-phenylalanine and D-phenylalanine. L-phenylalanine is the form found in proteins and is used by the body for protein synthesis, while D-phenylalanine has limited use in humans and is not involved in protein synthesis.

Individuals with a rare genetic disorder called phenylketonuria (PKU) must follow a low-phenylalanine diet or take special medical foods because they are unable to metabolize phenylalanine properly, leading to its buildup in the body and potential neurological damage.

I'm sorry for any confusion, but "Hydro-Lyases" is not a recognized medical term or category in biochemistry. It seems like there might be a misunderstanding or a typo in the term.

In biochemistry, "lyases" are enzymes that catalyze the removal of groups from substrates by means other than hydrolysis or oxidation, often forming a double bond or a ring-forming reaction. They are classified and named based on the type of bond they break.

If you meant to ask about a specific enzyme or reaction, could you please provide more context or clarify the term? I'd be happy to help further with accurate information.

Phenylpyruvic acid is not a medical condition, but rather a chemical compound that is produced in the body. It is a byproduct of phenylalanine metabolism, an essential amino acid that cannot be synthesized by the human body and must be obtained through dietary sources such as proteins.

In some rare genetic disorders, such as phenylketonuria (PKU), the body is unable to properly metabolize phenylalanine due to a deficiency or malfunction of the enzyme phenylalanine hydroxylase. As a result, phenylpyruvic acid and other toxic byproducts accumulate in the body, leading to various health problems such as intellectual disability, seizures, and behavioral issues.

Therefore, the medical relevance of phenylpyruvic acid lies in its association with certain metabolic disorders, particularly PKU, and its potential use as a diagnostic marker for these conditions.

Isomerases are a class of enzymes that catalyze the interconversion of isomers of a single molecule. They do this by rearranging atoms within a molecule to form a new structural arrangement or isomer. Isomerases can act on various types of chemical bonds, including carbon-carbon and carbon-oxygen bonds.

There are several subclasses of isomerases, including:

1. Racemases and epimerases: These enzymes interconvert stereoisomers, which are molecules that have the same molecular formula but different spatial arrangements of their atoms in three-dimensional space.
2. Cis-trans isomerases: These enzymes interconvert cis and trans isomers, which differ in the arrangement of groups on opposite sides of a double bond.
3. Intramolecular oxidoreductases: These enzymes catalyze the transfer of electrons within a single molecule, resulting in the formation of different isomers.
4. Mutases: These enzymes catalyze the transfer of functional groups within a molecule, resulting in the formation of different isomers.
5. Tautomeres: These enzymes catalyze the interconversion of tautomers, which are isomeric forms of a molecule that differ in the location of a movable hydrogen atom and a double bond.

Isomerases play important roles in various biological processes, including metabolism, signaling, and regulation.

Aromatic amino acids are a specific type of amino acids that contain an aromatic ring in their side chain. The three aromatic amino acids are phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp). These amino acids play important roles in various biological processes, including protein structure and function, neurotransmission, and enzyme catalysis.

The aromatic ring in these amino acids is composed of a planar six-membered carbon ring that contains alternating double bonds. This structure gives the side chains unique chemical properties, such as their ability to absorb ultraviolet light and participate in stacking interactions with other aromatic residues. These interactions can contribute to the stability and function of proteins and other biological molecules.

It's worth noting that while most amino acids are classified as either "hydrophobic" or "hydrophilic," depending on their chemical properties, aromatic amino acids exhibit characteristics of both groups. They can form hydrogen bonds with polar residues and also engage in hydrophobic interactions with nonpolar residues, making them versatile building blocks for protein structure and function.

Allosteric regulation is a process that describes the way in which the binding of a molecule (known as a ligand) to an enzyme or protein at one site affects the ability of another molecule to bind to a different site on the same enzyme or protein. This interaction can either enhance (positive allosteric regulation) or inhibit (negative allosteric regulation) the activity of the enzyme or protein, depending on the nature of the ligand and its effect on the shape and/or conformation of the enzyme or protein.

