An enzyme that catalyzes the conversion of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde. It was formerly characterized as EC 1.13.1.6.
An oxidation product of tryptophan metabolism. It may be a free radical scavenger and a carcinogen.
A metabolite of tryptophan with a possible role in neurodegenerative disorders. Elevated CSF levels of quinolinic acid are correlated with the severity of neuropsychological deficits in patients who have AIDS.
Kynurenine is a metabolic product of the amino acid tryptophan, formed via the kynurenine pathway, and serves as an important intermediate in the biosynthesis of nicotinamide adenine dinucleotide (NAD+) and other neuroactive compounds, while also playing a role in immune response regulation and potential involvement in various neurological disorders.
Non-heme iron-containing enzymes that incorporate two atoms of OXYGEN into the substrate. They are important in biosynthesis of FLAVONOIDS; GIBBERELLINS; and HYOSCYAMINE; and for degradation of AROMATIC HYDROCARBONS.
Benzoic acids, salts, or esters that contain an amino group attached to carbon number 2 or 6 of the benzene ring structure.
Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules.
An NADPH-dependent flavin monooxygenase that plays a key role in the catabolism of TRYPTOPHAN by catalyzing the HYDROXYLATION of KYNURENINE to 3-hydroxykynurenine. It was formerly characterized as EC 1.14.1.2 and EC 1.99.1.5.
Benzoic acid or benzoic acid esters substituted with one or more nitro groups.
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
An enzyme that catalyzes the conversion of 4-hydroxyphenylpyruvate plus oxygen to homogentisic acid and carbon dioxide. EC 1.13.11.27.
Catalyzes the oxidation of catechol to 2-hydroxymuconate semialdehyde in the carbazole and BENZOATE degradation via HYDROXYLATION pathways. It also catalyzes the conversion of 3-methylcatechol to cis, cis-2-hydroxy-6-oxohept-2,4-dienoate in the TOLUENE and XYLENE degradation pathway. This enzyme was formerly characterized as EC 1.13.1.2.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
An enzyme that catalyzes the oxidation of protocatechuate to 3-carboxy-cis-cis-muconate in the presence of molecular oxygen. It contains ferric ion. EC 1.13.11.3.
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.
An enzyme that catalyzes the oxidation of catechol to muconic acid with the use of Fe3+ as a cofactor. This enzyme was formerly characterized as EC 1.13.1.1 and EC 1.99.2.2.
A dioxygenase with specificity for the oxidation of the indoleamine ring of TRYPTOPHAN. It is a LIVER-specific enzyme that is the first and rate limiting enzyme in the kynurenine pathway of TRYPTOPHAN catabolism.
A mononuclear Fe(II)-dependent oxygenase, this enzyme catalyzes the conversion of homogentisate to 4-maleylacetoacetate, the third step in the pathway for the catabolism of TYROSINE. Deficiency in the enzyme causes ALKAPTONURIA, an autosomal recessive disorder, characterized by homogentisic aciduria, OCHRONOSIS and ARTHRITIS. This enzyme was formerly characterized as EC 1.13.1.5 and EC 1.99.2.5.
A group of 1,2-benzenediols that contain the general formula R-C6H5O2.
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.
Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers.

3-Hydroxyanthranilate 3,4-Dioxygenase is an enzyme that catalyzes the chemical reaction:

3-hydroxyanthranilate + O2 -> 2-amino-3-carboxymuconate semialdehyde

This enzyme is involved in the catabolism of tryptophan, an essential amino acid, through the kynurenine pathway. The reaction catalyzed by this enzyme involves the cleavage of the aromatic ring of 3-hydroxyanthranilate and the formation of 2-amino-3-carboxymuconate semialdehyde, which is further metabolized to produce NAD+ and other products. Defects in this enzyme have been associated with certain neurological disorders.

