3-Hydroxyacyl CoA Dehydrogenases
Peroxisomal Bifunctional Enzyme
Carbon-Carbon Double Bond Isomerases
Peroxisomal Multifunctional Protein-2
Enoyl-CoA Hydratase 2
Racemases and Epimerases
Acyl Coenzyme A
Mitochondrial Trifunctional Protein
Neoplastic Syndromes, Hereditary
Molecular Sequence Data
Carbonic Anhydrase I
Amino Acid Sequence
Inactivation of both RNA binding and aconitase activities of iron regulatory protein-1 by quinone-induced oxidative stress. (1/505)Iron regulatory protein-1 (IRP-1) controls the expression of several mRNAs by binding to iron-responsive elements (IREs) in their untranslated regions. In iron-replete cells, a 4Fe-4S cluster converts IRP-1 to cytoplasmic aconitase. IRE binding activity is restored by cluster loss in response to iron starvation, NO, or extracellular H2O2. Here, we study the effects of intracellular quinone-induced oxidative stress on IRP-1. Treatment of murine B6 fibroblasts with menadione sodium bisulfite (MSB), a redox cycling drug, causes a modest activation of IRP-1 to bind to IREs within 15-30 min. However, IRE binding drops to basal levels within 60 min. Surprisingly, a remarkable loss of both IRE binding and aconitase activities of IRP-1 follows treatment with MSB for 1-2 h. These effects do not result from alterations in IRP-1 half-life, can be antagonized by the antioxidant N-acetylcysteine, and regulate IRE-containing mRNAs; the capacity of iron-starved MSB-treated cells to increase transferrin receptor mRNA levels is inhibited, and MSB increases the translation of a human growth hormone indicator mRNA bearing an IRE in its 5'-untranslated region. Nonetheless, MSB inhibits ferritin synthesis. Thus, menadione-induced oxidative stress leads to post-translational inactivation of both genetic and enzymatic functions of IRP-1 by a mechanism that lies beyond the "classical" Fe-S cluster switch and exerts multiple effects on cellular iron metabolism. (+info)
The aconitase of yeast. IV. Studies on iron and sulfur in yeast aconitase. (2/505)Chemical analyses were carried out to determine the active components of the crystalline aconitase [EC 22.214.171.124] of Candida lipolytica. The enzyme contained 2 atoms of non-heme iron, 1 atom of labile sulfur, and 6 sulfhydryl groups per molecule. One atom of the non-heme iron was released by the addition of metal-chelating agents such as sodium citrate, sodium nitrilotriacetate (NTA) or sodium ethylenediaminetetraacetate (EDTA) without loss of the enzyme activity. The non-heme iron and labile sulfur were released by the addition of sulfhydryl reagents such as rho-chloromercuribenzoate (PCMB), sodium mersalyl or urea with loss of the enzyme activity. o-Phenanthroline reacted with the iron atoms in the enzyme at pH 6.0 with loss of the activity. These results show that yeast aconitase is an iron-sulfur protein and that only one of the two non-heme iron atoms is essential for enzyme activity. (+info)
The aconitase of yeast. V. The reconstitution of yeast aconitase. (3/505)The apoenzyme of yeast aconitase [EC 126.96.36.199] was prepared by treatment of yeast aconitase with sodium mersalyl, followed by passage by passage of the reaction mixture through a column of Dowex A-1 and gel filtration on Sephadex G-25. The apoenzyme had no aconitase activity, but the active enzyme could be reconstituted by treatment of the apoenzyme with ferrous ions and sodium sulfide in the presence of 2-mercapto-ethanol. The reconstituted active enzyme was isolated by DEAE-Sephadex A-50 column chromatography and Sephadex G-100 gel filtration from the reaction mixture. The reconstituted enzyme was identical with the original untreated enzyme in terms of specific activity, iron content and spectral characteristics, but not in terms of labile sulfur content. A significant difference in visible spectra between the holo- and apoenzymes appeared to be due to the difference in iron and labile sulfur contents between the two proteins. (+info)
Population structure and genetic divergence in Anopheles nuneztovari (Diptera: Culicidae) from Brazil and Colombia. (4/505)Anopheles nuneztovari is considered an important vector of human malaria in several localities in Venezuela and Colombia. Its status as a vector of human malaria is still unresolved in areas of the Brazilian Amazon, in spite of have been found infected with Plasmodium sp.. For a better understanding of the genetic differentiation of populations of A. nuneztovari, electrophoretic analysis using 11 enzymes was performed on four populations from Brazil and two from Colombia. The results showed a strong differentiation for two loci: alpha-glycerophosphate dehydrogenase (alpha-Gpd) and malate dehydrogenase (Mdh) from 16 loci analyzed. Diagnostic loci were not detected. The populations of A. nuneztovari from the Brazilian Amazon showed little genetic structure and low geographic differentiation, based on the F(IS) (0.029), F(ST) (0.070), and genetic distance (0.001-0.032) values. The results of the isozyme analysis do not coincide with the indication of two lineages in the Amazon Basin by analysis of mitochondrial DNA, suggesting that this evolutionary event is recent. The mean F(ST) value (0.324) suggests that there is considerable genetic divergence among populations from the Brazilian Amazon and Colombia. The genetic distance among populations from the Brazilian Amazon and Colombia is ranges from 0.047 to 0.148, with the highest values between the Brazilian Amazon and Sitronela (SIT) (0.125-0.148). These results are consistent with those observed among members of anopheline species complexes. It is suggested that geographic isolation has reduced the gene flow, resulting in the genetic divergence of the SIT population. Dendrogram analysis showed three large groups: one Amazonian and two Colombia, indicating some genetic structuring. The present study is important because it attempted to clarify the taxonomic status of A. nuneztovari and provide a better understanding of the role of this mosquito in transmission of human malaria in northern South America. (+info)
