Cysteine Dioxygenase
Dioxygenases
Oxygenases
Taurine
Amino Acids, Sulfur
Sulfinic Acids
4-Hydroxyphenylpyruvate Dioxygenase
Catechol 2,3-Dioxygenase
Protocatechuate-3,4-Dioxygenase
Catechol 1,2-Dioxygenase
Carboxy-Lyases
Tryptophan Oxygenase
Liver
Homogentisate 1,2-Dioxygenase
Effects of nonsulfur and sulfur amino acids on the regulation of hepatic enzymes of cysteine metabolism. (1/64)
To determine the role of nonsulfur vs. sulfur amino acids in regulation of cysteine metabolism, rats were fed a basal diet or diets supplemented with a mixture of nonsulfur amino acids (AA), sulfur amino acids (SAA), or both for 3 wk. Hepatic cysteine-sulfinate decarboxylase (CSDC), cysteine dioxygenase (CDO), and gamma-glutamylcysteine synthetase (GCS) activity, concentration, and mRNA abundance were measured. Supplementation with AA alone had no effect on any of these measures. Supplementation of the basal diet with SAA, with or without AA, resulted in a higher CDO concentration (32-45 times basal), a lower CSDC mRNA level (49-64% of basal), and a lower GCS-heavy subunit mRNA level (70-76%). The presence of excess SAA and AA together resulted in an additional type of regulation: a lower specific activity of all three enzymes was observed in rats fed diets with an excess of AA and SAA. Both SAA and AA played a role in regulation of these three enzymes of cysteine metabolism, but SAA had the dominant effects, and effects of AA were not observed in the absence of SAA. (+info)Human cysteine dioxygenase gene: structural organization, tissue-specific expression and downregulation by phorbol 12-myristate 13-acetate. (2/64)
The organization of the human cysteine dioxygenase (CDO) gene was found to be similar to its rat counterpart, and the location of the introns in the protein structure was identical to the rat CDO gene. The major transcription start site, identified by primer extension, was located 260 bp upstream from the ATG codon. The sequence of the 5'-immediate upstream region was highly conserved between the human and rat CDO genes. The putative promoter region contained a TATA-box-like sequence, and many putative cis-acting elements including HNF5, GRE, TRE, CRE, CArG box, ARE, MBS, and NF-kB. A Northern blot analysis revealed that CDO mRNA was strongly expressed in the liver and placenta, and weakly in the heart, brain and pancreas. CDO mRNA was also detected in human hepatoblastoma HepG2 cells. The CDO mRNA level in HepG2 cells was decreased after 2 h and reached a minimum 6 h-8 h after a phorbol 12-myristate 13-acetate (PMA) treatment, and then gradually returned to the basal level. (+info)C/EBPbeta, when expressed from the C/ebpalpha gene locus, can functionally replace C/EBPalpha in liver but not in adipose tissue. (3/64)
Knockout of C/EBPalpha causes a severe loss of liver function and, subsequently, neonatal lethality in mice. By using a gene replacement approach, we generated a new C/EBPalpha-null mouse strain in which C/EBPbeta, in addition to its own expression, substituted for C/EBPalpha expression in tissues. The homozygous mutant mice C/ebpalpha(beta/beta) are viable and fertile and show none of the overt liver abnormalities found in the previous C/EBPalpha-null mouse line. Levels of hepatic PEPCK mRNA are not different between C/ebpalpha(beta/beta) and wild-type mice. However, despite their normal growth rate, C/ebpalpha(beta/beta) mice have markedly reduced fat storage in their white adipose tissue (WAT). Expression of two adipocyte-specific factors, adipsin and leptin, is significantly reduced in the WAT of C/ebpalpha(beta/beta) mice. In addition, expression of the non-adipocyte-specific genes for transferrin and cysteine dioxygenase is reduced in WAT but not in liver. Our study demonstrates that when expressed from the C/ebpalpha gene locus, C/EBPbeta can act for C/EBPalpha to maintain liver functions during development. Moreover, our studies with the C/ebpalpha(beta/beta) mice provide new insights into the nonredundant functions of C/EBPalpha and C/EBPbeta on gene regulation in WAT. (+info)Cysteine regulates expression of cysteine dioxygenase and gamma-glutamylcysteine synthetase in cultured rat hepatocytes. (4/64)
Rat hepatocytes cultured for 3 days in basal medium expressed low levels of cysteine dioxygenase (CDO) and high levels of gamma-glutamylcysteine synthetase (GCS). When the medium was supplemented with 2 mmol/l methionine or cysteine, CDO activity and CDO protein increased by >10-fold and CDO mRNA increased by 1.5- or 3.2-fold. In contrast, GCS activity decreased to 51 or 29% of basal, GCS heavy subunit (GCS-HS) protein decreased to 89 or 58% of basal, and GCS mRNA decreased to 79 or 37% of basal for methionine or cysteine supplementation, respectively. Supplementation with cysteine consistently yielded responses of greater magnitude than did supplementation with an equimolar amount of methionine. Addition of propargylglycine to inhibit cystathionine gamma-lyase activity and, hence, cysteine formation from methionine prevented the effects of methionine, but not those of cysteine, on CDO and GCS expression. Addition of buthionine sulfoximine to inhibit GCS, and thus block glutathione synthesis from cysteine, did not alter the ability of methionine or cysteine to increase CDO. GSH concentration was not correlated with changes in either CDO or GCS-HS expression. The effectiveness of cysteine was equivalent to or greater than that of its precursors (S-adenosylmethionine, cystathionine, homocysteine) or metabolites (taurine, sulfate). Taken together, these results suggest that cysteine itself is an important cellular signal for upregulation of CDO and downregulation of GCS. (+info)The aetiology of idiopathic Parkinson's disease. (5/64)
