Tryptophan Transaminase
Tryptophan
Alanine Transaminase
4-Aminobutyrate Transaminase
Transaminases
Tryptophan Oxygenase
Aspartate Aminotransferases
Tryptophan Synthase
D-Alanine Transaminase
Tryptophan Hydroxylase
Kynurenine
Fluoxetine
Antidepressive Agents, Second-Generation
Serotonin Uptake Inhibitors
Serotonin
Drug Interactions
Product Labeling
Drug Labeling
Indole-3-acetic acid (IAA) synthesis in the biocontrol strain CHA0 of Pseudomonas fluorescens: role of tryptophan side chain oxidase. (1/15)
Pseudomonas fluorescens strain CHA0 is an effective biocontrol agent against soil-borne fungal plant pathogens. In this study, indole-3-acetic acid (IAA) biosynthesis in strain CHA0 was investigated. Two key enzyme activities were found to be involved: tryptophan side chain oxidase (TSO) and tryptophan transaminase. TSO was induced in the stationary growth phase. By fractionation of a cell extract of strain CHA0 on DEAE-Sepharose, two distinct peaks of constitutive tryptophan transaminase activity were detected. A pathway leading from tryptophan to IAA via indole-3-acetamide, which occurs in Pseudomonas syringae subsp. savastanoi, was not present in strain CHA0. IAA synthesis accounted for less than or equal to 1.5% of exogenous tryptophan consumed by resting cells of strain CHA0, indicating that the bulk of tryptophan was catabolized via yet another pathway involving anthranilic acid as an intermediate. Strain CHA750, a mutant lacking TSO activity, was obtained after Tn5 mutagenesis of strain CHA0. In liquid cultures (pH 6.8) supplemented with 10 mM-L-tryptophan, growing cells of strains CHA0 and CHA750 synthesized the same amount of IAA, presumably using the tryptophan transaminase pathway. In contrast, resting cells of strain CHA750 produced five times less IAA in a buffer (pH 6.0) containing 1 mM-L-tryptophan than did resting cells of the wild-type, illustrating the major contribution of TSO to IAA synthesis under these conditions. In artificial soils at pH approximately 7 or pH approximately 6, both strains had similar abilities to suppress take-all disease of wheat or black root rot of tobacco. This suggests that TSO-dependent IAA synthesis is not essential for disease suppression. (+info)A one-pot chemoenzymatic synthesis for the universal precursor of antidiabetes and antiviral bis-indolylquinones. (2/15)
Bis-indolylquinones represent a class of fungal natural products that display antiretroviral, antidiabetes, or cytotoxic bioactivities. Recent advances in Aspergillus genomic mining efforts have led to the discovery of the tdiA-E-gene cluster, which is the first genetic locus dedicated to bis-indolylquinone biosynthesis. We have now genetically and biochemically characterized the enzymes TdiA (bis-indolylquinone synthetase) and TdiD (L-tryptophan:phenylpyruvate aminotransferase), which, together, confer biosynthetic abilities for didemethylasterriquinone D to Aspergillus nidulans. This compound is the universal intermediate for all bis-indolylquinones. In this biochemical study of a bis-indolylquinone synthetase and a fungal natural product transaminase, we present a one-pot chemoenzymatic protocol to generate didemethylasterriquinone D in vitro. As TdiA resembles a nonribosomal peptide synthetase, yet catalyzes carbon-carbon-bond formation, we discuss the implications for peptide synthetase chemistry. (+info)A new gene for auxin synthesis. (3/15)
(+info)Rapid synthesis of auxin via a new tryptophan-dependent pathway is required for shade avoidance in plants. (4/15)
(+info)TAA1-mediated auxin biosynthesis is essential for hormone crosstalk and plant development. (5/15)
(+info)The TRANSPORT INHIBITOR RESPONSE2 gene is required for auxin synthesis and diverse aspects of plant development. (6/15)
(+info)vanishing tassel2 encodes a grass-specific tryptophan aminotransferase required for vegetative and reproductive development in maize. (7/15)
(+info)Conversion of tryptophan to indole-3-acetic acid by TRYPTOPHAN AMINOTRANSFERASES OF ARABIDOPSIS and YUCCAs in Arabidopsis. (8/15)
(+info)Tryptophan transaminase, also known as tryptophan aminotransferase or L-tryptophan aminotransferase, is an enzyme involved in the metabolism of the essential amino acid tryptophan. This enzyme catalyzes the transfer of an amino group from tryptophan to a ketoacid acceptor, such as alpha-ketoglutarate, resulting in the formation of beta-amino-isocaproic acid and glutamate. The reaction is part of the larger catabolic pathway for tryptophan degradation, which eventually leads to the production of several biologically important compounds, including niacin (vitamin B3) and serotonin, a neurotransmitter.
