Aspartate Ammonia-Lyase
Phenylalanine Ammonia-Lyase
Ammonia
Ammonia-Lyases
Ethanolamine Ammonia-Lyase
Aspartate Aminotransferases
Rhodotorula
Basidiomycota
Aspartate Carbamoyltransferase
Salicylic Acid
Phenylpropionates
ATP Citrate (pro-S)-Lyase
Aspartic Acid
Plant Leaves
Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue. (1/36)
A thermostable aspartase gene (aspB) from Bacillus sp. YM55-1 was cloned and the gene sequenced. The aspB gene (1407 bp ORF) encodes a protein with a molecular mass of 51 627 Da, consisting of 468 amino-acid residues. An amino-acid sequence comparison revealed that Bacillus YM55-1 aspartase shared 71% homology with Bacillus subtilis aspartase and 49% with Escherichia coli and Pseudomonas fluorescens aspartases. The E. coli TK237/pUCASPB strain, which was obtained by transforming E. coli TK237 (aspartase-null strain) with a vector plasmid (pUCASPB) containing the cloned aspB gene, produced a large amount of the enzyme corresponding to > 10% of the total soluble protein. The over-expressed recombinant enzyme (native molecular mass: 200 kDa) was purified effectively and rapidly using heat treatment and affinity chromatography. In order to probe the catalytic residues of this enzyme, two conserved amino-acid residues, Lys183 and His134, were individually mutated to alanine. Although the tertiary structure of each mutant was estimated to be the same as that of wild-type aspartase in CD and fluorescence measurements, the Lys183Ala mutant lost its activity completely, whereas His134Ala retained full activity. This finding suggests that Lys183 may be involved in the catalytic activity of this thermostable Bacillus YM55-1 aspartase. (+info)A monomeric L-aspartase obtained by in vitro selection. (2/36)
By mimicking the partial spatial structure of the dimer of the l-aspartase subunit, the central ten-helix bundle, and an "active site" between the cleft of domain 1 (D1) and domain 3 (D3) from different subunits, we designed l-aspartase variants, in which D1D2 and D2D3 were ligated with a random hexapeptide loop. As expected, we obtained the variant with the highest activity (relative activity is 21.3% of the native enzyme, named as drAsp017) by in vitro selection. The molecular weight of this variant, obtained from size-exclusion column chromatography, is about 81 kDa, which indicates that it is indeed a monomer, whereas native l-aspartase is a tetramer. The activity-reversibility of drAsp017 (10(-7) m) was 80% after incubation for 30 min at 50 degrees C, while native enzyme only retained about 17% under the same conditions. Reactivation of drAsp017 denatured in 4 m guanidine HCl was independent of protein concentration at up to 20 x 10(-8) m at 25 degrees C, whereas the protein concentration of native enzyme strongly affected its reactivation under the above conditions. The sensitivity of drAsp017 (10(-7) m) to effective factors in the fumarate-amination reaction compared with native enzyme was also determined. Half-saturating concentrations of the activator l-aspartate and Mg2+ for drAsp017 (0.8 and 0.5 mm, respectively) are much higher than that of the native enzyme (0.10 and 0.15 mm, respectively). The data show that a monomeric l-aspartase is obtained by in vitro selection. Thus, the conversion of oligomeric proteins into their functional monomers could have important applications. (+info)Thermostable aspartase from a marine psychrophile, Cytophaga sp. KUC-1: molecular characterization and primary structure. (3/36)
We found that a psychrophilic bacterium isolated from Antarctic seawater, Cytophaga sp. KUC-1, abundantly produces aspartase [EC4.3.1.1], and the enzyme was purified to homogeneity. The molecular weight of the enzyme was estimated to be 192,000, and that of the subunit was determined to be 51,000: the enzyme is a homotetramer. L-Aspartate was the exclusive substrate. The optimum pH in the absence and presence of magnesium ions was determined to be pH 7.5 and 8.5, respectively. The enzyme was activated cooperatively by the presence of L-aspartate and by magnesium ions at neutral and alkaline pHs. In the deamination reaction, the K(m) value for L-aspartate was 1.09 mM at pH 7.0, and the S(1/2) value was 2.13 mM at pH 8.5. The V(max) value were 99.2 U/mg at pH 7.0 and 326 U/mg at pH 8.5. In the amination reaction, the K(m) values for fumarate and ammonium were 0.797 and 25.2 mM, respectively, and V(max) was 604 U/mg. The optimum temperature of the enzyme was 55 degrees C. The enzyme showed higher pH and thermal stabilities than that from mesophile: the enzyme was stable in the pH range of 4.5-10.5, and about 80% of its activity remained after incubation at 50 degrees C for 60 min. The gene encoding the enzyme was cloned into Escherichia coli, and its nucleotides were sequenced. The gene consisted of an open reading frame of 1,410-bp encoding a protein of 469 amino acid residues. The amino acid sequence of the enzyme showed a high degree of identity to those of other aspartases, although these enzymes show different thermostabilities. (+info)Possible physiological roles of aspartase, NAD- and NADP-requiring glutamate dehydrogenases of Pseudomonas fluorescens. (4/36)
The levels of aspartase, NADP- and NAD-requiring glutamate dehydrogenases (GDHs) in Pseudomonas fluorescens grown under various nutritional conditions were determined. NADP-GDH showed the highest value on glucose-ammonium sulfate medium and markedly lower values on amino-acid and casamino-acids media, while the reverse was found for the NAD-GDH, as in the case of other microorganisms with two GDHs. Aspartase did not show a marked variation between the media examined. Glucose nutritionally induced NADP-GDH but suppressed NAD-GDH; and it had no effect on aspartase, which was slightly induced by casamino acids. Transfer of the cells grown on glucose-ammonium sulfate medium to casamino-acids medium clearly increased the levels of NAD-GDH and aspartase, while addition of chloramphenicol to the media abolished the increases, suggesting that the increases were due to de novo synthesis of the enzyme proteins. These results indicate that the aspartase of this microorganism has a different function from those in others, including Escherichia coli. (+info)Enzymes involved in anaerobic respiration appear to play a role in Actinobacillus pleuropneumoniae virulence. (5/36)