In an allosteric regulatory system, the binding of the first molecule to the enzyme or protein causes a conformational change in the protein structure that alters the affinity of the second site for its ligand. This can result in changes in the activity of the enzyme or protein, allowing for fine-tuning of biochemical pathways and regulatory processes within cells.

Allosteric regulation is a fundamental mechanism in many biological systems, including metabolic pathways, signal transduction cascades, and gene expression networks. Understanding allosteric regulation can provide valuable insights into the mechanisms underlying various physiological and pathological processes, and can inform the development of novel therapeutic strategies for the treatment of disease.

Aldehyde-lyases are a class of enzymes that catalyze the breakdown or synthesis of molecules involving an aldehyde group through a reaction known as lyase cleavage. This type of reaction results in the removal of a molecule, typically water or carbon dioxide, from the substrate.

In the case of aldehyde-lyases, these enzymes specifically catalyze reactions that involve the conversion of an aldehyde into a carboxylic acid or vice versa. These enzymes are important in various metabolic pathways and play a crucial role in the biosynthesis and degradation of several biomolecules, including carbohydrates, amino acids, and lipids.

The systematic name for this class of enzymes is "ald(e)hyde-lyases." They are classified under EC number 4.3.1 in the Enzyme Commission (EC) system.

Intramolecular transferases are a specific class of enzymes that catalyze the transfer of a functional group from one part of a molecule to another within the same molecule. These enzymes play a crucial role in various biochemical reactions, including the modification of complex carbohydrates, lipids, and nucleic acids. By facilitating intramolecular transfers, these enzymes help regulate cellular processes, signaling pathways, and metabolic functions.

The systematic name for this class of enzymes is: [donor group]-transferring intramolecular transferases. The classification system developed by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) categorizes them under EC 2.5. This category includes enzymes that transfer alkyl or aryl groups, other than methyl groups; methyl groups; hydroxylyl groups, including glycosyl groups; and various other specific functional groups.

Examples of intramolecular transferases include:

1. Protein kinases (EC 2.7.11): Enzymes that catalyze the transfer of a phosphate group from ATP to a specific amino acid residue within a protein, thereby regulating protein function and cellular signaling pathways.
2. Glycosyltransferases (EC 2.4): Enzymes that facilitate the transfer of glycosyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, playing a role in the biosynthesis and modification of complex carbohydrates.
3. Methyltransferases (EC 2.1): Enzymes that transfer methyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, contributing to the regulation of gene expression and other cellular processes.

Understanding the function and regulation of intramolecular transferases is essential for elucidating their roles in various biological processes and developing targeted therapeutic strategies for diseases associated with dysregulation of these enzymes.

Tetroses are a type of monosaccharides, which are simple sugars that cannot be broken down into simpler units by hydrolysis. Tetroses have four carbon atoms and are aldotetroses, meaning they contain an aldehyde functional group at the first carbon atom.

There are two naturally occurring tetroses: erythrose and threose. Erythrose has its hydroxyl groups on the second and fourth carbon atoms, while threose has its hydroxyl groups on the second and third carbon atoms. Tetroses can participate in various chemical reactions, including forming glycosidic bonds with other monosaccharides to create disaccharides or polysaccharides. However, tetroses are not as common as other monosaccharides, such as pentoses and hexoses.

"Streptomyces aureofaciens" is a species of aerobic, gram-positive bacteria belonging to the family Streptomycetaceae. These bacteria are known for their ability to produce a variety of bioactive secondary metabolites, including antibiotics and enzymes. "Streptomyces aureofaciens" is particularly known for producing the antibiotic undecylenic acid, which has antifungal properties. The bacteria are commonly found in soil and aquatic environments.

It's important to note that while I strive to provide accurate and up-to-date information, this definition may not be fully comprehensive or suitable for all purposes. For a more detailed and professional understanding, it is recommended to consult authoritative medical and scientific resources or speak with a healthcare provider or scientist in the field.