Tryptophan transaminase plays a crucial role in maintaining the balance of amino acids in the body and ensuring their proper utilization for various physiological functions. Dysregulation or deficiency of this enzyme can contribute to several metabolic disorders, including hyperphenylalaninemia (elevated levels of phenylalanine) and certain neurological conditions due to impaired serotonin synthesis.
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.
Alanine transaminase (ALT) is a type of enzyme found primarily in the cells of the liver and, to a lesser extent, in the cells of other tissues such as the heart, muscles, and kidneys. Its primary function is to catalyze the reversible transfer of an amino group from alanine to another alpha-keto acid, usually pyruvate, to form pyruvate and another amino acid, usually glutamate. This process is known as the transamination reaction.
When liver cells are damaged or destroyed due to various reasons such as hepatitis, alcohol abuse, nonalcoholic fatty liver disease, or drug-induced liver injury, ALT is released into the bloodstream. Therefore, measuring the level of ALT in the blood is a useful diagnostic tool for evaluating liver function and detecting liver damage. Normal ALT levels vary depending on the laboratory, but typically range from 7 to 56 units per liter (U/L) for men and 6 to 45 U/L for women. Elevated ALT levels may indicate liver injury or disease, although other factors such as muscle damage or heart disease can also cause elevations in ALT.
4-Aminobutyrate transaminase (GABA transaminase or GABA-T) is an enzyme that catalyzes the reversible transfer of an amino group from 4-aminobutyrate (GABA) to 2-oxoglutarate, forming succinic semialdehyde and glutamate. This enzyme plays a crucial role in the metabolism of the major inhibitory neurotransmitter gamma-aminobutyric acid (GABA) in the central nervous system. Inhibition of GABA transaminase is a therapeutic strategy for the treatment of various neurological disorders, such as epilepsy and anxiety, due to its ability to increase GABA levels in the brain.
Transaminases, also known as aminotransferases, are a group of enzymes found in various tissues of the body, particularly in the liver, heart, muscle, and kidneys. They play a crucial role in the metabolism of amino acids, the building blocks of proteins.
There are two major types of transaminases: aspartate aminotransferase (AST) and alanine aminotransferase (ALT). Both enzymes are normally present in low concentrations in the bloodstream. However, when tissues that contain these enzymes are damaged or injured, such as during liver disease or muscle damage, the levels of AST and ALT in the blood may significantly increase.
Measurement of serum transaminase levels is a common laboratory test used to assess liver function and detect liver injury or damage. Increased levels of these enzymes in the blood can indicate conditions such as hepatitis, liver cirrhosis, drug-induced liver injury, heart attack, and muscle disorders. It's important to note that while elevated transaminase levels may suggest liver disease, they do not specify the type or cause of the condition, and further diagnostic tests are often required for accurate diagnosis and treatment.
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.
Aspartate aminotransferases (ASTs) are a group of enzymes found in various tissues throughout the body, including the heart, liver, and muscles. They play a crucial role in the metabolic process of transferring amino groups between different molecules.
In medical terms, AST is often used as a blood test to measure the level of this enzyme in the serum. Elevated levels of AST can indicate damage or injury to tissues that contain this enzyme, such as the liver or heart. For example, liver disease, including hepatitis and cirrhosis, can cause elevated AST levels due to damage to liver cells. Similarly, heart attacks can also result in increased AST levels due to damage to heart muscle tissue.
It is important to note that an AST test alone cannot diagnose a specific medical condition, but it can provide valuable information when used in conjunction with other diagnostic tests and clinical evaluation.
Tryptophan synthase is a bacterial enzyme that catalyzes the final step in the biosynthesis of the essential amino acid tryptophan. It is a complex enzyme composed of two types of subunits, α and β, which form an αββα tetrameric structure.
