Glycine Transaminase
Glycine
Alanine Transaminase
4-Aminobutyrate Transaminase
Transaminases
Receptors, Glycine
Aspartate Aminotransferases
D-Alanine Transaminase
Alanine
Sensitivity and Specificity
Ketoglutaric Acids
Alanine aminotransferase and glycine aminotransferase from maize (Zea mays L.) leaves. (1/3)
Alanine aminotransferase (AlaAT, EC 2.6.1.2) and glycine aminotransferase (GlyAT, EC 2.6.1.4), two different enzymes catalyzing transamination reactions with L-alanine as the amino-acid substrate, were examined in maize in which alanine participates substantially in nitrogen transport. Preparative PAGE of a partially purified preparation of aminotransferases from maize leaves gave 6 fractions differing in electrophoretic mobility. The fastest migrating fraction I represents AlaAT specific for L-alanine as amino donor and 2-oxoglutarate as amino acceptor. The remaining fractions showed three aminotransferase activities: L-alanine-2-oxoglutarate, L-alanine-glyoxylate and L-glutamate-glyoxylate. By means of molecular sieving on Zorbax SE-250 two groups of enzymes were distinguished in the PAGE fractions: of about 100 kDa and 50 kDa. Molecular mass of 104 kDa was ascribed to AlaAT in fraction I, while the molecular mass of the three enzymatic activities in 3 fractions of the low electrophoretic mobility was about 50 kDa. The response of these fractions to: aminooxyacetate, 3-chloro-L-alanine and competing amino acids prompted us to suggest that five out of the six preparative PAGE fractions represented GlyAT isoforms, differing from each other by the L-glutamate-glyoxylate:L-alanine-glyoxylate:L-alanine-2-oxoglutarate activity ratio. (+info)Some properties of glycine aminotransferase purified from Rhodopseudomonas palustris No. 7 concerning extracellular porphyrin production. (2/3)
Glycine aminotransferase (EC 2.6.1.4; GlyAT) was presumed to be an enzyme concerning the supply of glycine for the extracellular porphyrin production by Rhodopseudomonas palustris No. 7. GlyAT was purified from strain No. 7 as an electrophoretically homogenous protein. The enzyme was a monomer protein with the molecular weight of about 42,000. From the absorption spectrum of the enzyme (350 nm, 410 nm), it was indicated that the enzyme had pyridoxal phosphate as a prosthetic group. The enzyme showed high substrate specificity for glutamate as an amino group donor. Apparent Kms for glutamate and glyoxylate were 6.20 mM and 3.75 mM, respectively. The Vmax and Kcat for glutamate were 66.8 mumol/min/mg protein and 46.8 s-1, respectively. The Vmax and Kcat for glyoxylate were 68.8 mumol/min/mg protein and 48.2 s-1. The optimum temperature and pH were 40-45 degrees C and 7.0-7.5, respectively. The enzyme activity lowered to about 50% in the presence of 15 mM ammonium chloride. (+info)Biochemical and structural characterization of a ureidoglycine aminotransferase in the Klebsiella pneumoniae uric acid catabolic pathway. (3/3)
(+info)Glycine transaminase, also known as alanine-glyoxylate aminotransferase (AGT) or glyoxylate transaminase (GOT2), is an enzyme that plays a role in the metabolism of glyoxylate and glycine. It catalyzes the transfer of an amino group from glycine to glutamate, forming α-ketoglutarate and creatine.
Deficiency of this enzyme can lead to a rare genetic disorder called primary hyperoxaluria type 1 (PH1), which is characterized by the overproduction of oxalate and subsequent deposition in various tissues, leading to kidney stones and kidney failure.
Glycine is a simple amino acid that plays a crucial role in the body. According to the medical definition, glycine is an essential component for the synthesis of proteins, peptides, and other biologically important compounds. It is also involved in various metabolic processes, such as the production of creatine, which supports muscle function, and the regulation of neurotransmitters, affecting nerve impulse transmission and brain function. Glycine can be found as a free form in the body and is also present in many dietary proteins.
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.
Glycine receptors (GlyRs) are ligand-gated ion channel proteins that play a crucial role in mediating inhibitory neurotransmission in the central nervous system. They belong to the Cys-loop family of receptors, which also includes GABA(A), nicotinic acetylcholine, and serotonin receptors.
GlyRs are composed of pentameric assemblies of subunits, with four different subunit isoforms (α1, α2, α3, and β) identified in vertebrates. The most common GlyR composition consists of α and β subunits, although homomeric receptors composed solely of α subunits can also be formed.