Agents potentially involved in the aetiology of idiopathic Parkinson's disease are discussed. These include factors regulating dopaminergic neurogenesis (Nurr 1, Ptx-3, and Lmx1b) and related proteins, together with genes involved in familial Parkinson's disease (alpha synuclein, parkin, and ubiquitin carboxy terminal hydroxylase L1), and endogenous and environmental agents. (+info)Enzymes and metabolites of cysteine metabolism in nonhepatic tissues of rats show little response to changes in dietary protein or sulfur amino acid levels. (6/64)
In liver, cysteine dioxygenase (CDO), cysteinesulfinate decarboxylase (CSD), and gamma-glutamylcysteine synthetase (GCS) play important regulatory roles in the metabolism of cysteine to sulfate, taurine and glutathione. Because glutathione is released by the liver and degraded by peripheral tissues that express gamma-glutamyl transpeptidase, some peripheral tissues may be exposed to relatively high concentrations of cysteine. Rats were fed diets that contained low, moderate or high concentrations of protein or supplemental cysteine or methionine for 2 wk, and CDO, CSD and GCS activities, concentrations and mRNA levels and the concentrations of cysteine, taurine and glutathione were measured in liver, kidney, lung and brain. All three enzymes in liver responded to the differences in dietary protein or sulfur amino acid levels, but only CSD in kidney and none of the three enzymes in lung and brain responded. Renal CSD activity was twice as much in rats fed the low protein diet as in rats fed the other diets. Changes in renal CSD activity were correlated with changes in CSD concentration. Some significant differences in cysteine concentration in kidney and lung and glutathione and taurine concentrations in kidney were observed, with higher concentrations in rats fed higher levels of protein or sulfur amino acids. In liver, the changes in cysteine level were consistent with cysteine-mediated regulation of hepatic CDO activity, and changes in taurine level were consistent with predicted changes in cysteine catabolism due to the changes in cysteine concentration and CDO activity. Changes in renal and lung cysteine, taurine or glutathione concentrations were not associated with a similar pattern of change in CDO, CSD or GCS activity. Overall, the results confirm the importance of the liver in the maintenance of cysteine homeostasis. (+info)Functional characterization and regulation of the taurine transporter and cysteine dioxygenase in human hepatoblastoma HepG2 cells. (7/64)
We investigated the characterization and the regulation of TAUT (taurine transporter) and CDO (cysteine dioxygenase), one of the key enzymes of taurine biosynthesis, in human hepatoblastoma HepG2 cells. The activity of TAUT in the HepG2 cells was evaluated by means of a sodium- and chloride-dependent high-affinity transport system, the characteristics of which were similar to those of the beta amino-acid-specific taurine transport system described previously for various tissues [Uchida, Kwon, Yamauchi, Preston, Marumo and Handler (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 8230-8234; Ramamoorthy, Leibach, Mahesh, Han, Yang-Feng, Blakely and Ganapathy (1994) Biochem. J. 300, 893-900; and Satsu, Watanabe, Arai and Shimizu (1997) J. Biochem. (Tokyo) 121, 1082-1087]. By culturing in a hypertonic medium, the intracellular taurine content of HepG2 cells was markedly increased. Under hypertonic conditions, the activity of TAUT was up-regulated, and the results of the kinetic analysis suggested that this up-regulation was associated with an increase in the amount of TAUT. The expression level of TAUT mRNA was markedly higher than that of the control cells. The expression level of CDO mRNA was also up-regulated under the hypertonic conditions. Culturing the cells in a taurine-rich medium resulted in both the activity of TAUT and the expression level of TAUT mRNA being down-regulated in HepG2 cells. On the other hand, the expression level of CDO mRNA was not affected under a taurine-rich condition. The present results show that both TAUT and CDO were co-operatively regulated in response to hypertonicity, but did not co-operatively respond to the change in extracellular taurine concentration. Generally, the TAUT and taurine biosynthetic enzymes have independent regulatory systems, but under certain conditions, they could be regulated in harmony with each other. (+info)Cysteine is the metabolic signal responsible for dietary regulation of hepatic cysteine dioxygenase and glutamate cysteine ligase in intact rats. (8/64)