Human cytoplasmic aconitase (Iron regulatory protein 1) is converted into its [3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding. (5/505)Iron regulatory protein 1 (IRP1) regulates the synthesis of proteins involved in iron homeostasis by binding to iron-responsive elements (IREs) of messenger RNA. IRP1 is a cytoplasmic aconitase when it contains a [4Fe-4S] cluster and an RNA-binding protein after complete removal of the metal center by an unknown mechanism. Human IRP1, obtained as the pure recombinant [4Fe-4S] form, is an enzyme as efficient toward cis-aconitate as the homologous mitochondrial aconitase. The aconitase activity of IRP1 is rapidly lost by reaction with hydrogen peroxide as the [4Fe-4S] cluster is quantitatively converted into the [3Fe-4S] form with release of a single ferrous ion per molecule. The IRE binding capacity of IRP1 is not elicited with H(2)O(2). Ferrous sulfate (but not other more tightly coordinated ferrous ions, such as the complex with ethylenediamine tetraacetic acid) counteracts the inhibitory action of hydrogen peroxide on cytoplasmic aconitase, probably by replenishing iron at the active site. These results cast doubt on the ability of reactive oxygen species to directly increase IRP1 binding to IRE and support a signaling role for hydrogen peroxide in the posttranscriptional control of proteins involved in iron homeostasis in vivo. (+info)
Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain. (6/505)Deletion of the yeast frataxin homologue, YFH1, elicits accumulation of iron in mitochondria and mitochondrial defects. We report here that in the presence of an iron chelator in the culture medium, the concentration of iron in mitochondria is the same in wild-type and YFH1 deletant strains. Under these conditions, the activity of the respiratory complexes is restored. However, the activity of the mitochondrial aconitase, a 4Fe-4S cluster-containing protein, remains low. The frataxin family bears homology to a bacterial protein family which confers resistance to tellurium, a metal closely related to sulfur. Yfh1p might control the synthesis of iron-sulfur clusters in mitochondria. (+info)
Bacillus subtilis aconitase is an RNA-binding protein. (7/505)The aconitase protein of Bacillus subtilis was able to bind specifically to sequences resembling the iron response elements (IREs) found in eukaryotic mRNAs. The sequences bound include the rabbit ferritin IRE and IRE-like sequences in the B. subtilis operons that encode the major cytochrome oxidase and an iron uptake system. IRE binding activity was affected by the availability of iron both in vivo and in vitro. In eukaryotic cells, aconitase-like proteins regulate translation and stability of iron metabolism mRNAs in response to iron availability. A mutant strain of B. subtilis that produces an enzymatically inactive aconitase that was still able to bind RNA sporulated 40x more efficiently than did an aconitase null mutant, suggesting that a nonenzymatic activity of aconitase is important for sporulation. The results support the idea that bacterial aconitases, like their eukaryotic homologs, are bifunctional proteins, showing aconitase activity in the presence of iron and RNA binding activity when cells are iron-deprived. (+info)
Iron-dependent regulation of transferrin receptor expression in Trypanosoma brucei. (8/505)Transferrin is an essential growth factor for African trypanosomes. Here we show that expression of the trypanosomal transferrin receptor, which bears no structural similarity with mammalian transferrin receptors, is regulated by iron availability. Iron depletion of bloodstream forms of Trypanosoma brucei with the iron chelator deferoxamine resulted in a 3-fold up-regulation of the transferrin receptor and a 3-fold increase of the transferrin uptake rate. The abundance of expression site associated gene product 6 (ESAG6) mRNA, which encodes one of the two subunits of the trypanosome transferrin receptor, is regulated 5-fold by a post-transcriptional mechanism. In mammalian cells the stability of transferrin receptor mRNA is controlled by iron regulatory proteins (IRPs) binding to iron-responsive elements (IREs) in the 3'-untranslated region (UTR). Therefore, the role of a T. brucei cytoplasmic aconitase (TbACO) that is highly related to mammalian IRP-1 was investigated. Iron regulation of the transferrin receptor was found to be unaffected in Deltaaco::NEO/Deltaaco::HYG null mutants generated by targeted disruption of the TbACO gene. Thus, the mechanism of post-transcriptional transferrin receptor regulation in trypanosomes appears to be distinct from the IRE/IRP paradigm. The transferrin uptake rate was also increased when trypanosomes were transferred from medium supplemented with foetal bovine serum to medium supplemented with sera from other vertebrates. Due to varying binding affinities of the trypanosomal transferrin receptor for transferrins of different species, serum change can result in iron starvation. Thus, regulation of transferrin receptor expression may be a fast compensatory mechanism upon transmission of the parasite to a new host species. (+info)
Aconitate hydratase is an enzyme that plays a role in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid cycle. It is responsible for converting aconitase to cis-aconitate, which is an important step in the breakdown of fatty acids and amino acids for energy production in the body. A deficiency in aconitate hydratase can lead to a rare genetic disorder called aconitase deficiency, which can cause a range of symptoms including muscle weakness, developmental delays, and seizures.