Tryptophan synthase catalyzes the conversion of indole-3-glycerol phosphate (IGP) and L-serine into tryptophan through two separate reactions that occur in a coordinated manner within the active site of the enzyme. In the first reaction, the α subunit catalyzes the breakdown of IGP into indole and glyceraldehyde-3-phosphate (G3P). The indole molecule then moves through a tunnel to the active site of the β subunit, where it is combined with L-serine to form tryptophan in the second reaction.
The overall reaction catalyzed by tryptophan synthase is:
Indole-3-glycerol phosphate + L-serine → L-tryptophan + glyceraldehyde-3-phosphate
Tryptophan synthase plays a critical role in the biosynthesis of tryptophan, which is an essential amino acid that cannot be synthesized by humans and must be obtained through diet. Defects in tryptophan synthase can lead to various genetic disorders, such as hyperbeta-alaninemia and tryptophanuria.
D-Alanine transaminase (DAT or Dalat) is an enzyme that catalyzes the reversible transfer of an amino group from D-alanine to α-ketoglutarate, producing pyruvate and D-glutamate. It is found in various bacteria and plays a role in their metabolism. However, it is not typically considered a medically significant enzyme in humans, as it is not commonly used as a clinical marker of liver or other organ function.
Tryptophan hydroxylase is an enzyme that plays a crucial role in the synthesis of neurotransmitters and hormones, including serotonin and melatonin. It catalyzes the conversion of the essential amino acid tryptophan to 5-hydroxytryptophan (5-HTP), which is then further converted to serotonin. This enzyme exists in two isoforms, TPH1 and TPH2, with TPH1 primarily located in peripheral tissues and TPH2 mainly found in the brain. The regulation of tryptophan hydroxylase activity has significant implications for mood, appetite, sleep, and pain perception.
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.
Fluoxetine is a selective serotonin reuptake inhibitor (SSRI) medication that is primarily used to treat major depressive disorder, obsessive-compulsive disorder, bulimia nervosa, panic disorder, and premenstrual dysphoric disorder. It works by increasing the levels of serotonin, a neurotransmitter in the brain that helps maintain mental balance.
Fluoxetine is available under the brand name Prozac and is also available as a generic medication. It comes in various forms, including capsules, tablets, delayed-release capsules, and liquid solution. The typical starting dose for adults with depression is 20 mg per day, but the dosage may be adjusted based on individual patient needs and response to treatment.
Fluoxetine has a relatively long half-life, which means it stays in the body for an extended period of time. This can be beneficial for patients who may have difficulty remembering to take their medication daily, as they may only need to take it once or twice a week. However, it also means that it may take several weeks for the full effects of the medication to become apparent.
As with any medication, fluoxetine can cause side effects, including nausea, dry mouth, sleepiness, insomnia, dizziness, and headache. In some cases, it may also increase the risk of suicidal thoughts or behavior in children, adolescents, and young adults, particularly during the initial stages of treatment. It is important for patients to discuss any concerns about side effects with their healthcare provider.
Second-generation antidepressants (SGAs) are a class of medications used primarily for the treatment of depression, although they are also used for other psychiatric and medical conditions. They are called "second-generation" because they were developed after the first generation of antidepressants, which include tricyclic antidepressants (TCAs) and monoamine oxidase inhibitors (MAOIs).
SGAs are also known as atypical antidepressants or novel antidepressants. They work by affecting the levels of neurotransmitters in the brain, such as serotonin, norepinephrine, and dopamine. However, they have a different chemical structure and mechanism of action than first-generation antidepressants.
Some examples of second-generation antidepressants include:
* Selective serotonin reuptake inhibitors (SSRIs) such as fluoxetine (Prozac), sertraline (Zoloft), and citalopram (Celexa)
* Serotonin-norepinephrine reuptake inhibitors (SNRIs) such as venlafaxine (Effexor) and duloxetine (Cymbalta)
* Norepinephrine and dopamine reuptake inhibitors (NDRIs) such as bupropion (Wellbutrin)
* Atypical antidepressants such as mirtazapine (Remeron), trazodone, and vortioxetine (Brintellix)
SGAs are generally considered to have a more favorable side effect profile than first-generation antidepressants. They are less likely to cause anticholinergic effects such as dry mouth, constipation, and blurred vision, and they are less likely to cause cardiac conduction abnormalities or orthostatic hypotension. However, SGAs may still cause side effects such as nausea, insomnia, sexual dysfunction, and weight gain.