Cysteine, rather than a precursor or metabolite of cysteine, appears to mediate the upregulation of cysteine dioxygenase (CDO) and the downregulation of glutamate cysteine ligase (GCL) in cultured primary rat hepatocytes. However, similar experiments in intact rats have not been performed to confirm in vivo that changes in hepatic cysteine levels are associated with the regulation of CDO or GCL activity. Therefore, rats were fed a low protein basal diet (100 g casein/kg diet) with or without supplemental sulfur amino acids (8 g cystine, 9 g homocystine or 10 g methionine/kg diet) and with or without propargylglycine (PPG, 1 mmol/kg), an irreversible inhibitor of cystathionine gamma-lyase. Rats were fed the assigned diet for 2 full days and up until the mid-point of the dark cycle on d 3, at which time they were killed for collection of liver. Rats fed the PPG-containing diets had hepatic cystathionine gamma-lyase activities that were approximately 16% of the uninhibited level. PPG treatment reduced CDO activity by 50 and 54%, increased GCL activity by 41 and 61% and lowered total cysteine concentration by 33 and 64% in liver of the homocystine and methionine-supplemented groups, respectively, but not in the cystine-supplemented groups or unsupplemented groups. Glutathione levels were not affected by PPG treatment in any groups. These experiments are consistent with a role for cysteine, rather than a precursor or metabolite of cysteine, in the metabolic signaling responsible for diet-induced regulation of CDO and GCL. (+info)Cysteine dioxygenase (CDO) is an enzyme that catalyzes the conversion of the amino acid L-cysteine to L-cysteinesulfinic acid, which is the first step in the catabolism of L-cysteine. This reaction also generates molecular oxygen as a byproduct. CDO plays important roles in various biological processes such as neurotransmitter biosynthesis and oxidative stress response. It exists as two isoforms, CDO1 and CDO2, which are encoded by separate genes and have distinct tissue distributions and functions.
Dioxygenases are a class of enzymes that catalyze the incorporation of both atoms of molecular oxygen (O2) into their substrates. They are classified based on the type of reaction they catalyze and the number of iron atoms in their active site. The two main types of dioxygenases are:
1. Intradiol dioxygenases: These enzymes cleave an aromatic ring by inserting both atoms of O2 into a single bond between two carbon atoms, leading to the formation of an unsaturated diol (catechol) intermediate and the release of CO2. They contain a non-heme iron(III) center in their active site.
An example of intradiol dioxygenase is catechol 1,2-dioxygenase, which catalyzes the conversion of catechol to muconic acid.
2. Extradiol dioxygenases: These enzymes cleave an aromatic ring by inserting one atom of O2 at a position adjacent to the hydroxyl group and the other atom at a more distant position, leading to the formation of an unsaturated lactone or cyclic ether intermediate. They contain a non-heme iron(II) center in their active site.
An example of extradiol dioxygenase is homogentisate 1,2-dioxygenase, which catalyzes the conversion of homogentisate to maleylacetoacetate in the tyrosine degradation pathway.
Dioxygenases play important roles in various biological processes, including the metabolism of aromatic compounds, the biosynthesis of hormones and signaling molecules, and the detoxification of xenobiotics.
Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.
Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.
Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.
Oxygenases are a class of enzymes that catalyze the incorporation of molecular oxygen (O2) into their substrates. They play crucial roles in various biological processes, including the biosynthesis of many natural products, as well as the detoxification and degradation of xenobiotics (foreign substances).
There are two main types of oxygenases: monooxygenases and dioxygenases. Monooxygenases introduce one atom of molecular oxygen into a substrate while reducing the other to water. An example of this type of enzyme is cytochrome P450, which is involved in drug metabolism and steroid hormone synthesis. Dioxygenases, on the other hand, incorporate both atoms of molecular oxygen into their substrates, often leading to the formation of new carbon-carbon bonds or the cleavage of existing ones.
It's important to note that while oxygenases are essential for many life-sustaining processes, they can also contribute to the production of harmful reactive oxygen species (ROS) during normal cellular metabolism. An imbalance in ROS levels can lead to oxidative stress and damage to cells and tissues, which has been linked to various diseases such as cancer, neurodegeneration, and cardiovascular disease.
Taurine is an organic compound that is widely distributed in animal tissues. It is a conditionally essential amino acid, meaning it can be synthesized by the human body under normal circumstances, but there may be increased requirements during certain periods such as infancy, infection, or illness. Taurine plays important roles in various physiological functions, including bile salt formation, membrane stabilization, neuromodulation, and antioxidation. It is particularly abundant in the brain, heart, retina, and skeletal muscles. In the human body, taurine is synthesized from the amino acids cysteine and methionine with the aid of vitamin B6.
Taurine can also be found in certain foods like meat, fish, and dairy products, as well as in energy drinks, where it is often added as a supplement for its potential performance-enhancing effects. However, there is ongoing debate about the safety and efficacy of taurine supplementation in healthy individuals.
Sulfur-containing amino acids are a type of amino acid that contain sulfur atoms in their side chains. There are three sulfur-containing amino acids that are considered essential for human health: methionine, cysteine, and homocysteine.
Methionine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. It contains a sulfur atom in its side chain and plays important roles in various biological processes, including methylation reactions, protein synthesis, and detoxification.