3-Hydroxyanthranilic acid is an intermediate metabolite in the catabolism (breakdown) of tryptophan, an essential amino acid. It is formed from the oxidation of 3-hydroxykynurenine by the enzyme kynureninase. Further breakdown of 3-hydroxyanthranilic acid can lead to the formation of various other metabolites, including quinolinic acid and picolinic acid, which are involved in the synthesis of nicotinamide adenine dinucleotide (NAD+), a coenzyme that plays a crucial role in cellular metabolism.

Abnormal accumulation or dysregulation of 3-hydroxyanthranilic acid has been implicated in several pathological conditions, including neurodegenerative disorders and certain types of cancer. However, more research is needed to fully understand the role of this metabolite in human health and disease.

Quinolinic acid is a metabolite found in the human body, produced during the metabolism of tryptophan, an essential amino acid. It is a component of the kynurenine pathway and acts as a neuroexcitatory chemical in the brain. In excessive amounts, quinolinic acid can lead to neurotoxicity, causing damage to neurons and contributing to several neurological disorders such as Huntington's disease, Alzheimer's disease, Parkinson's disease, AIDS-dementia complex, and multiple sclerosis. It also plays a role in the pathogenesis of psychiatric conditions like schizophrenia and major depressive disorder.

Kynurenine is an organic compound that is produced in the human body as part of the metabolism of the essential amino acid tryptophan. It is an intermediate in the kynurenine pathway, which leads to the production of several neuroactive compounds and NAD+, a coenzyme involved in redox reactions.

Kynurenine itself does not have any known physiological function, but some of its metabolites have been found to play important roles in various biological processes, including immune response, inflammation, and neurological function. For example, the kynurenine pathway produces several neuroactive metabolites that can act as agonists or antagonists at various receptors in the brain, affecting neuronal excitability, synaptic plasticity, and neurotransmission.

Abnormalities in the kynurenine pathway have been implicated in several neurological disorders, including depression, schizophrenia, Alzheimer's disease, and Huntington's disease. Therefore, understanding the regulation of this pathway and its metabolites has become an important area of research in neuroscience and neuropsychopharmacology.

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.

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

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.

Kynurenine 3-Monooxygenase (KMO) is an enzyme that is involved in the metabolism of the amino acid tryptophan. Specifically, it is a key enzyme in the kynurenine pathway, which is the primary route of tryptophan breakdown in mammals.

KMO catalyzes the conversion of L-kynurenine to 3-hydroxykynurenine using molecular oxygen and nicotinamide adenine dinucleotide phosphate (NADPH) as cofactors. This reaction is an important step in the production of several neuroactive metabolites, including quinolinic acid and kynurenic acid, which have been implicated in various neurological disorders such as Alzheimer's disease, Parkinson's disease, and depression.

Inhibition of KMO has been suggested as a potential therapeutic strategy for the treatment of these disorders due to its role in regulating the balance between neuroprotective and neurotoxic kynurenine metabolites.

Nitrobenzoates are a type of organic compound that consists of a benzoate group (a carboxylate derived from benzoic acid) with a nitro group (-NO2) attached to the benzene ring. They are often used in chemical synthesis and have also been studied for their potential medicinal properties, such as their antimicrobial and anti-inflammatory effects. However, they are not commonly used in modern medicine as therapeutic agents.

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

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

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.

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.

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.

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.

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.

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.

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.

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.

Catechols are a type of chemical compound that contain a benzene ring with two hydroxyl groups (-OH) attached to it in the ortho position. The term "catechol" is often used interchangeably with "ortho-dihydroxybenzene." Catechols are important in biology because they are produced through the metabolism of certain amino acids, such as phenylalanine and tyrosine, and are involved in the synthesis of various neurotransmitters and hormones. They also have antioxidant properties and can act as reducing agents. In chemistry, catechols can undergo various reactions, such as oxidation and polymerization, to form other classes of compounds.