It's important to note that the choice of antidepressant medication should be individualized based on the patient's specific symptoms, medical history, and other factors. It may take some trial and error to find the most effective and well-tolerated medication for a given patient.
Serotonin uptake inhibitors (also known as Selective Serotonin Reuptake Inhibitors or SSRIs) are a class of medications primarily used to treat depression and anxiety disorders. They work by increasing the levels of serotonin, a neurotransmitter in the brain that helps regulate mood, appetite, and sleep, among other functions.
SSRIs block the reuptake of serotonin into the presynaptic neuron, allowing more serotonin to be available in the synapse (the space between two neurons) for binding to postsynaptic receptors. This results in increased serotonergic neurotransmission and improved mood regulation.
Examples of SSRIs include fluoxetine (Prozac), sertraline (Zoloft), paroxetine (Paxil), citalopram (Celexa), and escitalopram (Lexapro). These medications are generally well-tolerated, with side effects that may include nausea, headache, insomnia, sexual dysfunction, and increased anxiety or agitation. However, they can have serious interactions with other medications, so it is important to inform your healthcare provider of all medications you are taking before starting an SSRI.
Serotonin, also known as 5-hydroxytryptamine (5-HT), is a monoamine neurotransmitter that is found primarily in the gastrointestinal (GI) tract, blood platelets, and the central nervous system (CNS) of humans and other animals. It is produced by the conversion of the amino acid tryptophan to 5-hydroxytryptophan (5-HTP), and then to serotonin.
In the CNS, serotonin plays a role in regulating mood, appetite, sleep, memory, learning, and behavior, among other functions. It also acts as a vasoconstrictor, helping to regulate blood flow and blood pressure. In the GI tract, it is involved in peristalsis, the contraction and relaxation of muscles that moves food through the digestive system.
Serotonin is synthesized and stored in serotonergic neurons, which are nerve cells that use serotonin as their primary neurotransmitter. These neurons are found throughout the brain and spinal cord, and they communicate with other neurons by releasing serotonin into the synapse, the small gap between two neurons.
Abnormal levels of serotonin have been linked to a variety of disorders, including depression, anxiety, schizophrenia, and migraines. Medications that affect serotonin levels, such as selective serotonin reuptake inhibitors (SSRIs), are commonly used to treat these conditions.
A drug interaction is the effect of combining two or more drugs, or a drug and another substance (such as food or alcohol), which can alter the effectiveness or side effects of one or both of the substances. These interactions can be categorized as follows:
1. Pharmacodynamic interactions: These occur when two or more drugs act on the same target organ or receptor, leading to an additive, synergistic, or antagonistic effect. For example, taking a sedative and an antihistamine together can result in increased drowsiness due to their combined depressant effects on the central nervous system.
2. Pharmacokinetic interactions: These occur when one drug affects the absorption, distribution, metabolism, or excretion of another drug. For example, taking certain antibiotics with grapefruit juice can increase the concentration of the antibiotic in the bloodstream, leading to potential toxicity.
3. Food-drug interactions: Some drugs may interact with specific foods, affecting their absorption, metabolism, or excretion. An example is the interaction between warfarin (a blood thinner) and green leafy vegetables, which can increase the risk of bleeding due to enhanced vitamin K absorption from the vegetables.
4. Drug-herb interactions: Some herbal supplements may interact with medications, leading to altered drug levels or increased side effects. For instance, St. John's Wort can decrease the effectiveness of certain antidepressants and oral contraceptives by inducing their metabolism.
5. Drug-alcohol interactions: Alcohol can interact with various medications, causing additive sedative effects, impaired judgment, or increased risk of liver damage. For example, combining alcohol with benzodiazepines or opioids can lead to dangerous levels of sedation and respiratory depression.
It is essential for healthcare providers and patients to be aware of potential drug interactions to minimize adverse effects and optimize treatment outcomes.