Aconitic acid is a dicarboxylic acid that is found naturally in many plants, including hops and walnuts. It is also produced synthetically and has been used in various medical applications. In the medical field, aconitic acid is primarily used as a local anesthetic. It is applied topically to the skin to numb the area and reduce pain. It is also used as a muscle relaxant and to treat muscle spasms. Aconitic acid has also been studied for its potential use in treating certain types of cancer. It has been shown to have anti-tumor effects and may be effective in combination with other cancer treatments. However, aconitic acid can be toxic in high doses and can cause serious side effects, including nausea, vomiting, and cardiac arrhythmias. As a result, it is typically only used under the supervision of a healthcare professional and is not available over-the-counter.
Isocitrate is a metabolic intermediate that is involved in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid cycle. It is a six-carbon compound that is produced when glucose is metabolized in the body. In the medical field, isocitrate is often used as a diagnostic tool to help identify certain metabolic disorders. For example, elevated levels of isocitrate in the blood or urine can be a sign of a genetic disorder called isocitrate dehydrogenase deficiency, which is a rare condition that affects the metabolism of certain amino acids and fatty acids. Isocitrate is also used as a precursor in the synthesis of other important molecules in the body, such as cholesterol and other lipids. In addition, it has been studied for its potential therapeutic uses in the treatment of various diseases, including cancer, Alzheimer's disease, and diabetes.
Hydrolyases are a class of enzymes that catalyze the hydrolysis of various substrates, including esters, amides, and phosphates, by breaking the bonds between the hydroxyl group and the carbon atom. In the medical field, hydrolyases are important in the metabolism of various compounds, including drugs, hormones, and neurotransmitters. For example, the enzyme chymotrypsin is a hydrolyase that breaks down proteins into smaller peptides and amino acids, which are essential for various bodily functions. Similarly, the enzyme acetylcholinesterase is a hydrolyase that breaks down the neurotransmitter acetylcholine, which is important for muscle movement and memory. In some cases, hydrolyases can also be involved in the formation of certain compounds, such as the synthesis of fatty acids from acetyl-CoA.
Fluorine is a chemical element with the symbol F and atomic number 9. It is a highly reactive, non-metallic gas that is commonly used in various medical applications. In the medical field, fluorine is used in the production of a wide range of compounds, including fluoride toothpaste, which helps to prevent tooth decay by strengthening tooth enamel. Fluoride is also used in the treatment of certain medical conditions, such as osteoporosis, by increasing bone density. Fluorine is also used in the production of certain medications, such as fluoroquinolones, which are antibiotics used to treat a variety of bacterial infections. Additionally, fluorine is used in the production of certain imaging agents, such as fluorodeoxyglucose (FDG), which is used in positron emission tomography (PET) scans to detect cancer and other diseases. However, it is important to note that fluorine is a highly toxic element and can cause serious health problems if not handled properly. Therefore, its use in medical applications is closely regulated and monitored to ensure safety.
Citrates are a group of compounds that contain the citric acid ion (C6H8O7^3-). In the medical field, citrates are commonly used as anticoagulants to prevent blood clots from forming. They are often used in patients who are undergoing dialysis or who have a condition called heparin-induced thrombocytopenia (HIT), which makes it difficult to use heparin, a commonly used anticoagulant. Citrates are also used to treat certain types of kidney stones, as they can help to neutralize the acidic environment in the urinary tract that can contribute to the formation of stones. In addition, citrates are sometimes used as a source of calcium in patients who cannot tolerate other forms of calcium supplementation. Citrates can be administered orally or intravenously, and they are usually well-tolerated by most people. However, like all medications, they can cause side effects, such as nausea, vomiting, and diarrhea. It is important to follow the instructions of your healthcare provider when taking citrates, and to report any side effects that you experience.
Enoyl-CoA hydratase is an enzyme that plays a crucial role in the metabolism of fatty acids. It catalyzes the hydration of enoyl-CoA, a molecule that is formed during the beta-oxidation of fatty acids, to produce hydroxyacyl-CoA. This reaction is an important step in the breakdown of fatty acids for energy production in the body. Enoyl-CoA hydratase is encoded by the ECH gene and is found in the mitochondria of cells. It is a member of the short-chain dehydrogenase/reductase (SDR) family of enzymes, which are involved in a wide range of metabolic processes. Deficiency or dysfunction of enoyl-CoA hydratase can lead to a rare genetic disorder called enoyl-CoA hydratase deficiency, which is characterized by the accumulation of toxic intermediates in the metabolism of fatty acids. This can cause a range of symptoms, including muscle weakness, developmental delays, and neurological problems.
Isocitrate dehydrogenase (IDH) is an enzyme that plays a critical role in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid cycle. It catalyzes the conversion of isocitrate to alpha-ketoglutarate (α-KG) in the presence of NAD+ as a cofactor. This reaction is an important step in the production of energy in the form of ATP through cellular respiration. In the medical field, IDH is of particular interest because mutations in the IDH1 and IDH2 genes have been implicated in the development of certain types of cancer, including gliomas, acute myeloid leukemia, and chondrosarcoma. These mutations result in the production of an abnormal form of the enzyme that has altered activity and can lead to the accumulation of alpha-ketoglutarate, which can promote tumor growth and progression. As a result, IDH mutations are now considered important biomarkers for the diagnosis and prognosis of certain types of cancer, and targeted therapies that inhibit the activity of mutant IDH enzymes are being developed for their treatment.