When glycine binds to the orthosteric site on the extracellular domain of the receptor, it triggers a conformational change that leads to the opening of an ion channel, allowing chloride ions (Cl-) to flow through and hyperpolarize the neuronal membrane. This inhibitory neurotransmission is essential for regulating synaptic excitability, controlling motor function, and modulating sensory processing in the brainstem, spinal cord, and other regions of the central nervous system.
Dysfunction of GlyRs has been implicated in various neurological disorders, including hyperekplexia (startle disease), epilepsy, chronic pain, and neurodevelopmental conditions such as autism spectrum disorder.
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.
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.
Alanine is an alpha-amino acid that is used in the biosynthesis of proteins. The molecular formula for alanine is C3H7NO2. It is a non-essential amino acid, which means that it can be produced by the human body through the conversion of other nutrients, such as pyruvate, and does not need to be obtained directly from the diet.
Alanine is classified as an aliphatic amino acid because it contains a simple carbon side chain. It is also a non-polar amino acid, which means that it is hydrophobic and tends to repel water. Alanine plays a role in the metabolism of glucose and helps to regulate blood sugar levels. It is also involved in the transfer of nitrogen between tissues and helps to maintain the balance of nitrogen in the body.
In addition to its role as a building block of proteins, alanine is also used as a neurotransmitter in the brain and has been shown to have a calming effect on the nervous system. It is found in many foods, including meats, poultry, fish, eggs, dairy products, and legumes.
Sensitivity and specificity are statistical measures used to describe the performance of a diagnostic test or screening tool in identifying true positive and true negative results.
* Sensitivity refers to the proportion of people who have a particular condition (true positives) who are correctly identified by the test. It is also known as the "true positive rate" or "recall." A highly sensitive test will identify most or all of the people with the condition, but may also produce more false positives.
* Specificity refers to the proportion of people who do not have a particular condition (true negatives) who are correctly identified by the test. It is also known as the "true negative rate." A highly specific test will identify most or all of the people without the condition, but may also produce more false negatives.
In medical testing, both sensitivity and specificity are important considerations when evaluating a diagnostic test. High sensitivity is desirable for screening tests that aim to identify as many cases of a condition as possible, while high specificity is desirable for confirmatory tests that aim to rule out the condition in people who do not have it.
It's worth noting that sensitivity and specificity are often influenced by factors such as the prevalence of the condition in the population being tested, the threshold used to define a positive result, and the reliability and validity of the test itself. Therefore, it's important to consider these factors when interpreting the results of a diagnostic test.
Alpha-ketoglutaric acid, also known as 2-oxoglutarate, is not an acid in the traditional sense but is instead a key molecule in the Krebs cycle (citric acid cycle), which is a central metabolic pathway involved in cellular respiration. Alpha-ketoglutaric acid is a crucial intermediate in the process of converting carbohydrates, fats, and proteins into energy through oxidation. It plays a vital role in amino acid synthesis and the breakdown of certain amino acids. Additionally, it serves as an essential cofactor for various enzymes involved in numerous biochemical reactions within the body. Any medical conditions or disorders related to alpha-ketoglutaric acid would typically be linked to metabolic dysfunctions or genetic defects affecting the Krebs cycle.
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.
Glycine transaminase
Glycine-oxaloacetate transaminase
Alanine-glyoxylate transaminase
List of EC numbers (EC 2)
Serine-pyruvate transaminase
Serine-glyoxylate transaminase
Diaminobutyrate-2-oxoglutarate transaminase
International Working Group on Neurotransmitter Related Disorders
4-aminobutyrate transaminase
Methionine-glyoxylate transaminase
Kynurenine-glyoxylate transaminase
4-aminobutyrate-pyruvate transaminase
Aromatic-amino-acid-glyoxylate transaminase
List of MeSH codes (D08)
Kynurenic acid
Staphylococcus aureus
Serine
Amino acid
Biochemistry
Succinic semialdehyde dehydrogenase deficiency
Γ-Aminobutyric acid
Chromosome 12
Affinity chromatography
Biosynthesis
Acetolactate synthase
Pyridoxal phosphate
Amino acid synthesis
List of OMIM disorder codes
List of diseases (G)
Vitamin B6
Glycine transaminase - Wikipedia
GeneOntology Annotation
Direct and Functional Biomarkers of Vitamin B6 Status
PAR-07-159: National Cooperative Drug Discovery Groups for the Treatment of Mental Disorders, Drug or Alcohol Addiction (U19)
metabolism of essential amino acids
BIOPRO J
Stiff Person Syndrome: Practice Essentials, Background, Pathophysiology
The American | DADOSPDF
WormFlux: mechanistic analysis of C. elegans metabolism
Neurochemistry & Psychopharmacology (Lecture Notes) - Flashcard Maker
SACOL RS02165 - AureoWiki
Сечові камені - Урогенітальні розлади - MSD Manual Professional Edition
SACOL0430 - AureoWiki
L-Lysine 6-Transaminase | Profiles RNS
Conversion Details
1 - Calforex montreal taux de change
AGXT gene: MedlinePlus Genetics
Kupffer cells. Medical search
SustainPineDB
Pesquisa | Prevenção e Controle de Câncer
IPR015424 | Syntrophy Portal
"sequence id","alias","species","description",...