Cysteine is a semi-essential amino acid, which means that it can be synthesized by the human body under normal conditions but may become essential during periods of growth or illness. It contains a sulfhydryl group (-SH) in its side chain, which allows it to form disulfide bonds with other cysteine residues and contribute to the stability and structure of proteins.
Homocysteine is a non-proteinogenic amino acid that is derived from methionine metabolism. It contains a sulfur atom in its side chain and has been linked to various health problems, including cardiovascular disease, when present at elevated levels in the blood.
Other sulfur-containing amino acids include taurine, which is not incorporated into proteins but plays important roles in bile acid conjugation, antioxidant defense, and neuromodulation, and cystathionine, which is an intermediate in methionine metabolism.
I apologize for any confusion, but "Sulfinic Acids" is not a term used in medical definitions. It is a term from the field of chemistry. Sulfinic acids are organic compounds that contain a functional group with the formula RSO(O)H, where R represents an alkyl or aryl group. They are important intermediates in organic synthesis and can be found in some natural sources. If you have any questions related to medical terminology or concepts, I would be happy to help!
4-Hydroxyphenylpyruvate dioxygenase (HPPD) is an enzyme that is involved in the catabolism of aromatic amino acids such as tyrosine. The gene for HPPD is located on human chromosome 12q24.11.
The HPPD enzyme catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisate, which is then further metabolized in the catabolic pathway leading to fumarate and acetoacetate. Deficiencies in HPPD activity have been associated with certain genetic disorders such as tyrosinemia type III, which can result in neurological symptoms and developmental delays.
In addition to its role in normal metabolism, HPPD has also been identified as a target for herbicides that inhibit the enzyme's activity, leading to the accumulation of 4-hydroxyphenylpyruvate and other toxic intermediates that can disrupt plant growth and development.
Sulfhydryl compounds, also known as thiol compounds, are organic compounds that contain a functional group consisting of a sulfur atom bonded to a hydrogen atom (-SH). This functional group is also called a sulfhydryl group. Sulfhydryl compounds can be found in various biological systems and play important roles in maintaining the structure and function of proteins, enzymes, and other biomolecules. They can also act as antioxidants and help protect cells from damage caused by reactive oxygen species. Examples of sulfhydryl compounds include cysteine, glutathione, and coenzyme A.
Catechol 2,3-dioxygenase is an enzyme that catalyzes the conversion of catechols to muconic acids as part of the meta-cleavage pathway in the breakdown of aromatic compounds. This enzyme plays a crucial role in the degradation of various aromatic hydrocarbons, including lignin and environmental pollutants such as polycyclic aromatic hydrocarbons (PAHs) and polychlorinated biphenyls (PCBs). Catechol 2,3-dioxygenase requires Fe(II) as a cofactor for its activity. The gene that encodes this enzyme is often used as a bioremediation marker to monitor the degradation of aromatic pollutants in the environment.
Protocatechuate-3,4-dioxygenase is an enzyme that catalyzes the ortho-cleavage of protocatechuate, an aromatic compound, in the meta-cleavage pathway of aerobic bacterial catabolism. The enzyme requires Fe(II) as a cofactor and has two subunits: alpha and beta. The alpha subunit contains the catalytic site and is responsible for binding and cleaving protocatechuate, while the beta subunit serves a regulatory role.
The reaction catalyzed by protocatechuate-3,4-dioxygenase is as follows:
Protocatechuate + O2 -> 3-carboxy-cis,cis-muconate
This enzyme plays an important role in the degradation of various aromatic compounds and is widely distributed in bacteria, fungi, and plants. It has been studied extensively as a model system for understanding the mechanisms of aromatic ring cleavage and has potential applications in bioremediation and industrial biotechnology.
Ferrous compounds are inorganic substances that contain iron (Fe) in its +2 oxidation state. The term "ferrous" is derived from the Latin word "ferrum," which means iron. Ferrous compounds are often used in medicine, particularly in the treatment of iron-deficiency anemia due to their ability to provide bioavailable iron to the body.
Examples of ferrous compounds include ferrous sulfate, ferrous gluconate, and ferrous fumarate. These compounds are commonly found in dietary supplements and multivitamins. Ferrous sulfate is one of the most commonly used forms of iron supplementation, as it has a high iron content and is relatively inexpensive.
It's important to note that ferrous compounds can be toxic in large doses, so they should be taken under the guidance of a healthcare professional. Overdose can lead to symptoms such as nausea, vomiting, diarrhea, abdominal pain, and potentially fatal consequences if left untreated.
Catechol 1,2-dioxygenase is an enzyme that catalyzes the conversion of catechols to muconic acids as part of the meta-cleavage pathway in the breakdown of aromatic compounds in bacteria. The enzyme requires iron as a cofactor and functions by cleaving the aromatic ring between the two hydroxyl groups in the catechol molecule. This reaction is an important step in the degradation of various environmental pollutants, such as polychlorinated biphenyls (PCBs) and lignin, by certain bacterial species.