Malates are a group of organic compounds that are commonly found in plants and some microorganisms. In the medical field, malates are often used as a dietary supplement or as a component in certain medications. One of the most well-known uses of malates is in the treatment of metabolic disorders such as diabetes and obesity. Malates have been shown to improve insulin sensitivity and glucose metabolism, which can help to regulate blood sugar levels and reduce the risk of complications associated with these conditions. Malates are also used in the treatment of liver disease, as they can help to protect liver cells from damage and promote liver function. In addition, malates have been shown to have anti-inflammatory properties, which may make them useful in the treatment of a variety of inflammatory conditions. Overall, malates are a versatile compound with a range of potential health benefits. However, more research is needed to fully understand their mechanisms of action and potential therapeutic applications.
Fumarate hydratase (FH) is an enzyme that plays a critical role in the metabolism of fumarate, a molecule involved in the citric acid cycle. In the medical field, FH deficiency is a rare genetic disorder that affects the metabolism of fumarate and leads to the accumulation of this molecule in the body. This accumulation can cause a variety of health problems, including kidney disease, high blood pressure, and an increased risk of developing certain types of cancer, such as kidney cancer and ovarian cancer. Treatment for FH deficiency typically involves managing the symptoms of the condition and addressing any complications that arise.
3-Hydroxyacyl CoA dehydrogenases are a group of enzymes that play a crucial role in the metabolism of fatty acids. These enzymes catalyze the oxidation of 3-hydroxyacyl-CoA molecules to their corresponding trans-enoyl-CoA molecules, which is an essential step in the breakdown of fatty acids for energy production. In the medical field, 3-hydroxyacyl CoA dehydrogenases are often studied in the context of metabolic disorders such as diabetes, obesity, and fatty liver disease. Abnormalities in the activity or expression of these enzymes can lead to the accumulation of toxic intermediates in the fatty acid metabolism pathway, which can cause cellular damage and contribute to the development of these diseases. In addition, 3-hydroxyacyl CoA dehydrogenases are also important in the regulation of energy metabolism in the body. They are involved in the control of the citric acid cycle, which is the primary source of energy for the body's cells. Therefore, understanding the function and regulation of these enzymes is important for developing new treatments for metabolic disorders and improving overall health.
Leiomyomatosis is a medical term that refers to the presence of benign (non-cancerous) tumors made up of smooth muscle cells, called leiomyomas or leiomyomata, in various parts of the body. These tumors are most commonly found in the uterus (womb) and are known as uterine leiomyomas or fibroids. Leiomyomas can also occur in other parts of the body, such as the esophagus, stomach, small intestine, colon, and rectum, as well as in the skin, breast, and other organs. In these cases, the tumors are referred to as extragenital leiomyomas. Leiomyomas are typically asymptomatic and do not require treatment unless they cause symptoms such as pain, heavy bleeding, or pressure on surrounding organs. Treatment options for leiomyomas may include medication, surgery, or other interventions, depending on the size, location, and symptoms of the tumors.
Peroxisomal bifunctional enzyme (PBE) is a type of enzyme that catalyzes two different reactions within peroxisomes, which are small organelles found in the cytoplasm of cells. Peroxisomes are involved in various metabolic processes, including the breakdown of fatty acids and the detoxification of harmful substances. PBEs are unique in that they contain two catalytic domains, each of which is capable of catalyzing a different reaction. This allows PBEs to perform two different functions within the peroxisome, making them highly efficient enzymes. PBEs are involved in a number of important metabolic pathways, including the beta-oxidation of fatty acids, the breakdown of branched-chain amino acids, and the detoxification of harmful substances such as alcohol and drugs. Mutations in the genes encoding PBEs can lead to a variety of metabolic disorders, including Zellweger syndrome and neonatal adrenoleukodystrophy.
Dodecenoyl-CoA isomerase is an enzyme that catalyzes the isomerization of dodecenoyl-CoA to tetradecenoyl-CoA in the process of fatty acid metabolism. This enzyme is involved in the breakdown of very long-chain fatty acids (VLCFAs) and plays a role in the regulation of energy metabolism in the body. Mutations in the gene encoding dodecenoyl-CoA isomerase have been associated with a rare genetic disorder called Refsum disease, which is characterized by the accumulation of VLCFAs in the body and can lead to neurological and vision problems.
In the medical field, Carbon-Carbon Double Bond Isomerases are enzymes that catalyze the isomerization of carbon-carbon double bonds in organic molecules. These enzymes play important roles in various metabolic pathways, including the biosynthesis of fatty acids, terpenoids, and steroids. There are several types of carbon-carbon double bond isomerases, including enoyl-acyl carrier protein reductase (ENR), 2-enoyl-CoA hydratase (ECH), and 3-hydroxyacyl-CoA dehydrogenase (HADH). These enzymes are involved in the metabolism of fatty acids, where they catalyze the isomerization of enoyl-CoA to 3-ketoacyl-CoA, which is a key step in the biosynthesis of fatty acids. In addition to their role in fatty acid metabolism, carbon-carbon double bond isomerases are also involved in the metabolism of other organic molecules, such as terpenoids and steroids. For example, the enzyme squalene epoxidase, which is involved in the biosynthesis of cholesterol, is a carbon-carbon double bond isomerase that catalyzes the isomerization of squalene to 2,3-oxidosqualene. Overall, carbon-carbon double bond isomerases are important enzymes that play critical roles in various metabolic pathways in the body.