Brevibacterium is a genus of Gram-positive, rod-shaped bacteria that are commonly found in nature, particularly in soil, water, and various types of decaying organic matter. Some species of Brevibacterium can also be found on the skin of animals and humans, where they play a role in the production of body odor.

Brevibacterium species are known for their ability to produce a variety of enzymes that allow them to break down complex organic compounds into simpler molecules. This makes them useful in a number of industrial applications, such as the production of cheese and other fermented foods, as well as in the bioremediation of contaminated environments.

In medical contexts, Brevibacterium species are rarely associated with human disease. However, there have been occasional reports of infections caused by these bacteria, particularly in individuals with weakened immune systems or who have undergone surgical procedures. These infections can include bacteremia (bloodstream infections), endocarditis (inflammation of the heart valves), and soft tissue infections. Treatment typically involves the use of antibiotics that are effective against Gram-positive bacteria, such as vancomycin or teicoplanin.

Tryptophan is an essential amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C11H12N2O2. Tryptophan plays a crucial role in various biological processes as it serves as a precursor to several important molecules, including serotonin, melatonin, and niacin (vitamin B3). Serotonin is a neurotransmitter involved in mood regulation, appetite control, and sleep-wake cycles, while melatonin is a hormone that regulates sleep-wake patterns. Niacin is essential for energy production and DNA repair.

Foods rich in tryptophan include turkey, chicken, fish, eggs, cheese, milk, nuts, seeds, and whole grains. In some cases, tryptophan supplementation may be recommended to help manage conditions related to serotonin imbalances, such as depression or insomnia, but this should only be done under the guidance of a healthcare professional due to potential side effects and interactions with other medications.

Tyrosine is an non-essential amino acid, which means that it can be synthesized by the human body from another amino acid called phenylalanine. Its name is derived from the Greek word "tyros," which means cheese, as it was first isolated from casein, a protein found in cheese.

Tyrosine plays a crucial role in the production of several important substances in the body, including neurotransmitters such as dopamine, norepinephrine, and epinephrine, which are involved in various physiological processes, including mood regulation, stress response, and cognitive functions. It also serves as a precursor to melanin, the pigment responsible for skin, hair, and eye color.

In addition, tyrosine is involved in the structure of proteins and is essential for normal growth and development. Some individuals may require tyrosine supplementation if they have a genetic disorder that affects tyrosine metabolism or if they are phenylketonurics (PKU), who cannot metabolize phenylalanine, which can lead to elevated tyrosine levels in the blood. However, it is important to consult with a healthcare professional before starting any supplementation regimen.

"Vinyl compounds" is not a term used in medical definitions. It is a term used in chemistry and materials science to refer to a group of chemicals that contain carbon-based molecules with a vinyl group, which is a functional group consisting of a double bond between two carbon atoms, with one of the carbons also being bonded to a hydrogen atom (-CH2=CH-).

Vinyl compounds are used in various industrial and consumer products, including plastics, resins, adhesives, and coatings. Some vinyl compounds, such as polyvinyl chloride (PVC), have been used in medical devices and supplies, such as intravenous (IV) bags, tubing, and blood vessel catheters. However, the use of PVC and other vinyl compounds in medical applications has raised concerns about potential health risks due to the release of toxic chemicals, such as phthalates and dioxins, during manufacturing, use, and disposal. Therefore, alternative materials are being developed and used in medical devices and supplies.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Ortho-Aminobenzoates are chemical compounds that contain a benzene ring substituted with an amino group in the ortho position and an ester group in the form of a benzoate. They are often used as pharmaceutical intermediates, plastic additives, and UV stabilizers. In medical contexts, one specific ortho-aminobenzoate, para-aminosalicylic acid (PABA), is an antibiotic used in the treatment of tuberculosis. However, it's important to note that "ortho-aminobenzoates" in general do not have a specific medical definition and can refer to any compound with this particular substitution pattern on a benzene ring.