2023 ICD-10-CM Diagnosis Code E72.81: Disorders of gamma aminobutyric acid metabolism
DeCS 2019 - June 12, 2019 version
Genetic Brain Disorders | MedlinePlus
DeCS 2019 - June 12, 2019 version
DeCS 2018 - July 31, 2018 version
DeCS 2017 - July 04, 2017 version
Pyruvate4
- Catalysis of the reaction: L-alanine + glyoxylate = pyruvate + glycine. (umassmed.edu)
- Glycine radical, Pyruvate formate lyase-like [Interproscan]. (ntu.edu.sg)
- In the liver, alanine transaminase transfers the ammonia to α-KG and regenerates pyruvate. (medmuv.com)
- Li, J. (2002) Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase FEBS Lett 527 199-204. (unipr.it)
Aminotransferase6
- The systematic name of this enzyme class is glycine:2-oxoglutarate aminotransferase. (wikipedia.org)
- Other names in common use include glutamic-glyoxylic transaminase, glycine aminotransferase, glyoxylate-glutamic transaminase, L-glutamate:glyoxylate aminotransferase, and glyoxylate-glutamate aminotransferase. (wikipedia.org)
- In the peroxisome, alanine-glyoxylate aminotransferase converts a compound called glyoxylate to the protein building block (amino acid) glycine. (medlineplus.gov)
- Most of the AGXT gene mutations decrease or eliminate alanine-glyoxylate aminotransferase activity, which impairs the conversion of glyoxylate to glycine. (medlineplus.gov)
- 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)
- 3 mmol/L), lower median numbers of leukocytes in cerebrospinal fluid, and higher median serum levels of alanine aminotransferase and aspartate transaminase than did patients who were positive for enteroviruses. (cdc.gov)
Alanine4
- 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)
- This reaction is catalyzed by alanine transaminase, ALT. (medmuv.com)
- 3-Hydroxykynurenine transaminase identity with alanine glyoxylate transaminase. (unipr.it)
- alanine transaminase (alt) estimation kit in serum by mod. (tendersingujarat.com)
Metabolism3
- This enzyme participates in glycine, serine and threonine metabolism. (wikipedia.org)
- Functional biomarkers include erythrocyte transaminase activities and, more recently, plasma levels of metabolites involved in PLP-dependent reactions, such as the kynurenine pathway, one-carbon metabolism, transsulfuration (cystathionine), and glycine decarboxylation (serine and glycine). (nih.gov)
- Amino acid metabolism has extremely extensive effects in cancer cells, including, but not limited to, (1) establishing amino acid pools as building blocks, especially the production of non-essential amino acids … An overview of the metabolism of the sulfur amino acids is depicted in Fig. The outline of glycine metabolism is depicted in Fig. Oxidation via TCA cycle to produce energy (about 10-15% of body needs). (slimwithlynne.com)
Glyoxylate2
- In enzymology, a glycine transaminase (EC 2.6.1.4) is an enzyme that catalyzes the chemical reaction glycine + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } glyoxylate + L-glutamate Thus, the two substrates of this enzyme are glycine and 2-oxoglutarate, whereas its two products are glyoxylate and L-glutamate. (wikipedia.org)
- All AGXT gene mutations result in the accumulation of glyoxylate, which is converted to oxalate instead of glycine. (medlineplus.gov)
Enzyme2
- This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. (wikipedia.org)
- Here, we report a noncanonical FAD-dependent enzyme Orf1 that adds a glycine-derived N-formimidoyl group to glycinothricin to form the antibiotic BD-12. (hokudai.ac.jp)
Reactions1
- This reactions strongly favours synthesis of glycine. (wikipedia.org)
Disease1
- Elevated levels of the transaminases can indicate myocardial infarction, hepatic disease, muscular dystrophy, or organ damage. (cdc.gov)
Serine5
- This enzyme participates in glycine, serine and threonine metabolism. (wikipedia.org)
- Reductive amination (transamination) of this ketone by phosphoserine transaminase (EC 2.6.1.52 ) yields 3-phosphoserine ( O -phosphoserine) which is hydrolyzed to serine by phosphoserine phosphatase (EC 3.1.3.3 ). (iiab.me)