Peroxisomal Multifunctional Protein-2 (PMP2) is a protein that is involved in the transport of molecules across the peroxisomal membrane. It is a member of the PMP family of proteins, which are involved in the biogenesis and maintenance of peroxisomes. PMP2 is encoded by the PEX5 gene and is found in a variety of tissues in the body, including the liver, kidney, and brain. In the medical field, PMP2 is of interest because it is involved in the metabolism of various substances, including fatty acids and bile acids. Mutations in the PEX5 gene can lead to peroxisome biogenesis disorders, which are a group of rare genetic disorders that affect the functioning of peroxisomes. These disorders can cause a range of symptoms, including neurological problems, liver disease, and developmental delays.
Enoyl-CoA hydratase 2 (ECHS2) is an enzyme that plays a role in the metabolism of fatty acids. It is a member of the enoyl-CoA hydratase family of enzymes, which catalyze the hydration of enoyl-CoA thioesters to trans-2-enoyl-CoA thioesters. This reaction is an important step in the beta-oxidation of fatty acids, which is the process by which fatty acids are broken down to produce energy. In the medical field, ECHS2 is of interest because it has been implicated in the development of certain diseases, including obesity and type 2 diabetes. Mutations in the ECHS2 gene have been associated with an increased risk of developing these conditions, and the enzyme has been proposed as a potential therapeutic target for the treatment of these diseases. Additionally, ECHS2 has been shown to play a role in the metabolism of other lipids, such as cholesterol and triglycerides, and may be involved in the development of cardiovascular disease.
Isomerases are a class of enzymes that catalyze the interconversion of isomers, which are molecules with the same molecular formula but different arrangements of atoms. In the medical field, isomerases are important because they play a role in many biological processes, including metabolism, signal transduction, and gene expression. There are several types of isomerases, including: 1. Stereoisomerases: These enzymes catalyze the interconversion of stereoisomers, which are molecules with the same molecular formula and connectivity but different spatial arrangements of atoms. Examples of stereoisomerases include epimerases, which interconvert epimers (stereoisomers that differ in configuration at a single chiral center), and diastereomerases, which interconvert diastereomers (stereoisomers that differ in configuration at two or more chiral centers). 2. Conformational isomerases: These enzymes catalyze the interconversion of conformational isomers, which are molecules with the same molecular formula and connectivity but different three-dimensional structures. Examples of conformational isomerases include chaperones, which assist in the folding and unfolding of proteins, and peptidyl-prolyl cis-trans isomerases, which catalyze the interconversion of cis and trans isomers of proline residues in peptides and proteins. 3. Metabolic isomerases: These enzymes catalyze the interconversion of metabolic isomers, which are molecules that are involved in metabolic pathways. Examples of metabolic isomerases include aldolases, which catalyze the reversible cleavage of aldoses into ketoses and aldehydes, and transketolases, which catalyze the transfer of a keto group from one aldose to another. Isomerases are important in the medical field because they can be targeted for the treatment of diseases. For example, some drugs target specific isomerases to treat metabolic disorders, such as diabetes and obesity, and some drugs target isomerases to treat cancer, such as by inhibiting the activity of enzymes involved in the metabolism of cancer cells.
Racemases and epimerases are enzymes that catalyze the interconversion of stereoisomers in biological systems. They are involved in the biosynthesis and degradation of many important molecules, including amino acids, sugars, and lipids. Racemases are enzymes that catalyze the racemization of chiral centers, converting a molecule from one enantiomer to its mirror image. This process is important in the biosynthesis of many amino acids, which are chiral molecules that are essential for the structure and function of proteins. Epimerases, on the other hand, are enzymes that catalyze the interconversion of epimers, which are stereoisomers that differ in configuration at a single chiral center. This process is important in the biosynthesis and degradation of many sugars and other chiral molecules. Both racemases and epimerases play important roles in the metabolism of living organisms, and their activity is often regulated by various factors, including the availability of substrates and the presence of inhibitors. In the medical field, racemases and epimerases are the targets of several drugs, including antibiotics and antiviral agents, and they are also being studied as potential therapeutic targets for a variety of diseases.
Acyl Coenzyme A (acyl-CoA) is a molecule that plays a central role in metabolism. It is formed when an acyl group (a fatty acid or other long-chain hydrocarbon) is attached to the coenzyme A molecule, which is a small molecule that contains a thiol (-SH) group. Acyl-CoA molecules are involved in a variety of metabolic processes, including the breakdown of fatty acids (beta-oxidation), the synthesis of fatty acids (fatty acid synthesis), and the synthesis of other important molecules such as cholesterol and ketone bodies. In the medical field, acyl-CoA is often measured as a way to assess the activity of certain metabolic pathways, and imbalances in acyl-CoA levels can be associated with a variety of diseases and disorders.