Cobamides are a class of compounds that are structurally related to vitamin B12 (cobalamin). They consist of a corrin ring, which is a large heterocyclic ring made up of four pyrrole rings, and a cobalt ion in the center. The lower axial ligand of the cobalt ion can be a variety of different groups, including cyano, hydroxo, methyl, or 5'-deoxyadenosyl groups.

Cobamides are involved in a number of important biological processes, including the synthesis of amino acids and nucleotides, the metabolism of fatty acids and cholesterol, and the regulation of gene expression. They function as cofactors for enzymes called cobamide-dependent methyltransferases, which transfer methyl groups (CH3) from one molecule to another.

Cobamides are found in a wide variety of organisms, including bacteria, archaea, and eukaryotes. In humans, the most important cobamide is vitamin B12, which is essential for the normal functioning of the nervous system and the production of red blood cells. Vitamin B12 deficiency can lead to neurological problems and anemia.

Transaminases, also known as aminotransferases, are a group of enzymes found in various tissues of the body, particularly in the liver, heart, muscle, and kidneys. They play a crucial role in the metabolism of amino acids, the building blocks of proteins.

There are two major types of transaminases: aspartate aminotransferase (AST) and alanine aminotransferase (ALT). Both enzymes are normally present in low concentrations in the bloodstream. However, when tissues that contain these enzymes are damaged or injured, such as during liver disease or muscle damage, the levels of AST and ALT in the blood may significantly increase.

Measurement of serum transaminase levels is a common laboratory test used to assess liver function and detect liver injury or damage. Increased levels of these enzymes in the blood can indicate conditions such as hepatitis, liver cirrhosis, drug-induced liver injury, heart attack, and muscle disorders. It's important to note that while elevated transaminase levels may suggest liver disease, they do not specify the type or cause of the condition, and further diagnostic tests are often required for accurate diagnosis and treatment.

Cyclohexanes are organic compounds that consist of a six-carbon ring arranged in a cyclic structure, with each carbon atom joined to two other carbon atoms by single bonds. This gives the molecule a shape that resembles a hexagonal ring. The carbons in the ring can be saturated, meaning that they are bonded to hydrogen atoms, or they can contain double bonds between some of the carbon atoms.

Cyclohexanes are important intermediates in the production of many industrial and consumer products, including plastics, fibers, dyes, and pharmaceuticals. They are also used as solvents and starting materials for the synthesis of other organic compounds.

One of the most well-known properties of cyclohexane is its ability to exist in two different conformations: a "chair" conformation and a "boat" conformation. In the chair conformation, the carbon atoms are arranged in such a way that they form a puckered ring, with each carbon atom bonded to two other carbons and two hydrogens. This conformation is more stable than the boat conformation, in which the carbon atoms form a flattened, saddle-shaped ring.

Cyclohexanes are relatively nonpolar and have low water solubility, making them useful as solvents for nonpolar substances. They also have a relatively high boiling point compared to other hydrocarbons of similar molecular weight, due to the fact that they can form weak intermolecular forces called London dispersion forces.

Cyclohexane is a flammable liquid with a mild, sweet odor. It is classified as a hazardous substance and should be handled with care. Exposure to cyclohexane can cause irritation of the eyes, skin, and respiratory tract, and prolonged exposure can lead to more serious health effects, including neurological damage.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

The periplasm is a term used in the field of microbiology, specifically in reference to gram-negative bacteria. It refers to the compartment or region located between the bacterial cell's inner membrane (cytoplasmic membrane) and its outer membrane. This space contains a unique mixture of proteins, ions, and other molecules that play crucial roles in various cellular processes, such as nutrient uptake, waste excretion, and the maintenance of cell shape.

The periplasm is characterized by its peptidoglycan layer, which provides structural support to the bacterial cell and protects it from external pressures. This layer is thinner in gram-negative bacteria compared to gram-positive bacteria, which do not have an outer membrane and thus lack a periplasmic space.

Understanding the periplasmic region of gram-negative bacteria is essential for developing antibiotics and other therapeutic agents that can target specific cellular processes or disrupt bacterial growth and survival.

Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.

The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.

Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.

Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Anthranilate synthase is a key enzyme in the synthesis of aromatic amino acids, specifically tryptophan. It catalyzes the reaction of chorismate and glutamine to form anthranilate, which is the first committed step in the biosynthetic pathway leading to tryptophan. Anthranilate synthase is a heterotetrameric enzyme composed of two different subunits, ASα and ASβ, in eukaryotes and some bacteria. In other bacteria, anthranilate synthase is a single polypeptide chain with both active sites. The activity of anthranilate synthase is tightly regulated at the transcriptional and allosteric levels to control the flow of carbon into the tryptophan biosynthetic pathway.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

A lyase is a type of enzyme that catalyzes the breaking of various chemical bonds in a molecule, often resulting in the formation of two new molecules. Lyases differ from other types of enzymes, such as hydrolases and oxidoreductases, because they create double bonds or rings as part of their reaction mechanism.

In the context of medical terminology, lyases are not typically discussed on their own, but rather as a type of enzyme that can be involved in various biochemical reactions within the body. For example, certain lyases play a role in the metabolism of carbohydrates, lipids, and amino acids, among other molecules.

One specific medical application of lyase enzymes is in the diagnosis of certain genetic disorders. For instance, individuals with hereditary fructose intolerance (HFI) lack the enzyme aldolase B, which is a type of lyase that helps break down fructose in the liver. By measuring the activity of aldolase B in a patient's blood or tissue sample, doctors can diagnose HFI and recommend appropriate dietary restrictions to manage the condition.

Overall, while lyases are not a medical diagnosis or condition themselves, they play important roles in various biochemical processes within the body and can be useful in the diagnosis of certain genetic disorders.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

In a medical context, feedback refers to the information or data about the results of a process, procedure, or treatment that is used to evaluate and improve its effectiveness. This can include both quantitative data (such as vital signs or laboratory test results) and qualitative data (such as patient-reported symptoms or satisfaction). Feedback can come from various sources, including patients, healthcare providers, medical equipment, and electronic health records. It is an essential component of quality improvement efforts, allowing healthcare professionals to make informed decisions about changes to care processes and treatments to improve patient outcomes.