Product labeling, in the context of medicine or healthcare, refers to the information that is required by law to be present on the packaging of a pharmaceutical product or medical device. This information typically includes:
1. The name of the product, often with an active ingredient listed separately.
2. A description of what the product is used for (indications).
3. Dosage instructions and route of administration.
4. Warnings about potential side effects, contraindications, and precautions.
5. The name and address of the manufacturer or distributor.
6. The expiration date or storage conditions, if applicable.
7. Any other relevant information, such as whether the product is subject to additional monitoring.
The purpose of product labeling is to provide accurate and standardized information to healthcare professionals and patients about the safe and effective use of a medical product. It helps to ensure that the product is used appropriately, reducing the risk of adverse events or misuse.
Drug labeling refers to the information that is provided on the packaging or container of a medication, as well as any accompanying promotional materials. This information is intended to provide healthcare professionals and patients with accurate and up-to-date data about the drug's composition, intended use, dosage, side effects, contraindications, and other important details that are necessary for safe and effective use.
The labeling of prescription drugs in the United States is regulated by the Food and Drug Administration (FDA), which requires manufacturers to submit proposed labeling as part of their new drug application. The FDA reviews the labeling to ensure that it is truthful, balanced, and not misleading, and provides accurate information about the drug's risks and benefits.
The labeling of over-the-counter (OTC) drugs is also regulated by the FDA, but in this case, the agency has established a set of monographs that specify the conditions under which certain active ingredients can be used and the labeling requirements for each ingredient. Manufacturers of OTC drugs must ensure that their labeling complies with these monographs.
In addition to the information required by regulatory agencies, drug labeling may also include additional information provided by the manufacturer, such as detailed instructions for use, storage requirements, and any warnings or precautions that are necessary to ensure safe and effective use of the medication. It is important for healthcare professionals and patients to carefully review and understand all of the information provided on a drug's labeling before using the medication.
Tryptophan transaminase
Tryptophan-phenylpyruvate transaminase
List of EC numbers (EC 2)
Kynurenine-oxoglutarate transaminase
Transferase
Histidinol-phosphate transaminase
Aromatic-amino-acid transaminase
Vitamin B6
List of MeSH codes (D08)
Kynurenic acid
Biochemistry
Natural product
Amino acid
Kynurenine
Dicarboxylic aminoaciduria
Serine
Aminodeoxychorismate synthase
Amino acid synthesis
Tranilast
Clomipramine
Niacin
Daptomycin
Pyridoxal phosphate
Tyrosine
List of enzymes
Human serum albumin
Biosynthesis
Anorexia nervosa
Tryptophan transaminase - Wikipedia
Similarities of Characterized Proteins
Plant Biology - Works - Citation Index - NCSU Libraries
B6db references : 71150797
Kynurenic Acid-Targeted Approaches in Dementia | Encyclopedia MDPI
Indole-3-acetic acid | 87-51-4
Scholars@Duke publication: A mathematical model of tryptophan metabolism via the kynurenine pathway provides insights into the...
AADAT protein expression summary - The Human Protein Atlas
MMTB
EurekaMag Full Text Articles Chapter 43410
MMTB
ExplorEnz: New Enzymes
Oliver Florey - Publications | Babraham Institute
Genomic and transcriptomic analysis of sacred fig (Ficus religiosa) | BMC Genomics | Full Text
Protein Concepts Dictionary
DeCS 2017 - December 21, 2017 version
L-Lysine 6-Transaminase | Profiles RNS
DeCS 2016 - June 12, 2016 version
DeCS 2018 - July 31, 2018 version
DeCS 2017 - July 04, 2017 version
DeCS 2019 - June 12, 2019 version
Nutritional Deficiencies with Tom Malterre: Rational Wellness Podcast 240 - Weitz Sports Chiropractic and Nutrition
Vitamin B-6
Prozac:Depression, Uses, Dosages, Side Effects, Interactions, Warnings
BiGG Metabolite akg c in iUMN146 1321
DailyMed - FLUOXETINE- fluoxetine hydrochloride tablet
DailyMed - FLUOXETINE capsule
EMF-Portal | Biological effects of power frequency magnetic fields: Neurochemical and toxicological changes in developing chick...