Carboxy-lyases are a class of enzymes that catalyze the removal of a carboxyl group from a substrate, often releasing carbon dioxide in the process. These enzymes play important roles in various metabolic pathways, such as the biosynthesis and degradation of amino acids, sugars, and other organic compounds.
Carboxy-lyases are classified under EC number 4.2 in the Enzyme Commission (EC) system. They can be further divided into several subclasses based on their specific mechanisms and substrates. For example, some carboxy-lyases require a cofactor such as biotin or thiamine pyrophosphate to facilitate the decarboxylation reaction, while others do not.
Examples of carboxy-lyases include:
1. Pyruvate decarboxylase: This enzyme catalyzes the conversion of pyruvate to acetaldehyde and carbon dioxide during fermentation in yeast and other organisms.
2. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): This enzyme is essential for photosynthesis in plants and some bacteria, as it catalyzes the fixation of carbon dioxide into an organic molecule during the Calvin cycle.
3. Phosphoenolpyruvate carboxylase: Found in plants, algae, and some bacteria, this enzyme plays a role in anaplerotic reactions that replenish intermediates in the citric acid cycle. It catalyzes the conversion of phosphoenolpyruvate to oxaloacetate and inorganic phosphate.
4. Aspartate transcarbamylase: This enzyme is involved in the biosynthesis of pyrimidines, a class of nucleotides. It catalyzes the transfer of a carboxyl group from carbamoyl aspartate to carbamoyl phosphate, forming cytidine triphosphate (CTP) and fumarate.
5. Urocanase: Found in animals, this enzyme is involved in histidine catabolism. It catalyzes the conversion of urocanate to formiminoglutamate and ammonia.
Tryptophan oxygenase, also known as tryptophan 2,3-dioxygenase (TDO) or tryptophan pyrrolase, is an enzyme that catalyzes the breakdown of the essential amino acid tryptophan. This enzyme requires molecular oxygen and plays a crucial role in regulating tryptophan levels within the body.
The reaction catalyzed by tryptophan oxygenase involves the oxidation of the indole ring of tryptophan, leading to the formation of N-formylkynurenine. This metabolite is further broken down through several enzymatic steps to produce other biologically active compounds, such as kynurenine and niacin (vitamin B3).
Tryptophan oxygenase activity is primarily found in the liver and is induced by various factors, including corticosteroids, cytokines, and tryptophan itself. The regulation of this enzyme has implications for several physiological processes, such as immune response, neurotransmitter synthesis, and energy metabolism. Dysregulation of tryptophan oxygenase activity can contribute to the development of various pathological conditions, including neurological disorders and cancer.
The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:
1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.
Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.
Homogentisate 1,2-dioxygenase (HGD) is an enzyme that plays a crucial role in the catabolism of tyrosine, an aromatic amino acid. This enzyme is involved in the third step of the tyrosine degradation pathway, also known as the tyrosine breakdown or catabolic pathway.
The homogentisate 1,2-dioxygenase enzyme catalyzes the conversion of homogentisic acid (HGA) into maleylacetoacetic acid. This reaction involves the cleavage of the aromatic ring of HGA and the introduction of oxygen, hence the name 'dioxygenase.' The reaction can be summarized as follows:
Homogentisate + O2 → Maleylacetoacetate
Deficiency or dysfunction in homogentisate 1,2-dioxygenase leads to a rare genetic disorder called alkaptonuria. In this condition, the body cannot break down tyrosine properly, resulting in an accumulation of HGA and its oxidation product, alkapton, which can cause damage to connective tissues and joints over time.
Cysteine dioxygenase
Cysteine dioxygenase type 1
Sulfinic acid
Cysteine metabolism
Alpha-ketoglutarate-dependent hydroxylases
Hypotaurine
Cystathionine
Dioxygenase
Chromosome 5
List of MeSH codes (D08)
Insect-based pet food
List of EC numbers (EC 1)
Rosemary Waring
CDO
Taurine
Cysteine sulfinic acid
Aromatic-ring-hydroxylating dioxygenases
Ferredoxin
EGF-like domain
Trace metal stable isotope biogeochemistry
Rieske protein
Metalloprotein
Chromosome 7
Chromosome 12
Arachidonate 5-lipoxygenase
Isopenicillin N synthase
TET enzymes
O-GlcNAc
Iron-binding proteins
List of examples of convergent evolution
Cysteine dioxygenase - Wikipedia
DNA methylation dynamics underlie metamorphic gene regulation programs in Xenopus tadpole brain
Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants - Ludwig Cancer Research
Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants - Target Discovery Institute
Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants - NDM Research Building
Ferroptosis: past, present and future | Cell Death & Disease
sulfur compound catabolic process - Ontology Report - Rat Genome Database
SCOP 1.73: Domain d2atfa1: 2atf A:5-190
Pantothenate Kinase-Associated Neurodegeneration (PKAN): Practice Essentials, Background, Etiology
Publikationen • AG Dau • Physik
Prognostic value and potential function of splicing events in prostate adenocarcinoma
Bioscience, Biotechnology, and Biochemistry
Proposal summaries | Avon Longitudinal Study of Parents and Children
News | Libertas Academica
Biosulfur Analysis -SulfoBiotics- HSip-1 | CAS 1346220-52-7(free base) Dojindo
Mass spectrometry-based approaches to explore metabolism regulating ferroptosis
Cannabis Compound Database: Showing Compound Card for L-Cysteine (CDB004848)
Bio2Vec
SZGR2
Myeloid-Derived Suppressor Cells | Cancer Immunology Research | American Association for Cancer Research
Michael J. Maroney: H-index & Awards - Academic Profile | Research.com
The diagnostic value of circulating tumor DNA in hepatitis B virus induced hepatocellular carcinoma: a systematic review and...