... is found at a branch point in the pathway. The enzyme channels the substrate, chorismate to the biosynthesis ... For example, the secondary structure of the chorismate mutase of yeast is very similar to that of E. coli. Chorimate mutase in ... The systematic name of this enzyme class is chorismate pyruvatemutase. Chorismate mutase, also known as hydroxyphenylpyruvate ... chorismate mutase (EC 5.4.99.5) is an enzyme that catalyzes the chemical reaction for the conversion of chorismate to ...
Schmidt JC; Zalkin H (1969). "Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from ...
C10H10O6 Helmut Goerisch (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700-3705. doi: ... It is biosynthesized by a [3,3]-sigmatropic Claisen rearrangement of chorismate. Prephenic acid is an example of achiral ( ... "Thermodynamics of the Conversion of Chorismate to Prephenate: Experimental Results and Theoretical Predictions". J. Phys. Chem ...
"InterPro." Bifunctional Chorismate Mutase/prephenate Dehydrogenase T-protein (IPR008244). InterPro, n.d. Web. 24 Apr. 2014. ... prephenate dehydrogenase is fused with the enzyme chorismate mutase. This fusion is not found in plants or animals. As of late ... and chorismate mutase---prephenate dehydrogenase. This enzyme participates in phenylalanine, tyrosine and tryptophan ...
Prephenic acid is then synthesized by a Claisen rearrangement of chorismate by chorismate mutase. Prephenate is oxidatively ... Helmut Goerisch (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700-3705. doi:10.1021/ ... Then 5-enolpyruvylshikimate-3-phosphate is transformed into chorismate by a chorismate synthase. ... The pathway starts with two substrates, phosphoenol pyruvate and erythrose-4-phosphate, and ends with chorismate (chrorismic ...
Prephenic acid is then synthesized by a Claisen rearrangement of chorismate by chorismate mutase. Prephenate is oxidatively ... Goerisch, H. (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700-3705. doi:10.1021/ ... Then 5-enolpyruvylshikimate-3-phosphate is transformed into chorismate by a chorismate synthase. ... The pathway starts with two substrates, phosphoenol pyruvate and erythrose-4-phosphate and ends with chorismate, a substrate ...
Chorismate mutase is an intramolecular transferase and it catalyzes the conversion of chorismate to prephenate, used as a ... though the rate increases 106 fold in the presence of chorismate mutase. The reaction goes through a chair transition state ... "A strategically positioned cation is crucial for efficient catalysis by chorismate mutase". The Journal of Biological Chemistry ... Sub-categories of this class are: This category (EC 5.4) includes intramolecular transferases (mutases). These isomerases ...
Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3 ... Such cases exist: for example, a mutase such as phosphoglucomutase catalyses the transfer of a phospho group from one position ... Enzymes with single-substrate mechanisms include isomerases such as triosephosphateisomerase or bisphosphoglycerate mutase, ...
Chorismate mutase (right) catalyzes (speeds up) the production of the amino acids phenylalanine and tyrosine. Fructose-1,6- ... "Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures". Structure. 5 (11): 1437- ...
Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3 ...
For instance, the natural enzyme chorismate mutase, which catalyzes the Claisen rearrangement of chorismate, features many ... "New insight into the catalytic mechanism of chorismate mutases from structural studies". Chemistry & Biology. 2 (4): 195-203. ...
Chorismate mutase then converts chorismic acid to prephenate via a Claisen rearrangement (1,3-sigmatropic rearrangement). ...
This process is mediated by a phenylalanine (PheA) or tyrosine (TyrA) specific chorismate mutase-prephenate dehydrogenase. PheA ... trpE encodes the first subunit, which binds to chorismate and moves the amino group from the donor to chorismate. trpG encodes ... The rest of the enzymes in the common pathway (conversion of DAHP to chorismate) appear to be synthesized constitutively, ... Phenylalanine, tyrosine, and tryptophan, the aromatic amino acids, arise from chorismate. The first step, condensation of 3- ...
... is a structural homolog of the chorismate mutase enzyme in E. coli, and actually exhibits non-physiological ... Using the chorismate produced from that metabolic process, first the enzyme PchA will catalyze the reaction of chorismate into ... a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities". The Journal of ... chorismate mutase activity, albeit at a much lower efficiency. IPL also has several homologs found in other organisms, ...