Aminotransferase4
- The systematic name of this enzyme class is L-tryptophan:2-oxoglutarate aminotransferase. (wikipedia.org)
- Other names in common use include L-phenylalanine-2-oxoglutarate aminotransferase, tryptophan aminotransferase, 5-hydroxytryptophan-ketoglutaric transaminase, hydroxytryptophan aminotransferase, L-tryptophan aminotransferase, and L-tryptophan transaminase. (wikipedia.org)
- Vitamin B-6 deficiency is associated with impaired tryptophan metabolism because of the coenzyme role of pyridoxal 5'-phosphate (PLP) for kynureninase and kynurenine aminotransferase. (duke.edu)
- Serum aminotransferases such as aspartate aminotransferase, AST and alanine transaminase, ALT have been used as clinical markers of tissue damage, with increasing serum levels indicating an increased extent of damage. (medmuv.com)
Alanine transaminase4
- Additionally, there are multiple enzymes that may be measured in testing, such as: gamma glutamyl transpeptidase, alanine transaminase, and others. (dailypanchayat.com)
- Alanine transaminase has an important function in the delivery of skeletal muscle carbon and nitrogen (in the form of alanine) to the liver. (medmuv.com)
- In the liver, alanine transaminase transfers the ammonia to α-KG and regenerates pyruvate. (medmuv.com)
- This reaction is catalyzed by alanine transaminase, ALT. (medmuv.com)
Metabolism5
- This enzyme participates in tryptophan metabolism. (wikipedia.org)
- Scholars@Duke publication: A mathematical model of tryptophan metabolism via the kynurenine pathway provides insights into the effects of vitamin B-6 deficiency, tryptophan loading, and induction of tryptophan 2,3-dioxygenase on tryptophan metabolites. (duke.edu)
- To investigate the underlying mechanism, we developed a mathematical model of tryptophan metabolism via the kynurenine pathway. (duke.edu)
- These results show that the model successfully simulated tryptophan metabolism via the kynurenine pathway and can be used to complement experimental investigations. (duke.edu)
- Pyridoxal kinase phosphorylates pyridoxine and pyridoxamine, after which they are converted to PLP, a coenzyme in tryptophan and methionine metabolism. (medscape.com)
Serotonin2
- Additionally, cherry juice also contains procyanidin B-2, which increases the availability of tryptophan -- the amino acid the body uses to produce serotonin and melatonin. (priceplow.com)
- You'll know it could be excess serotonin because your anxiety gets worse if you use L-Tryptophan or 5- HTP . (nootropicsexpert.com)
Enzyme4
- In enzymology, a tryptophan transaminase (EC 2.6.1.27) is an enzyme that catalyzes the chemical reaction L-tryptophan + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } (indol-3-yl)pyruvate + L-glutamate Thus, the two substrates of this enzyme are L-tryptophan and 2-oxoglutarate, whereas its two products are (indol-3-yl)pyruvate and L-glutamate. (wikipedia.org)
- This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. (wikipedia.org)
- The model includes mammalian data on enzyme kinetics and tryptophan transport from the intestinal lumen to liver, muscle, and brain. (duke.edu)
- Rare metabolic and acute alpha-aminoadipic hyperaminoaciduria is documented as due to a hereditary defect in the Alpha-aminoadipic acid transaminase enzyme and in the next enzyme in the sequence, alpha-ketoadipic acid dehydrogenase. (healthmatters.io)
Coenzyme1
- In the liver, pyridoxine is essential for glucose production from amino acids via its role as coenzyme for the transaminase enzymes. (getcompletecare.com)
Transamination1
- Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). (affbiotech.com)
Enzymes1
- B6 is needed by the transaminase enzymes, which convert one amino acid to another, and thus facilitate feeding them into the Krebs cycle. (healthmatters.io)
Lysine4
- L-Lysine 6-Transaminase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ouhsc.edu)
- This graph shows the total number of publications written about "L-Lysine 6-Transaminase" by people in this website by year, and whether "L-Lysine 6-Transaminase" was a major or minor topic of these publications. (ouhsc.edu)
- Below are the most recent publications written about "L-Lysine 6-Transaminase" by people in Profiles. (ouhsc.edu)
- Alpha-aminoadipic acid (a-Aminoadipic acid) is an intermediary metabolite of lysine (primarily) and of tryptophan. (healthmatters.io)