"Pseudomonas" is a genus of Gram-negative, rod-shaped bacteria that are widely found in soil, water, and plants. Some species of Pseudomonas can cause disease in animals and humans, with P. aeruginosa being the most clinically relevant as it's an opportunistic pathogen capable of causing various types of infections, particularly in individuals with weakened immune systems.

P. aeruginosa is known for its remarkable ability to resist many antibiotics and disinfectants, making infections caused by this bacterium difficult to treat. It can cause a range of healthcare-associated infections, such as pneumonia, bloodstream infections, urinary tract infections, and surgical site infections. In addition, it can also cause external ear infections and eye infections.

Prompt identification and appropriate antimicrobial therapy are crucial for managing Pseudomonas infections, although the increasing antibiotic resistance poses a significant challenge in treatment.

Environmental biodegradation is the breakdown of materials, especially man-made substances such as plastics and industrial chemicals, by microorganisms such as bacteria and fungi in order to use them as a source of energy or nutrients. This process occurs naturally in the environment and helps to break down organic matter into simpler compounds that can be more easily absorbed and assimilated by living organisms.

Biodegradation in the environment is influenced by various factors, including the chemical composition of the substance being degraded, the environmental conditions (such as temperature, moisture, and pH), and the type and abundance of microorganisms present. Some substances are more easily biodegraded than others, and some may even be resistant to biodegradation altogether.

Biodegradation is an important process for maintaining the health and balance of ecosystems, as it helps to prevent the accumulation of harmful substances in the environment. However, some man-made substances, such as certain types of plastics and industrial chemicals, may persist in the environment for long periods of time due to their resistance to biodegradation, leading to negative impacts on wildlife and ecosystems.

In recent years, there has been increasing interest in developing biodegradable materials that can break down more easily in the environment as a way to reduce waste and minimize environmental harm. These efforts have led to the development of various biodegradable plastics, coatings, and other materials that are designed to degrade under specific environmental conditions.