ADTs contain an N-terminal transit peptide, a PDT-like domain, and an ACT (Aspartokinase, chorismate mutase, TyrA) domain. ...
The ACT domain is named after three of the proteins that contain it: aspartate kinase, chorismate mutase and TyrA. The ...
In the synthesis of L-phenylalanine, chorismate undergoes a Claisen rearrangement by a Chorismate mutase enzyme to form ...
One project demonstrated that an engineered version of Chorismate mutase still had catalytic activity when only nine amino ...
The enzyme chorismate mutase catalyzes the Claisen rearrangement of the enol ether called chorismate to prephenate, an ...
... may refer to: Prephenate dehydrogenase, an enzyme Chorismate mutase, an enzyme This set index ...
The enzyme chorismate mutase (EC 5.4.99.5) catalyzes the Claisen rearrangement of chorismate to prephenate, an intermediate in ...
... reported to have opportunities in the development of a new class of antibiotics as the compound clings to the chorismate mutase ...
... pathway of aromatic amino acids in Nocardia mediterranei 1994 Cloning vector system for Nocardia spp 1995 Chorismate mutase and ...
... chorismate mutase (CM) and isochorismatase (ICM), thought to be interfering on the salicylic acid pathway and thereby altering ...
2-acetolactate mutase MeSH D08.811.399.520.250 - chorismate mutase MeSH D08.811.399.520.250.500 - prephenate dehydratase MeSH ... phosphoglycerate mutase MeSH D08.811.399.894.200 - amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 - phosphoglucomutase MeSH D08.811.399.520.750.700 - ... D08.811.399.520.250.750 - prephenate dehydrogenase MeSH D08.811.399.520.625 - methylmalonyl-coa mutase MeSH D08.811.399.520.750 ...
2-acetolactate mutase EC 5.4.99.4: 2-methyleneglutarate mutase EC 5.4.99.5: chorismate mutase EC 5.4.99.6: Now EC 5.4.4.2, ... phosphoenolpyruvate mutase EC 5.4.2.10: phosphoglucosamine mutase EC 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate- ... benzene mutase EC 5.4.4.2: isochorismate synthase EC 5.4.4.3: 3-(hydroxyamino)phenol mutase EC 5.4.4.4: geraniol isomerase EC ... isobutyryl-CoA mutase EC 5.4.99.14: 4-carboxymethyl-4-methylbutenolide mutase EC 5.4.99.15: (1→4)-α-D-glucan 1-α-D- ...
Other names for this enzyme include: Isochorismate mutase Menaquinone-specific isochorismate synthase MenF MenF is a gene that ... More specifically it is classified as an intramolecular transferase because it transfers the hydroxy group of chorismate ... Isochorismate synthase catalyzes the irreversible conversion of chorismate to isochorismate: Isochorismate synthase is most ... 5-dihydrochorismate analogues as inhibitors of the chorismate-utilising enzymes". Organic & Biomolecular Chemistry. 7 (11): ...
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 ...
Chorismate mutase (1). * Common SYM gene (1). * Conservation (1). * GPAT (1). * Gene clustering (1) ...
Fold d.79: Bacillus chorismate mutase-like [55297] (9 superfamilies). core: beta-alpha-beta-alpha-beta(2); mixed beta-sheet: ...
Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner. The ... Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis. The FEBS Journal 272:375-389 ...
Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity. Author. *Keeffe ... Computational protein design methods were used to predict five variants of monofunctional Escherichia coli chorismate mutase ...
chorismate mutase 11, 18, 96, 138. MMP0596. C/D box methylation guide ribonucleoprotein complex aNOP56 subunit 20, 81. ...
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... chorismate mutase/prephenate dehydratase [Ensembl]. Prephenate dehydratase, Chorismate mutase type II [Interproscan].","protein ... Chorismate mutase type II [Interproscan].","protein_coding" "CRO74793","lgrE_1","Pseudomonas aeruginosa","Linear gramicidin ... ","p-aminobenzoate synthetase, component I [Ensembl]. chorismate binding enzyme, Anthranilate synthase component I [ ... ","Isochorismate synthase EntC [Ensembl]. chorismate binding enzyme [Interproscan].","protein_coding" "CRO74758","pchB"," ...
Chorismate mutase II, prokaryotic-type; Aminotransferase class V domain [Interproscan].","protein_coding" "SymbC1. ... ","Cyclic nucleotide-binding domain; Methylmalonyl-CoA mutase, alpha/beta chain, catalytic; Cobalamin (vitamin B12)-binding ...
... chorismate mutase and TyrA (prephenate dehydrogenase) [1]. The ACT domain is found in a variety of contexts and is proposed to ...