Hydroxylase1
- It is believed to be produced by the body through the process of tryptophan hydroxylase. (magnificentworld.com)
Several neurotransmitters1
- Tryptophan is a precursor to several neurotransmitters and is required for niacin production. (medscape.com)
Pyruvate2
- Tryptophan is the only known substrate other than pyruvate that is used for fermentative cell growth in this organism [5]. (screeninglibraries.com)
- Two buy Staurosporine copies of the gene (Dhaf_1324 and Dhaf_2460) coding for tryptophanase which converts tryptophan to indole, pyruvate, and ammonia were identified in association with two permease genes (Dhaf_1325 and Dhaf_2459). (screeninglibraries.com)
Metabolite2
- We simulated the effects of graded reduction in cellular PLP concentration, tryptophan loads and induction of tryptophan 2,3-dioxygenase (TDO) on metabolite profiles and urinary excretion. (duke.edu)
- Tryptophan load simulations with and without vitamin B-6 deficiency showed altered metabolite concentrations consistent with published data. (duke.edu)
Acid4
- 3-Indolylacetic acid is biosynthesised in plants from tryptophan by two pathways, the indolylpyruvic acid pathway being quantitatively the more important. (sabinaorganizasyon.com)
- Experiments with tomato shoots have shown the existence of a tryptophan transaminase, which catalyses the formation of indolylpyruvic acid, and a tryptophan decarboxylase, which catalyses the formation of tryptamine. (sabinaorganizasyon.com)
- Pyridoxine is also needed by the liver and muscles to make stored glycogen available for glucose production, and to synthesize niacin from the amino acid tryptophan. (getcompletecare.com)
- Your body can make niacin from the common amino acid tryptophan. (dailypanchayat.com)
Serum levels1
- CBD may raise serum levels of medications and may interfere with hepatic transaminases. (magnificentworld.com)
Pathway1
- The BCAAs enter this pathway via the removal of an amino group by a transaminase, which is then fed into the urea cycle. (ast-ss.com)
Plasma1
- Supplementation with Muscle Energy BCAAs can prevent CNS fatigue by competing with free-tryptophan for uptake from the plasma into the brain. (ast-ss.com)
Methionine1
- Pyridoxal kinase phosphorylates pyridoxine and pyridoxamine, after which they are converted to PLP, a coenzyme in tryptophan and methionine metabolism. (medscape.com)
Phenylalanine4
- Other names in common use include L-phenylalanine-2-oxoglutarate aminotransferase, tryptophan aminotransferase, 5-hydroxytryptophan-ketoglutaric transaminase, hydroxytryptophan aminotransferase, L-tryptophan aminotransferase, and L-tryptophan transaminase. (wikipedia.org)
- Like endotoxin, dihydroxyphenylalanine (DOPA) lowered hepatic tryptophan pyrrolase (TP) activity within 6 hr and this effect was specific since neither of the two other analogues parachlorophenylalanine (PCPA) and phenylalanine, nor serotonin and LSD-25, depressed the hepatic TP. (erowid.org)
- The LSD-25 or PCPA, but not phenylalanine, DOPA or serotonin, increased hepatic tyrosine transaminase (TT). (erowid.org)
- Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. (cathdb.info)
Serum3
- Notably, IDO1 knockout mice were protected from CCl 4 -induced liver fibrosis, as reflected by unchanged serum alanine transaminase and aspartate transaminase levels and lower collagen deposition, α-smooth muscle actin expression and apoptotic cell death rates. (oncotarget.com)
- Serum ALT level, serum AST ( aspartate transaminase ) level, and their ratio ( AST/ALT ratio ) are commonly measured clinically as biomarkers for liver health. (wikidoc.org)
- Further, increased liver collagen staining and serum transaminase levels showed that TCDD induced liver fibrosis in the HFD fed mice. (nih.gov)
Glycine2
- Amino acid profile in autistic children showed statistically significant lower levels of aspartic acid, glycine, β-alanine, tryptophan, lysine and proline amino acids with significantly higher asparagine amino acid derivative levels among autistic patients versus the control group (p˂0.05). (dovepress.com)
- It is the precursor to several amino acids including glycine and cysteine , as well as tryptophan in bacteria. (iiab.me)
Amino group3