PhD thesis named Computational studies of Iron dependent dioxygenases, under mentor prof. Sanja Tomić, was defended in 2014th. ... 89 (4): 619-627. doi:10.1111/cbdd.12887. PMID 27754592. S2CID 21167604. Brkić, Hrvoje; Ivković, Ana; Kasabašić, Mladen; Poje ... 34 (4): 578-584. doi:10.1038/jcbfm.2014.7. ISSN 0271-678X. PMC 3982101. PMID 24473483. Brkić, Hrvoje; Buongiorno, Daniela; ... 88 (3): 297-306. doi:10.5562/cca2685. ISSN 0011-1643. Vrselja, Zvonimir; Brkic, Hrvoje; Mrdenovic, Stefan; Radic, Radivoje; ...
3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) is an enzyme encoded by the HAAO gene that catalyzes the chemical reaction ... The systematic name of this enzyme class is 3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing). Other names in ... 2-amino-3-carboxymuconate semialdehyde Thus, the two substrates of this enzyme are 3-hydroxyanthranilate and O2, whereas its ... 3-hydroxyanthranilic acid oxidase and 3HAO. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron. ...
... dioxygenases MeSH D08.811.682.690.416.277 - catechol 1,2-dioxygenase MeSH D08.811.682.690.416.305 - catechol 2,3-dioxygenase ... 2-oxoglutarate 5-dioxygenase MeSH D08.811.682.690.708.673 - procollagen-proline dioxygenase MeSH D08.811.682.690.708.715 - ... MeSH D08.811.682.690.416.319 - cysteine dioxygenase MeSH D08.811.682.690.416.326 - homogentisate 1,2-dioxygenase MeSH D08.811. ... gamma-butyrobetaine dioxygenase MeSH D08.811.682.690.708.410 - heme oxygenase (decyclizing) MeSH D08.811.682.690.708.410.500 - ...
... dioxygenase EC 1.14.11.4: procollagen-lysine 5-dioxygenase EC 1.14.11.5: Now included with EC 1.14.11.6 thymine dioxygenase EC ... peptide-aspartate β-dioxygenase EC 1.14.11.17: taurine dioxygenase EC 1.14.11.18: phytanoyl-CoA dioxygenase EC 1.14.11.19: Now ... dioxygenase EC 1.14.11.12: gibberellin-44 dioxygenase EC 1.14.11.13: gibberellin 2β-dioxygenase EC 1.14.11.14: Now EC 1.14. ... persulfide dioxygenase EC 1.13.11.19: cysteamine dioxygenase EC 1.13.11.20: cysteine dioxygenase EC 1.13.11.21: Now EC 1.14. ...
PhD thesis named Computational studies of Iron dependent dioxygenases, under mentor prof. Sanja Tomić, was defended in 2014th. ... 89 (4): 619-627. doi:10.1111/cbdd.12887. PMID 27754592. S2CID 21167604. Brkić, Hrvoje; Ivković, Ana; Kasabašić, Mladen; Poje ... 34 (4): 578-584. doi:10.1038/jcbfm.2014.7. ISSN 0271-678X. PMC 3982101. PMID 24473483. Brkić, Hrvoje; Buongiorno, Daniela; ... 88 (3): 297-306. doi:10.5562/cca2685. ISSN 0011-1643. Vrselja, Zvonimir; Brkic, Hrvoje; Mrdenovic, Stefan; Radic, Radivoje; ...
No candidates for nbaC: 3-hydroxyanthranilate 3,4-dioxygenase. GapMind classifies a step as low confidence even if it does not ...
3hydroxyanthranilate oxygenase 3hydroxyanthranilic kiseline dioxygenase; Biosynthesis od nicotinic ki ... Lanac Lodderomyces elongisporus 3-hydroxyanthranilate 3,4-dioxygenase (BNA1) KM 11.78 Gene Name : BNA1; LELG_03286; 3HAO; IMAO. ... Lanac Vitis vinifera Dihydroflavonol-4-reductase (DFR) (Lanac Proteina) KM 68.40 Gene Name : DFR; dfr1 dihydroflavonol ... Lanac Svinji 3-oxo-5-alfa-steroida 4-dehydrogenaze 2 (SRD5A2) (Lanac Proteina) KM 63.83 ...
Mechanistically, both 5-HT and 3-HA act as potent radical trapping antioxidants (RTA) to eliminate lipid peroxidation, thereby ... Kynureninase (KYNU), which is essential for 3-HA production, confers cells resistant to ferroptotic cell death, whereas 3- ... hydroxyanthranilate 3,4-dioxygenase (HAAO) significantly blocks 3-HA mediated ferroptosis inhibition by consuming 3-HA. In ... Here, the authors show that the tryptophan metabolites serotonin (5-HT) and 3-hydroxyanthranilic acid (3-HA) remarkably ...