Tungsten is a chemical element with the symbol W and atomic number 74. It is a hard, dense, and lustrous transition metal that is often used in medical applications due to its unique properties. One of the main uses of tungsten in medicine is in the production of medical devices such as surgical instruments, dental tools, and prosthetic implants. Tungsten is used because of its high melting point, which allows it to withstand the high temperatures generated during surgical procedures. It is also highly resistant to corrosion, which makes it ideal for use in medical devices that are exposed to bodily fluids. Tungsten is also used in radiation therapy for cancer treatment. Tungsten-based shielding materials are used to protect medical personnel and patients from the harmful effects of radiation during treatment. Tungsten is also used in the production of radiation therapy equipment, such as linear accelerators and brachytherapy sources. In addition, tungsten is used in the production of medical imaging equipment, such as X-ray machines and computed tomography (CT) scanners. Tungsten is used in the construction of X-ray targets, which are used to produce high-energy X-rays that are used to create images of the inside of the body. Overall, tungsten is an important material in the medical field due to its unique properties, which make it ideal for use in a wide range of medical applications.
Mitochondrial trifunctional protein (MTP) is a multi-enzyme complex that is located in the inner mitochondrial membrane. It is composed of three enzymes: alpha-ketoglutarate dehydrogenase, dihydrolipoyl transacetylase, and dihydrolipoyl dehydrogenase. These enzymes work together to catalyze the final step in the beta-oxidation of fatty acids, which is the conversion of acetyl-CoA to CO2 and hydrogen. MTP plays a critical role in the metabolism of fatty acids and is essential for the production of energy in the mitochondria. Mutations in the genes encoding the subunits of MTP can lead to a group of inherited metabolic disorders known as mitochondrial trifunctional protein deficiency. These disorders are characterized by a deficiency in fatty acid oxidation and can cause a range of symptoms, including muscle weakness, developmental delays, and neurological problems.
In the medical field, "crotonates" refers to a class of organic compounds that are derived from the plant species Croton tiglium. These compounds are also known as "croton oil" or "tiglium oil" and are commonly used as a laxative or purgative. Crotonates are made up of a long chain of carbon atoms with a carboxyl group (-COOH) at one end. They are typically colorless or yellowish liquids with a strong, unpleasant odor. When ingested, crotonates can cause diarrhea and abdominal cramping due to their ability to stimulate the production of digestive juices and increase the movement of the intestines. While crotonates have been used for medicinal purposes for centuries, they can also be toxic in high doses and may cause liver damage or other serious health problems. As a result, their use as a laxative is now generally discouraged, and alternative treatments are preferred.
In the medical field, a multienzyme complex is a group of two or more enzymes that are physically and functionally linked together to form a single, larger enzyme complex. These complexes can work together to catalyze a series of sequential reactions, or they can work in parallel to carry out multiple reactions simultaneously. Multienzyme complexes are found in a variety of biological processes, including metabolism, DNA replication and repair, and signal transduction. They can be found in both prokaryotic and eukaryotic cells, and they can be composed of enzymes from different cellular compartments. One example of a multienzyme complex is the 2-oxoglutarate dehydrogenase complex, which is involved in the citric acid cycle and the metabolism of amino acids. This complex consists of three enzymes that work together to catalyze the conversion of 2-oxoglutarate to succinyl-CoA. Multienzyme complexes can have important implications for human health. For example, mutations in genes encoding enzymes in these complexes can lead to metabolic disorders, such as maple syrup urine disease and glutaric acidemia type II. Additionally, some drugs target specific enzymes in multienzyme complexes as a way to treat certain diseases, such as cancer.
Acrylonitrile is a colorless gas that is used in the production of various chemicals, including acrylic fibers, plastics, and resins. It is not typically used in the medical field, as it is a toxic substance that can cause respiratory and neurological problems if inhaled or ingested. However, acrylonitrile is sometimes used as a solvent or a chemical intermediate in the production of other medical compounds. In these cases, it is important to handle acrylonitrile with care to prevent exposure and to follow proper safety protocols.
Epoxide hydrolases are a group of enzymes that catalyze the hydrolysis of epoxides, which are three-membered cyclic ethers. These enzymes play an important role in the metabolism of various compounds, including some drugs and environmental pollutants. In the medical field, epoxide hydrolases are of particular interest because they can modulate the activity of certain drugs by converting them into less active or inactive metabolites. For example, some anti-cancer drugs, such as tamoxifen and etoposide, are activated by epoxide hydrolases in certain tissues, while others, such as benzo[a]pyrene, are detoxified by these enzymes. Epoxide hydrolases are also involved in the metabolism of some endogenous compounds, such as fatty acids and bile acids. In addition, they have been implicated in the development of certain diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. Overall, epoxide hydrolases play a critical role in the metabolism of a wide range of compounds, and their activity can have important implications for human health.
Polyhydroxyalkanoates (PHAs) are a group of biodegradable and biocompatible polymers that are produced by various microorganisms, including bacteria and algae. In the medical field, PHAs are being studied for their potential use in a variety of applications, including drug delivery systems, tissue engineering scaffolds, and medical implants. PHAs are synthesized by microorganisms as a way to store excess carbon and energy. They are composed of repeating units of hydroxyalkanoic acids, which are linked together by ester bonds. The specific composition and properties of PHAs can vary depending on the microorganism that produces them and the conditions under which they are synthesized. One of the key advantages of PHAs is their biodegradability, which means that they can be broken down by the body or the environment over time. This makes them an attractive alternative to traditional synthetic polymers, which can persist in the environment for decades or even centuries. In the medical field, PHAs are being investigated for their potential use in drug delivery systems, where they can be used to encapsulate and release drugs over time. They are also being studied as potential tissue engineering scaffolds, where they can be used to support the growth and differentiation of cells. Additionally, PHAs are being explored as potential materials for medical implants, such as sutures and dental fillings, due to their biocompatibility and ability to be tailored to specific applications.