- Serine hydroxymethyltransferase (SHMT = serine transhydroxymethylase) also catalyzes the reversible conversions of L -serine to glycine (retro-aldol cleavage) and 5,6,7,8-tetrahydrofolate to 5,10-methylenetetrahydrofolate (mTHF) (hydrolysis). (iiab.me)
- Industrially, L -serine is produced from glycine and methanol catalyzed by hydroxymethyltransferase. (iiab.me)
- Indeed, flux through glycolysis and lactate secretion remains a hallmark of many tumor cells, presumably to facilitate biosynthesis of ribose, purines (via serine and glycine), and lipid headgroups (via glycerol-3-phosphate and serine). (biomedcentral.com)
Cysteine2
- It is the precursor to several amino acids including glycine and cysteine , as well as tryptophan in bacteria. (iiab.me)
- cysteine and glycine rich protein 3. (gsea-msigdb.org)
Glutamate7
- In enzymology, a glycine transaminase (EC 2.6.1.4) is an enzyme that catalyzes the chemical reaction glycine + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } glyoxylate + L-glutamate Thus, the two substrates of this enzyme are glycine and 2-oxoglutarate, whereas its two products are glyoxylate and L-glutamate. (wikipedia.org)
- A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the transfer of the amino group of GLYCINE onto 2-oxoglutarate to generate GLYOXYLATE and L-GLUTAMATE . (nih.gov)
- Glutamate can be packaged for release from synaptic clefts, and it can be acted on by several transaminases to transform it to either glutamine or GABA. (medscape.com)
- 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)
- We found that metabolism of glutamate to α-ketoglutarate by glutamate dehydrogenase or the glutamate-pyruvate or glutamate-oxaloacetate transaminases is not required for collagen protein production. (nih.gov)
- 1). The amino group is transferred to \-ketoglutarate by transaminase (PLP/PMP) to form glutamate , and then diaminated in the mitochondrion to yield NH 4 + by glutamate DHase . (idv.tw)
- Glutamate dehydrogenase is a key enzyme in the process because it generates the free NH4+ previously transferred to α-ketoglutarate from many amino acids by transaminases. (dentals.se)
Threonine1
- Encodes a threonine aldolase, involved in threonine degradation to glycine. (or.jp)
Liver4
- 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)
- The term transaminase is outdated and no longer used in liver disease. (wikidoc.org)
- Glycine in Carolina rinse solution reduces reperfusion injury, improves graft function, and increases graft survival after rat liver transplantation. (musc.edu)
- Liver enzyme abnormalities and monitoring: Persistent elevations in hepatic transaminase can occur. (nih.gov)
Biosynthesis1
- 10). ALA , which is synthesized from glycine and succinyl-CoA , is converted to PBG for biosynthesis of heme. (idv.tw)
Proline2
Hepatic1
- Elevated levels of the transaminases can indicate myocardial infarction, hepatic disease, muscular dystrophy, or organ damage. (cdc.gov)
Synthase1
- Glycine can also be formed from CO 2, NH 4 + , and mTHF in a reaction catalyzed by glycine synthase . (iiab.me)
Synthesis1
- This reactions strongly favours synthesis of glycine. (wikipedia.org)
Activity2
- The latter result provides evidence they are deficient in activity of glycine N-methyltransferase (GNMT). (nih.gov)
- Increasd levels of 4-hydroxyglutamate could also result from decreased activity of glutamic-oxaloacetic transaminase 2 (GOT2 = AspAT in figure 1 from ref 4) (1). (blogspot.com)
Primarily1
- In stiff person syndrome, spinal interneurons function to inhibit spontaneous discharges from spinal motor neurons, primarily through the action of glycine. (medscape.com)
GABA1
- [ 25 ] and GABA-transaminase. (medscape.com)
Human1
- It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine . (iiab.me)
Solution1
- meglumin - 6.25 mg, glycofurfural - 100 mg, poloxamer 188 - 50 mg, Glycine - 5 mg, sodium chloride - 3.5 mg, sodium hydroxide solution 1M - pH 8.6-9, water d / and - up to 1 ml. (bestpharmbuy.com)