3.501693 3.523507 acireductone dioxygenase 1 APL1; ARD; Fe-ARD; MTCBP1; Ni-ARD; SIPL ... 104.000592 104.02104 3-hydroxybutyrate dehydrogenase, type 2 DHRS6; EFA6R; PRO20933; SDR15C1; UCPA-OR; UNQ6308 ... 3-nucleotidase, cytosolic DNT; DNT1; P5N2; PN-I; PN-II; UMPH2; cdN; dNT-1 ... alpha 1-3-N-acetylgalactosaminyltransferase; transferase B, alpha 1-3-galactosyltransferase) A3GALNT; A3GALT1; GTB; NAGAT ...
hydroxyanthranilate. 3,4-dioxygenase. 2-amino-3-. carboxymuconate-. 6- semialdehyde. decarboxylase. Probable. phenylalanine-. 4 ... 2,4-. dioxobutanoic. acid. Kynurenic acid. Oxoglutaric. acid. L-Glutamic acid. NADPH. O. 2. L-3-. Hydroxykynurenine. ... 3-monooxygenase. Unknown. Unknown. CYtochrome P450. family. Unknown. Nicotinamide N-. methyltransferase. Unknown. Tyrosine. ... 2,3-dioxygenase. Kynureninase. ArylForMamiDase. ArylForMamiDase. Kynureninase. Unknown. Kynurenine. 3-monooxygenase. ...
von Rango, U.; Krusche, C.A.; Beier, H.M.; Classen-Linke, I. Indoleamine-Dioxygenase Is Expressed in Human Decidua at the Time ... Glial and Tissue-Specific Regulation of Kynurenine Pathway Dioxygenases by Acute Stress of Mice. Neurobiol. Stress 2017, 7, 1- ... The Role of IFN-Gamma and TNF-Alpha-Responsive Regulatory Elements in the Synergistic Induction of Indoleamine Dioxygenase. J. ... Figure 3. A review of kynurenine pathway (A) enzymes and (B) metabolites detected across animal kingdoms. If both gene and ...
Dioxygenases [D08.811.682.690.416] * AlkB Enzymes [D08.811.682.690.416.139] * Catechol 1,2-Dioxygenase [D08.811.682.690.416.277 ... 2-DIOXYGENASE was indexed under DIOXYGENASES 1975-2005, & under CATECHOL 1973-1974. History Note. 2006(1980); use DIOXYGENASES ... Catechol 1,2-Dioxygenase Preferred Concept UI. M0072800. Registry Number. EC 1.13.11.1. Related Numbers. 9027-16-1. Scope Note ... Catechol 1,2-Dioxygenase Preferred Term Term UI T102803. LexicalTag NON. ThesaurusID NLM (2006). ...
Zhan, X., Gimenez, L. E., Gurevich, V. V., and Spiller, B. W. (2011) Crystal structure of arrestin-3 reveals the basis of the ... Zhang, Y., Colabroy, K. L., Begley, T. P., and Ealick, S. E. (2005) Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase ...
Dioxygenases [D08.811.682.690.416] * AlkB Enzymes [D08.811.682.690.416.139] * Catechol 1,2-Dioxygenase [D08.811.682.690.416.277 ... Dioxygenases Preferred Concept UI. M0464092. Registry Number. EC 1.13.11.-. Related Numbers. EC 1.14.11.-. EC 1.14.12.-. Scope ... Dioxygenases Preferred Term Term UI T582228. Date04/09/2004. LexicalTag NON. ThesaurusID NLM (2005). ... Dioxygenase Term UI T000996428. Date11/14/2019. LexicalTag NON. ThesaurusID NLM (2021). ...
3-dioxygenase (IDO), the first step in the kynurenine pathway (KP), is upregulated in some cancers and represents an attractive ... Indoleamine 2,3-dioxygenase (IDO), the first step in the kynurenine pathway (KP), is upregulated in some cancers and represents ... including kynurenine 3-monoxygenase (KMO) and 3-hydroxyanthranilate-3,4-dioxygenase (HAAO), with a concomitant maintenance or ...
2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 1-Acylglycerol-3-Phosphate O-Acyltransferase 1-Acylglycerophosphocholine Acyltransferase use 1-Acylglycerophosphocholine O- ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3 End Processing, RNA use RNA 3 ... 4 Hydroxyphenylpyruvate Dioxygenase Deficiency Disease use Tyrosinemias 4-Nitrophenol-2-Hydroxylase use Cytochrome P-450 CYP2E1 ... 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase 3-beta-Hydroxysteroid Dehydrogenase use 3- ... 3,5-Cyclic-Nucleotide Phosphodiesterase use 3,5-Cyclic-AMP Phosphodiesterases 3-alpha-Hydroxysteroid Dehydrogenase (B- ...