HALLMARK XENOBIOTIC METABOLISM
Tadhg Begley - Texas A&M University (TAMU) Scholar
Anticholesterolemic and Antiatherogenic Effects of Taurine Supplementation is Model Dependent | IntechOpen
PHYRE Protein Fold Recognition Server
Publications | Page 9 | Department of Anesthesiology
Sulfinic acid4
- Cysteine dioxygenase (CDO) is a non-heme iron enzyme that catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate). (wikipedia.org)
- It oxidizes cysteine to the corresponding sulfinic acid by activation of dioxygen, although the exact mechanism of the reaction is still unclear. (wikipedia.org)
- CDO oxidizes to cysteine sulfinic acid (which exists predominantly in the anionic sulfinate form in vivo). (wikipedia.org)
- Cysteine dioxygenase (CDO) catalyzes the oxidation of cysteine to cysteine sulfinic acid, which is the first major step in cysteine catabolism in mammalian tissues. (umass.edu)
CDO11
- Using pharmacological unmasking microarray, we identified promoter DNA methylation of cysteine dioxygenase 1 (CDO1) gene in human cancer. (nih.gov)
Oxidase1
- Additionally, after treatment of TE 671 cells with 0.005-0.5 μM 4- n -octylphenol, bis(2-ethylhexyl)phthalate, and diisodecyl phthalate, real-time RT-PCR showed dose-dependent decreases in the steady-state mRNA levels of cysteine dioxygenase type I, sulfite oxidase, and 3′-phosphate 5′-phosphosulfate synthase I. (nih.gov)
Enzymes3
- Presented here are the results of O2-dependent 2-mercaptoaniline reaction using two different thiol dioxygenase enzymes mouse CDO and 3-mercaptopropionic acid dioxygenase isolated from Azotobacter vinelandii. (genscript.com)
- It has been shown that children with food intolerance are slow or null metabolisers of cysteine dioxygenase which is one of the CYP450 enzymes (Breakey 2004), the same enzyme system that cause problems with psychiatric drug intolerance. (fedup.com.au)
- Acireductone dioxygenases (ARDs) are enzymes involved in the methionine recycle pathway. (umass.edu)
Pathways4
- An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways. (nih.gov)
- The existence of two pathways for cysteine synthesis might ensure its participation in the formation of proteins, heavy metal detoxification, and the sulfide-binding function of haemoglobin. (biomedcentral.com)
- We elucidated several molecular pathways of sulfate activation, cysteine and cholesterol synthesis, and trehalose metabolism. (biomedcentral.com)
- Contrary to the previous analysis, two pathways for cysteine synthesis and the cycloartenol-C-24-methyltransferase gene were identified in animals for the first time. (biomedcentral.com)
Oxidation2
- Furthermore, research has shown that cysteamine, a structurally similar molecule to cysteine, enhances cysteine oxidation but is not a substrate. (wikipedia.org)
- One model postulates that the iron-sensing capacity of the 73d is based on site-specific oxidation of conserved cysteine residues upon direct iron binding [ 11 ]. (biomedcentral.com)
Glutamate-cystei3
- Ten Eleven Translocation-1 knockdown decreased 5-hydroxymethylcytosine formation following hydroquinone exposure as well as the induction of glutamate-cysteine ligase catalytic subunit and 14-3-3σ. (nih.gov)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Glutamate Cysteine Ligase, Modifier Subunit (GCLM) in Tissue homogenates and other biological fluids. (isogem.org)
- Description: A sandwich ELISA kit for detection of Glutamate Cysteine Ligase, Modifier Subunit from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (isogem.org)
Intracellular6
- CDO plays an important role in cysteine catabolism, regulating intracellular levels of cysteine and responding changes in cysteine availability. (wikipedia.org)
- Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range. (nih.gov)
- Using DL-propargylglycine, a particular irreversible CSE inhibitor [15], CSE offers been shown to become important in rat liver organ, kidney and cultured hepatocytes for a satisfactory way to obtain cysteine to synthesize glutathione [11,16,17], a significant intracellular antioxidant that protects cells from oxidative tension. (health-ground.com)
- Cysteine can be used for biosynthesis of taurine also, probably the most abundant intracellular free of charge amino acid, which includes numerous biological functions and may become an antioxidant also. (health-ground.com)
- However, due to its reactive thiol side chain, elevated levels of intracellular cysteine can be toxic and therefore need to be rapidly eliminated from the cellular milieu. (microbialcell.com)
- Overexpressing the high affinity cysteine transporter, YCT1 , enabled yeast cells to rapidly accumulate high levels of intracellular cysteine. (microbialcell.com)
Biosynthesis1