Ac3H11_2574: Chorismate mutase I (EC 5.4.99.5) / Prephenate dehydratase (EC 4.2.1.51). is similar to:. PaperBLAST. ... O30012: prephenate dehydrogenase (EC 1.3.1.12); prephenate dehydratase (EC 4.2.1.51); chorismate mutase (EC 5.4.99.5) from ... O30012: prephenate dehydrogenase (EC 1.3.1.12); prephenate dehydratase (EC 4.2.1.51); chorismate mutase (EC 5.4.99.5) from ...
Regulation of Chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from alcaligenes eutrophus. J Bacteriol. ...
Regulation of Chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from alcaligenes eutrophus. J Bacteriol. ...
2007) Exhaustive mutagenesis of six secondary active-site residues in Escherichia coli chorismate mutase shows the importance ... 2005) Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity; Protein ...
A DFT-based QM-MM approach designed for the treatment of large molecular systems: Application to chorismate mutase. A Crespo, ... Multiple-steering QM− MM calculation of the free energy profile in chorismate mutase. A Crespo, MA Mart , DA Estrin, AE ...
Gene: b2600: Chorismate mutase I (EC 5.4.99.5) / Cyclohexadienyl dehydrogenase (EC 1.3.1.12)(EC 1.3.1.43) ... Gene: STM2669: Chorismate mutase I (EC 5.4.99.5) / Cyclohexadienyl dehydrogenase (EC 1.3.1.12)(EC 1.3.1.43) ... Gene: y0904: Chorismate mutase I (EC 5.4.99.5) / Cyclohexadienyl dehydrogenase (EC 1.3.1.12)(EC 1.3.1.43) ... Gene: ECA3351: Chorismate mutase I (EC 5.4.99.5) / Cyclohexadienyl dehydrogenase (EC 1.3.1.12)(EC 1.3.1.43) ...
Evaluating the Diagnostic Potential of Chorismate Mutase Poly-Clonal Peptide Antibody for the Acanthamoeba Keratitis in an ... Here, the diagnostic potential of polyclonal antibodies targeting the chorismate mutase (CM) of Acanthamoeba spp. was evaluated ...
P-protein Includes: Chorismate mutase Short=CM EC=5.4.99.5 Includes: Prephenate dehydratase Short=PDT EC=4.2.1.51; ...
1. Crystallization and Preliminary Structural Studies of a Chorismate Mutase Catalytic Antibody Complexed With a Transition ...
... and topological redesign of a chorismate mutase.[48][55][56][57] To develop enzymes with new activities, one can take advantage ...
Designing new chorismate mutase enzymes with PoET. Aliphatic amidase sequence analysis (substitution and deletions). Screening ...
Abstracts: A DFT-based QM-MM approach designed for the treatment of large molecular systems: application to chorismate mutase ...
An evolution-based model for designing chorismate mutase enzymes. Science. 369, pp.440-445 (2020). ...
","Chorismate synthase, chloroplastic OS=Capnoides sempervirens (sp,p27793,aroc_capse : 118.0)","protein_coding" "MA_ ... ","UDP-L-arabinose mutase","protein_coding" "MA_1472069g0010","No alias","Picea abies","No annotation","protein_coding" "MA_ ... ","UDP-L-arabinose mutase","protein_coding" "MA_148293g0010","No alias","Picea abies","no hits & (original description: none ...
  • 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)
  • The conversion of chorismate to prephenate is the first committed step in the pathway to the production of the aromatic amino acids: tyrosine and phenylalanine. (wikipedia.org)
  • The ACT domain is a 90 amino acid long domain, which has been named after three of the allosterically regulated enzymes in which it is found: aspartate kinase, chorismate mutase and TyrA (prephenate dehydrogenase) [ 1 ]. (expasy.org)
  • Regulation of Chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from alcaligenes eutrophus. (medscape.com)
  • There are organisms such as Bacillus subtilis whose chorismate mutase have a completely different structure and are monofunctional. (wikipedia.org)
  • 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 transition state promoted catalysis. (wikipedia.org)
  • In the chorismate mutase active site, the transition-state analog is stabilized by 12 electrostatic and hydrogen-bonding interactions. (wikipedia.org)
  • 1. Crystallization and Preliminary Structural Studies of a Chorismate Mutase Catalytic Antibody Complexed With a Transition State Analog. (jinpanbio.cn)
  • These chorismate mutases are typically bifunctional enzymes, meaning they contain two catalytic capacities in the same polypeptide chain. (wikipedia.org)
  • The presence of chorismate mutase increases the rate of the reaction a million fold. (wikipedia.org)
  • Chorismate mutase is found at a branch point in the pathway. (wikipedia.org)
  • Chorismate mutase is only found in fungi, bacteria, and higher plants. (wikipedia.org)
  • In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. (bvsalud.org)
  • 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)