Hereditary neoplastic syndromes are a group of genetic disorders that increase the risk of developing cancer. These syndromes are caused by mutations in certain genes that are involved in regulating cell growth and division. People with these syndromes may have an increased risk of developing certain types of cancer, such as breast, ovarian, colorectal, and pancreatic cancer. They may also have other symptoms, such as developmental delays, skin abnormalities, and an increased risk of bleeding or blood clots. These syndromes are usually inherited in an autosomal dominant pattern, which means that a person only needs to inherit one copy of the mutated gene from one parent to develop the syndrome.
17-Hydroxysteroid dehydrogenases (17-HSDs) are a group of enzymes that play a crucial role in the metabolism of sex hormones in the human body. These enzymes are responsible for converting one form of a sex hormone into another, which can affect the hormone's activity and impact various physiological processes. There are several types of 17-HSDs, each with a specific function. For example, 17-HSD1 is involved in the conversion of estradiol to estrone, while 17-HSD2 is involved in the conversion of testosterone to dihydrotestosterone. These enzymes are found in various tissues throughout the body, including the liver, adrenal glands, and reproductive organs. Abnormalities in the activity of 17-HSDs can lead to various medical conditions, such as polycystic ovary syndrome (PCOS), which is characterized by hormonal imbalances and irregular menstrual cycles. In addition, some forms of cancer, such as breast and ovarian cancer, have been linked to changes in the activity of 17-HSDs. Overall, 17-HSDs play a critical role in regulating sex hormone metabolism and are an important area of research in the field of endocrinology.
Brevibacterium is a genus of Gram-positive bacteria that are commonly found in soil, water, and the air. In the medical field, Brevibacterium species are known to cause a variety of infections in humans and animals, including skin infections, respiratory infections, and ear infections. Some species of Brevibacterium have also been associated with food spoilage and the production of certain antibiotics. Treatment for Brevibacterium infections typically involves the use of antibiotics, although the specific antibiotic used may depend on the species of Brevibacterium causing the infection.
Carbonic anhydrase I (CA I) is an enzyme that catalyzes the reversible hydration of carbon dioxide (CO2) to bicarbonate (HCO3-) and a proton (H+). It is primarily found in red blood cells, where it plays a crucial role in the transport of CO2 from tissues to the lungs for exhalation. In the medical field, CA I is often measured as a biomarker for various diseases and conditions, including renal disease, liver disease, and cancer. Abnormal levels of CA I can indicate impaired kidney function, liver damage, or the presence of certain types of cancer. Additionally, CA I inhibitors are being developed as potential treatments for certain types of cancer and other diseases.
In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.
Deltaproteobacteria is a class of bacteria that belongs to the phylum Proteobacteria. They are gram-negative bacteria that are found in a variety of environments, including soil, water, and the human gut. Some species of Deltaproteobacteria are pathogenic and can cause infections in humans and animals, while others are beneficial and play important roles in nutrient cycling and the breakdown of organic matter. In the medical field, Deltaproteobacteria are of interest because of their potential as sources of new antibiotics and their role in the development of diseases such as periodontitis and respiratory infections.
Fibric acids are a group of organic compounds that are produced by the metabolism of carbohydrates in the body. They are also known as fatty acids or triglycerides. In the medical field, fibric acids are often used to treat high cholesterol levels and other related conditions. They work by reducing the amount of cholesterol and triglycerides in the blood, which can help to prevent heart disease and stroke. Fibric acids are available as prescription medications and are typically taken in pill form.
Vanillic acid is a naturally occurring compound that is found in a variety of plants, including vanilla beans. It is a phenolic acid that is structurally related to p-hydroxybenzoic acid and has a molecular formula of C8H8O4. In the medical field, vanillic acid has been studied for its potential therapeutic effects, including its ability to reduce inflammation, improve cognitive function, and modulate the immune system. It has also been used in the treatment of certain skin conditions, such as eczema and psoriasis. However, more research is needed to fully understand the potential benefits and risks of vanillic acid as a therapeutic agent.
Fumarates are organic compounds that contain the functional group -COO-. They are named after the chemical compound fumaric acid, which is a dicarboxylic acid with the formula C4H4O4. Fumarates are commonly used in the medical field as drugs to treat various conditions, including: 1. Hyperkalemia: Fumarates are used to treat high levels of potassium in the blood (hyperkalemia) by increasing the excretion of potassium in the urine. 2. Heart failure: Fumarates are used to treat heart failure by improving the function of the heart muscle and reducing the workload on the heart. 3. Gout: Fumarates are used to treat gout by reducing the production of uric acid in the body. 4. Cancer: Fumarates are being studied as potential cancer treatments due to their ability to inhibit the growth of cancer cells. 5. Inflammatory bowel disease: Fumarates are being studied as potential treatments for inflammatory bowel disease (IBD) by reducing inflammation in the gut. Some examples of fumarate drugs include fumaric acid esters (FAEs), which are used to treat psoriasis and multiple sclerosis, and dimethyl fumarate (DMF), which is used to treat relapsing-remitting multiple sclerosis.