2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 1-Acylglycerol-3-Phosphate O-Acyltransferase 1-Acylglycerophosphocholine Acyltransferase use 1-Acylglycerophosphocholine O- ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3 End Processing, RNA use RNA 3 ... 4 Hydroxyphenylpyruvate Dioxygenase Deficiency Disease use Tyrosinemias 4-Nitrophenol-2-Hydroxylase use Cytochrome P-450 CYP2E1 ... 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase 3-beta-Hydroxysteroid Dehydrogenase use 3- ... 3,5-Cyclic-Nucleotide Phosphodiesterase use 3,5-Cyclic-AMP Phosphodiesterases 3-alpha-Hydroxysteroid Dehydrogenase (B- ...
Dioxygenase. 4-Nitrophenol-2-Hydroxylase use Cytochrome P-450 CYP2E1 ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-Isomer ...
3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3 End Processing, RNA use RNA 3 ... 4 Hydroxyphenylpyruvate Dioxygenase Deficiency Disease use Tyrosinemias 4-Nitrophenol-2-Hydroxylase use Cytochrome P-450 CYP2E1 ... 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase 3-beta-Hydroxysteroid Dehydrogenase use 3- ... 3,5-Cyclic-Nucleotide Phosphodiesterase use 3,5-Cyclic-AMP Phosphodiesterases 3-alpha-Hydroxysteroid Dehydrogenase (B- ...
2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-Glucose use ... 3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 1-Acylglycerol-3-Phosphate O-Acyltransferase 1-Acylglycerophosphocholine Acyltransferase use 1-Acylglycerophosphocholine O- ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-Glucose use ... 3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 1-Acylglycerol-3-Phosphate O-Acyltransferase 1-Acylglycerophosphocholine Acyltransferase use 1-Acylglycerophosphocholine O- ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 1-Acylglycerol-3-Phosphate O-Acyltransferase 1-Acylglycerophosphocholine Acyltransferase use 1-Acylglycerophosphocholine O- ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
Dioxygenase. 4-Nitrophenol-2-Hydroxylase use Cytochrome P-450 CYP2E1 ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-Isomer ...
2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 1-Acylglycerol-3-Phosphate O-Acyltransferase 1-Acylglycerophosphocholine Acyltransferase use 1-Acylglycerophosphocholine O- ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 1-Acylglycerol-3-Phosphate O-Acyltransferase 1-Acylglycerophosphocholine Acyltransferase use 1-Acylglycerophosphocholine O- ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
Dioxygenase. 4-Nitrophenol-2-Hydroxylase use Cytochrome P-450 CYP2E1 ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... 3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-Isomer ...
ELISA Kit FOR 3-hydroxy-3-methylglutaryl-coenzyme A reductase - E10451b ELISA Kit FOR 3-hydroxy-3-methylglutaryl-coenzyme A ... ELISA Kit FOR 3-hydroxy-3-methylglutaryl-coenzyme A reductase - E10451m ELISA Kit FOR 3-hydroxy-3-methylglutaryl-coenzyme A ... ELISA Kit FOR 3-hydroxy-3-methylglutaryl-coenzyme A reductase - E10451r ELISA Kit FOR 3-hydroxyacyl-CoA dehydrogenase type-2 - ... ELISA Kit FOR 3-hydroxyisobutyrate dehydrogenase, mitochondrial - E12565r ELISA Kit FOR 3-oxo-5-alpha-steroid 4-dehydrogenase 1 ...
1.13.11.74 2-aminophenol 1,6-dioxygenase - MK BRENDA: BR50513 KEGG: R05405 ... 4-nitrophenyl_sulfate + 2-Aminophenol <=> 4-nitrophenol + 2-aminophenyl_sulfate 2.8.2.22 aryl-sulfate sulfotransferase - ... 3-phosphoadenylyl_sulfate + 2-Aminophenol <=> adenosine_3,5-bisphosphate + 2-aminophenyl_sulfate 2.8.2.1 aryl ... N-hydroxyaniline <=> 2-Aminophenol + 4-Aminophenol 5.4.4.3 3-(hydroxyamino)phenol mutase - ...