- Microarray based gene expression studies revealed the upregulation of arginine/ornithine biosynthesis a few hours after the cysteine overload, and suggest that the non-toxic, non-reactive thiol based metabolic products are eventually utilized for amino acid and polyamine biogenesis, thereby enabling cell growth. (microbialcell.com)
Metabolism2
- CDO is responsible for the first major step in metabolism of cysteine. (wikipedia.org)
- In human cysteine metabolism, L-cysteine is consumed in several ways as shown below. (dadamo.com)
1.13.11.201
- It also has some activity as EC 1.13.11.20 , cysteine dioxygenase, and can perform the reaction of EC 1.14.99.50 , γ-glutamyl hercynylcysteine sulfoxide synthase, albeit with low activity [4]. (enzyme-database.org)
Catabolism1
- Indoleamine 2,3-dioxygenase (IDO) is a heme-containing dioxygenase that catalyses the first and rate-limiting step in the kynurenine (Kyn) pathway of L-tryptophan (L-Trp)catabolism. (edu.au)
Sulfur4
- Furthermore, crystal structures show the amino nitrogen and thiolate sulfur of cysteine coordinated to the iron in addition to a single water molecule (see figure). (wikipedia.org)
- One proposed mechanism, supported by computational and spectroscopic studies, involves O2 binding cis to a thiolate to form reactive iron (III)-superoxo species (A), which then attacks the bound sulfur of cysteine to form a four-membered ring structure (B). Heterolytic O-O bond cleavage then affords a high-valent iron (IV) oxo intermediate (C), which transfers the second oxygen to sulfur. (wikipedia.org)
- The investigation of two non-heme iron dioxygenases with sulfur-containing substrates is reported along with studies of seleno-compounds by gas chromatography with atomic emission detection (GC-AED). (umass.edu)
- Moreover, sulfide can serve directly as a sulfur source for cysteine synthesis in L. luymesi . (biomedcentral.com)
Metabolites2
- In particular, the metabolites 2-aminobutyric acid, cysteine, alanine, and tyrosine all displayed areas under the receiver operating characteristic curve were above 0.9. (biomedcentral.com)
- Additional metabolites include benzoquinone, multiple glutathione conjugates, and N -acetyl cysteine conjugates. (nih.gov)
Taurine3
- The role of CDO may vary between cell types as it can either be used primarily for taurine or sulfate production or for degradation of cysteine. (wikipedia.org)
- CDO is also regulated in adipose tissue, where high cysteine levels cause increased hypotaurine/taurine production. (wikipedia.org)
- Of its part as the precursor of such bioactive substances Irrespective, cysteine itself could up-regulate the manifestation of cysteine dioxygenase that mediates taurine creation and down-regulate the manifestation of -glutamylcysteine synthetase, which mediates glutathione creation in cultured rat hepatocytes and intact rats [18,19]. (health-ground.com)
Thiol1
- Thus, cells can handle potentially toxic amounts of cysteine by a combination of thiol trapping, metabolic redistribution to non-reactive thiols and subsequent consumption for anabolism. (microbialcell.com)
1973-19791
- use AMINO ACIDS, BRANCHED-CHAIN 1979, & KETO ACIDS & VALERATES 1973-1979 MH - 3-Hydroxyanthranilate 3,4-Dioxygenase UI - D050561 MN - D8.811.682.690.416.328 MS - An enzyme that catalyzes the conversion of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde. (nih.gov)
Methionine1
- This pathway visualises the conversion of methionine to cysteine, after which it is further metabolised in either an oxidative or non-oxidative manner. (wikipathways.org)
Residues1
- Persulfide Dioxygenase From Acidithiobacillus caldus: Variable Roles of Cysteine Residues and Hydrogen Bond Networks of the Active Site. (tu-darmstadt.de)
Hypotaurine2
- Pour chaque prélèvement, ces étapes ont été réalisées en parallèle avec des milieux supplémentés en hypotaurine (bras « H+ ») ou sans hypotaurine (bras « H- »). Après décongélation, nous avons mesuré la mobilité totale et progressive, la vitalité, l'intégrité de l'acrosome, des marqueurs de la voie de signalisation de la capacitation et la qualité nucléaire. (biomedcentral.com)
- la première à démontrer les effets bénéfiques de la supplémentation en hypotaurine dans les milieux de préparation et de congélation sur la capacité de fécondation des spermatozoïdes humains et leur qualité nucléaire. (biomedcentral.com)
Degradation2
- High cysteine levels inhibit ubiquitinylation, which lowers the rate of proteasomal degradation. (wikipedia.org)
- In mammals and many other organisms, excess cysteine is believed to be primarily eliminated by the cysteine dioxygenase dependent oxidative degradation of cysteine, followed by the removal of the oxidative products. (microbialcell.com)
TET13