Cobalt is a chemical element with the symbol Co and atomic number 27. It is a hard, silvery-gray metal that is often used in the production of magnets, batteries, and pigments. In the medical field, cobalt is used in the production of radioactive isotopes, such as cobalt-60, which are used in radiation therapy to treat cancer. Cobalt-60 is a strong gamma emitter that can be used to destroy cancer cells while minimizing damage to surrounding healthy tissue. It is also used in the production of medical devices, such as stents and implants, and as a component in some dental fillings.
List of MeSH codes (D08)
List of EC numbers (EC 4)
Crossover experiment (chemistry)
List of EC numbers (EC 5)
List of EC numbers (EC 2)
Aconitate hydratase 1 (Escherichia coli O6) | Protein Target - PubChem
Aco1 MGI Mouse Gene Detail - MGI:87879 - aconitase 1
ALCOdbCyano - slr1138
Propagation of Fur regulog to Staphylococcus haemolyticus JCSC1435
Acyltransferases - Small-Molecule Inhibitor of Hepatitis C Virus Infectivity
Institute of Biochemistry and Molecular Biology - Research output - National Yang Ming Chiao Tung University Academic Hub
Network Portal - Gene GSU1856
Protein PP 2112 in Pseudomonas putida KT2440
Botton-up proteomics suggests an association between differential expression of mitochondrial proteins and chronic fatigue...
Inhibition of mitochondrial aconitase by succination in fumarate hydratase deficiency. - NDM Research Building
Global transcriptional control by glucose and
Legit Cheats | Mods, Aimbot & More | Balkan Grill Garten
Differential phenotyping of Brucella species using a newly developed semi-automated metabolic system | BMC Microbiology | Full...
Fumarate Hydratase | Profiles RNS
Esketamine) | BLDpharm
's research topics | Profiles RNS
CITRIC ACID | SelfDecode | Genome Analysis
CoP: Co-expressed Biological Processes
Reactive Oxygen Species | Immunology/Inflammation| CSNpharm
Krebs Cycle | Encyclopedia.com
Cardiac Proteomic Responses to Ischemia
An evaluation of genetic causes and environmental risks for bilateral optic atrophy - PubMed
Crystal structure of human iron regulatory protein 1 as cytosolic aconitase - PubMed
Code System Concept
Propagation of Fur regulog to Staphylococcus aureus subsp. aureus str. JKD6008
Finding step acn for L-valine catabolism in Azospirillum brasilense Sp245
Network Portal - Gene GSU0844
NWMN 1966 - AureoWiki
Pharos : Target Details - ACO2
Pharos : Target Details - ACO1
NDF-RT Code NDF-RT Name
BBO SDW 850 - Telegraph
Metabolic adaptation to chronic hypoxia in cardiac mitochondria. - Oxford Stem Cell Institute
Nano Minerals: Nanoclays) | BLDpharm
- Inhibition of mitochondrial aconitase by succination in fumarate hydratase deficiency. (ox.ac.uk)
- The gene encoding the Krebs cycle enzyme fumarate hydratase (FH) is mutated in hereditary leiomyomatosis and renal cell cancer (HLRCC). (ox.ac.uk)
- Fumarate Hydratase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
- This graph shows the total number of publications written about "Fumarate Hydratase" by people in this website by year, and whether "Fumarate Hydratase" was a major or minor topic of these publications. (uchicago.edu)
- Below are the most recent publications written about "Fumarate Hydratase" by people in Profiles. (uchicago.edu)
- Computational Saturation Screen Reveals the Landscape of Mutations in Human Fumarate Hydratase. (uchicago.edu)
- Reappraisal of Morphologic Differences Between Renal Medullary Carcinoma, Collecting Duct Carcinoma, and Fumarate Hydratase-deficient Renal Cell Carcinoma. (uchicago.edu)
- Fumarate hydratase is a critical metabolic regulator of hematopoietic stem cell functions. (uchicago.edu)
- Identification of fumarate hydratase inhibitors with nutrient-dependent cytotoxicity. (uchicago.edu)
- The selected proteins were as follows: aconitate hydratase (ACON), ATP synthase subunit beta (ATPB) and malate dehydrogenase (MDHM). (unipi.it)
- Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (By similarity). (smpdb.ca)
- In step two of the Krebs cycle, citrate is isomerized to isocitrate by means of a dehydration reaction that yields cis -aconitate, followed by a hydration reaction that replaces the H + and OH- to form isocitrate. (encyclopedia.com)
- The enzyme aconitase catalyzes both steps, since the intermediate is cis -aconitate. (encyclopedia.com)
- ptr aryl hydrocarbon receptor isoform X2 K() bbo:BBOV_III variant erythrocyte surface antigen- (20) xac:XAC aconitate hydratase 1 K() 4 swd:Swoo_ 2-methylisocitrate dehydratase, Fe/S-depe K fy2bQ+OrbvJVQf8As3gb79XLusBu9/G7Paux0Ayfrt/47+i38ZdlYjkl3 J6S6S6RakKf6RdeG4J+p+lbWX4X4X4X4X4X4X4X4N/D7C/BO+WmxX1P0ra2c. (telegra.ph)
- An enzyme that catalyzes the reversible hydration of cis-aconitate to yield citrate or isocitrate. (bvsalud.org)
- Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. (nih.gov)
- It is an enzyme that catalyzes the interconversion of citrate to isocitrate via cis-aconitate in the second step of the TCA cycle. (nih.gov)