- A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the transfer amino group from L-TRYPTOPHAN to 2-oxoglutarate in order to generate indolepyruvate and L-GLUTAMATE . (nih.gov)
- HN - 2006(1981) MH - 2-Aminoadipate Transaminase UI - D051307 MN - D8.811.913.477.700.120 MS - A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the transfer of amino group of L-2-aminoadipate onto 2-OXOGLUTARATE to generate 2-oxoadipate and L-GLUTAMATE. (nih.gov)
- The BCAAs enter this pathway via the removal of an amino group by a transaminase, which is then fed into the urea cycle. (ast-ss.com)
Synthesis3
- The present study aimed to examine the relationship between behavioural measures of anxiety and depression with liver TDO activity, brain tryptophan concentration and serotonin synthesis in rats treated chronically with nicotine. (bvsalud.org)
- Each 60 mg of excess tryptophan (after protein synthesis) is converted to approximately 1 mg of niacin. (empowerpharmacy.com)
- Synthesis of the vitamin from tryptophan in proteins supplies roughly half the niacin requirement in man. (empowerpharmacy.com)
Rate-limiti1
- Tryptophan-5-hydroxylase-1 (T5H-1) is the rate-limiting enzyme within the biosynthesis of serotonin, which is concerned within the biosynthesis of melatonin (Mel). (mytaq.com)
Biosynthesis1
- However, the body's niacin requirement is also met by the biosynthesis of niacin from tryptophan, an amino acid. (empowerpharmacy.com)
Niacin5
- Tryptophan is a precursor to several neurotransmitters and is required for niacin production. (medscape.com)
- The body also converts some tryptophan, an amino acid in protein, to NAD, so tryptophan is considered a dietary source of niacin. (nih.gov)
- For example, milk and eggs do not contain niacin, but do contain large amounts of tryptophan from which niacin is derived. (empowerpharmacy.com)
- Iron-deficiency or inadequate pyridoxine or riboflavin status will decrease the conversion of tryptophan to niacin and may contribute to deficiency, due to an interdependence of coenzymes in the niacin production pathway. (empowerpharmacy.com)
- Pellagra may result from a niacin- and protein-deficient diet, isoniazid therapy, or certain diseases that result in poor utilization of tryptophan. (empowerpharmacy.com)
IDO12
- Additionally, an IDO1 inhibitor (1-methyl- D -tryptophan) was administered to WT fibrosis mice. (oncotarget.com)
- Indoleamine 2,3-dioxygenase 2 (IDO2) is a tryptophan-catabolizing enzyme and a homolog of IDO1 with a distinct expression pattern compared with IDO1. (bvsalud.org)
Activity2
- In dendritic cells (DCs), IDO activity and the resulting changes in tryptophan level regulate T-cell differentiation and promote immune tolerance. (bvsalud.org)
- Popov, V.O. Counterbalance of Stability and Activity Observed for Thermostable Transaminase from Thermobaculum terrenum in the Presence of Organic Solvents. (fbras.ru)
Gene2
- Therefore, in the present study, we modified the 3-hydroxykynurenine transaminase ( 3hkt ) and hormone receptor 3 ( hr3 ) RNAi vectors to remove antibiotic resistance marker genes and retain the expression cassette of the inverse repeat sequence of the 3hkt/hr3 target gene. (biomedcentral.com)
- Deletion of the tryptophan 2,3-dioxygenase ( TDO2 ) gene induces an anxiolytic-like behaviour in mice and TDO inhibition by allopurinol elicits an antidepressant-like effect in rats exposed to restraint stress. (bvsalud.org)
Levels1
- The levels of glutamate decarboxylase, GABA transaminase, succinate-semialdehyde dehydrogenase, and methylisocitrate lyase were reduced or absent in diabetic rats compared with controls and obese rats. (edu.krd)
Brain2
- Because L-Kyn is produced in a significant amount in the liver through the degradation of L-tryptophan by tryptophan-2,3-dioxygenase (TDO), 13 it is more likely to accumulate in the liver than in the brain due to ischemia. (researchsquare.com)
- Supplementation with Muscle Energy BCAAs can prevent CNS fatigue by competing with free-tryptophan for uptake from the plasma into the brain. (ast-ss.com)
Term1
- The term transaminase is outdated and no longer used in liver disease. (wikidoc.org)
Family1
- This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. (wikipedia.org)
Muscle1
- Alanine transaminase has an important function in the delivery of skeletal muscle carbon and nitrogen (in the form of alanine) to the liver. (tdmuv.com)