- Hydroquinone increases 5-hydroxymethylcytosine formation through ten eleven translocation 1 (TET1) 5-methylcytosine dioxygenase. (nih.gov)
- Ten-eleven translocation methylcytosine dioxygenase 1 (TET1), a CpG island binding protein, can repress gene expression by occupying hypomethylated CpG-rich promoters, and therefore SNCA could be a target for TET1. (einj.org)
- Ten-eleven translocation methylcytosine dioxygenase 1 (TET1) acts as a repressor for α-synuclein gene ( SNCA ). (einj.org)
Indoleamine5
- In this study the expression and purification of recombinant human indoleamine 2,3-dioxygenase (rhIDO) in E. coli(pQE-9-IDO, pREP4) was investigated in order to obtain high quality enzyme in high yields. (edu.au)
- Expression and purification of indoleamine 2,3-dioxygenase -- 3. (edu.au)
- Characterisation of indoleamine 2,3-dioxygenase -- 4. (edu.au)
- Re-incorporation of heme into indoleamine 2,3-dioxygenase -- 5. (edu.au)
- Mutagenesis of indoleamine 2,3-dioxygenase -- 6. (edu.au)
Molecule1
- Organoseleno compounds have been observed, including selenomethionine, and possibly the newly-discovered S-(methylseleno)-cysteine molecule. (umass.edu)
Gene1
- Title: Placental and fetal cysteine dioxygenase gene expression in mouse gestation. (genscript.com)
Type2
- Cysteine Dioxygenase Type 1 Inhibits Osteogenesis by Regulating Wnt Signaling in Primary Mouse Bone Marrow Stromal Cells. (genscript.com)
- Title: Cysteine dioxygenase type 1 promotes adipogenesis via interaction with peroxisome proliferator-activated receptor gamma. (genscript.com)
Metabolite1
- Using targeted metabolite analysis, we observe that cysteine is initially rapidly interconverted to non-reactive cystine in vivo . (microbialcell.com)
Fosfomycin1
- protein_coding" "Cz03g38230.t1","No alias","Chromochloris zofingiensis","Glyoxalase/fosfomycin resistance/dioxygenase domain [Interproscan]. (ntu.edu.sg)
Concentrations2
- Critical regulator of cellular cysteine concentrations. (nih.gov)
- Furthermore, high cysteine concentrations could possibly be neurotoxic and cytotoxic in rats [20,21] and high plasma cysteine concentrations in human beings had been connected with pre-eclampsia, early delivery, low delivery pounds and cardiovascular illnesses [22C24]. (health-ground.com)
Regulator1
- These lines of proof suggest important jobs for CSE as the regulator of cysteine homoeostasis as well as the glutathioneCtaurine rheostat. (health-ground.com)
Catalytic2
- The contribution of individual cysteines towards the overall catalytic properties and stability of the rhIDO was evaluated through mutagenesis studies. (edu.au)
- This study confirms that the Cys to Ala site-directed mutagenesis contributes to the changes in the kinetics of the mutated rhIDO, and that the cysteine moieties of rhIDO are involved in the normal catalytic function of the enzyme. (edu.au)
Cofactor1
- Crosslinking increases efficiency of CDO ten-fold and is regulated by levels of cysteine, an unusual example of protein cofactor formation mediated by substrate (feedforward activation). (wikipedia.org)
Descriptor1
- Homogentisate 1,2-Dioxygenase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
Escherichia1
- protein_coding" "AAC74417","ogt","Escherichia coli","O-6-alkylguanine-DNA:cysteine-protein methyltransferase [Ensembl]. (ntu.edu.sg)
Reaction2
- Overall, the reaction involves addition of O2 to cysteine, which occurs spontaneously without enzyme catalysis. (wikipedia.org)
- Cysteine (Cys) supply is directly related to the rate of GSH synthesis and its concentration represents the rate-limiting step for the first reaction (i.e., the formation of γ-glutamylcysteine). (medscape.com)
Mechanism1
- 2006. Structure and mechanism of mouse cysteine dioxygenase. . (cornell.edu)
Human2
- 3. Cysteine Dioxygenase 1 Mediates Erastin-Induced Ferroptosis in Human gastric cancer Cells. (nih.gov)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Cysteine And Glycine Rich Protein 1 (CSRP1) in Tissue homogenates and other biological fluids. (jemsec.com)
Description1
- Description: A competitive ELISA for quantitative measurement of Rat Cysteine and glycine rich protein 1(CSRP1) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (jemsec.com)
High1
- In particular, CDO responds to changes in dietary cysteine availability and protein intake, maintaining decreased activity with low cysteine levels and increased activity at high levels to prevent cytotoxicity. (wikipedia.org)
Major1
- This graph shows the total number of publications written about "Homogentisate 1,2-Dioxygenase" by people in this website by year, and whether "Homogentisate 1,2-Dioxygenase" was a major or minor topic of these publications. (umassmed.edu)
Role1
- These observations support a role of cysteine in cancer progression, recurrence and chemoresistance. (biomedcentral.com)