  • Tomić, Sanja Human 3-hydroxyanthranilate 3, 4-dioxygenase (3HAO) dynamics and reaction, a multilevel computational study. (wikipedia.org)
  • PhD thesis named Computational studies of Iron dependent dioxygenases, under mentor prof. Sanja Tomić, was defended in 2014th. (wikipedia.org)
  • Zhang, Y. , Colabroy, K. L. , Begley, T. P. , and Ealick, S. E. (2005) Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis . (cornell.edu)
  • Indoleamine 2,3-dioxygenase (IDO), the first step in the kynurenine pathway (KP), is upregulated in some cancers and represents an attractive therapeutic target given its role in tumour immune evasion. (physiciansweekly.com)
  • l -3,4-dihydroxyphenylalanine , is an amino acid that is made and used as part of the normal biology of some plants [3] and animals, including humans. (cloudfront.net)
  • A mononuclear Fe(II)-dependent oxygenase, this enzyme catalyzes the conversion of homogentisate to 4-maleylacetoacetate, the third step in the pathway for the catabolism of TYROSINE . (nih.gov)
  • 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)
  • PhD thesis named Computational studies of Iron dependent dioxygenases, under mentor prof. Sanja Tomić, was defended in 2014th. (wikipedia.org)
  • cyclin dependent kinase 4 [Source:HGNC S. (gsea-msigdb.org)
  • HN - 2006(1983) MH - 2-Oxoisovalerate Dehydrogenase (Acylating) UI - D050645 MN - D8.811.682.657.350.825 MS - An NAD+ dependent enzyme that catalyzes the oxidation 3-methyl-2-oxobutanoate to 2-methylpropanoyl-CoA. (nih.gov)
  • An enzyme that catalyzes the conversion of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde. (nih.gov)
  • 9/3/2005) TOTAL DESCRIPTORS = 935 MH - 1-Acylglycerol-3-Phosphate O-Acyltransferase UI - D051103 MN - D8.811.913.50.173 MS - An enzyme that catalyzes the acyl group transfer of ACYL COA to 1-acyl-sn-glycerol 3-phosphate to generate 1,2-diacyl-sn-glycerol 3-phosphate. (nih.gov)
  • 15. Mouse chronic social stress increases blood and brain kynurenine pathway activity and fear behaviour: Both effects are reversed by inhibition of indoleamine 2,3-dioxygenase. (nih.gov)
  • 7. Indoleamine 2,3-dioxygenase-expressing leukemic dendritic cells impair a leukemia-specific immune response by inducing potent T regulatory cells. (nih.gov)
  • 11. Up-regulated expression of indoleamine 2,3-dioxygenase 1 in non-Hodgkin lymphoma correlates with increased regulatory T-cell infiltration. (nih.gov)
  • actin related protein 2/3 complex subuni. (gsea-msigdb.org)
  • HN - 2006(1981) BX - Cofilins MH - Actin-Related Protein 2 UI - D051377 MN - D5.750.78.730.246.500 MN - D12.776.220.525.246.500 MS - A PROFILIN binding domain protein that is part of the Arp2-3 complex. (nih.gov)
  • HN - 2006(1998) MH - Actin-Related Protein 2-3 Complex UI - D051376 MN - D5.750.78.730.246 MN - D12.776.220.525.246 MS - A complex of seven proteins including ARP2 PROTEIN and ARP3 PROTEIN that plays an essential role in maintenance and assembly of the CYTOSKELETON. (nih.gov)
  • Arp2-3 complex binds WASP PROTEIN and existing ACTIN FILAMENTS, and it nucleates the formation of new branch point filaments. (nih.gov)
  • HN - 2006 BX - Arp2-3 Complex MH - Actin-Related Protein 3 UI - D051378 MN - D5.750.78.730.246.750 MN - D12.776.220.525.246.750 MS - A component of the Arp2-3 complex that is related in sequence and structure to ACTIN and that binds ATP. (nih.gov)