Actinobacillus pleuropneumoniae, the etiological agent of porcine pleuropneumonia, is able to survive on respiratory epithelia, in tonsils, and in the anaerobic environment of encapsulated sequesters. It was previously demonstrated that a deletion of the anaerobic dimethyl sulfoxide reductase gene (dmsA) results in attenuation in acute disease (N. Baltes, S. Kyaw, I. Hennig-Pauka, and G. F. Gerlach, Infect. Immun. 71:6784-6792, 2003). In the present study, using two-dimensional polyacrylamide gel electrophoresis and quadrupole time-of-flight mass spectrometry, we identified an aspartate ammonia-lyase (AspA) which is upregulated upon induction with bronchoalveolar lavage fluid (BALF). This enzyme is involved in the production of fumarate, an alternative electron acceptor under anaerobic conditions. The coding gene (aspA) was cloned and shown to be present in all A. pleuropneumoniae serotype reference strains. The transcriptional start point was identified downstream of a putative FNR binding motif, and BALF-dependent activation of aspA was confirmed by construction of an isogenic A. pleuropneumoniae mutant carrying a chromosomal aspA::luxAB transcriptional fusion. Two aspA deletion mutants, A. pleuropneumoniae DeltaaspA and A. pleuropneumoniae DeltaaspADeltadmsA, were constructed, both showing reduced growth under anaerobic conditions in vitro. Pigs challenged with either of the two mutants in an aerosol infection model showed a lower lung lesion score than that of the A. pleuropneumoniae wild-type (wt) controls. Pigs challenged with A. pleuropneumoniae DeltaaspADeltadmsA had a significantly lower clinical score, and this mutant was rarely reisolated from unaltered lung tissue; in contrast, A. pleuropneumoniae DeltaaspA and the A. pleuropneumoniae wt were consistently reisolated in high numbers. These results suggest that enzymes involved in anaerobic respiration are necessary for the pathogen's ability to persist on respiratory tract epithelium and play an important role in A. pleuropneumoniae pathogenesis. (+info)Deletion of the anaerobic regulator HlyX causes reduced colonization and persistence of Actinobacillus pleuropneumoniae in the porcine respiratory tract. (6/36)
Actinobacillus pleuropneumoniae, the etiological agent of porcine pleuropneumonia, is able to persist on respiratory epithelia, in tonsils, and in the anaerobic environment of encapsulated lung sequesters. We have demonstrated previously that putative HlyX-regulated genes, coding for dimethyl sulfoxide (DMSO) reductase and aspartate ammonia lyase, are upregulated during infection and that deletions in these genes result in attenuation of the organism. The study presented here investigates the role of HlyX, the fumarate nitrate reductase regulator (FNR) homologue of A. pleuropneumoniae. By constructing an isogenic A. pleuropneumoniae hlyX mutant, the HlyX protein is shown to be responsible for upregulated expression of both DMSO reductase and aspartate ammonia lyase (AspA) under anaerobic conditions. In a challenge experiment the A. pleuropneumoniae hlyX mutant is shown to be highly attenuated, unable to persist in healthy lung epithelium and tonsils, and impaired in survival inside sequestered lung tissue. Further, using an A. pleuropneumoniae strain carrying the luxAB genes as transcriptional fusion to aspA on the chromosome, the airway antioxidant glutathione was identified as one factor potentially responsible for inducing HlyX-dependent gene expression of A. pleuropneumoniae in epithelial lining fluid. (+info)Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase. (7/36)
L-Aspartase was purified from Bacillus subtilis, its N-terminal amino acid sequence was determined to construct a probe for the aspartase gene, and the gene (termed ansB) was cloned and sequenced. A second gene (termed ansA) was found upstream of the ansB gene and coded for L-asparaginase. These two genes were in an operon designated the ans operon, which is 80% cotransformed with the previously mapped aspH1 mutation at 215 degrees. Primer extension analysis of in vivo ans mRNA revealed two transcription start sites, depending on the growth medium. In wild-type cells in log-phase growth in 2x YT medium (tryptone-yeast extract rich medium), the ans transcript began at -67 relative to the translation start site, while cells in log-phase growth or sporulating (t1 to t4) in 2x SG medium (glucose nutrient broth-based moderately rich medium) had an ans transcript which began at -73. The level of the -67 transcript was greatly increased in an aspH mutant grown in 2x YT medium; the -67 transcript also predominated when this mutant was grown in 2x SG medium, although the -73 transcript was also present. In vitro transcription of the ans operon by RNA polymerase from log-phase cells grown in 2x YT medium and log-phase or sporulating cells grown in 2x SG medium yielded only the -67 transcript. Depending on the growth medium, the levels of asparaginase and aspartase were from 2- to 40-fold higher in an aspH mutant than in wild-type cells, and evidence was obtained indicating that the gene defined by the aspH1 mutation codes for a trans-acting transcriptional regulatory factor. In wild-type cells grown in 2x SG medium, the levels of both aspartase and asparaginase decreased significantly by t0 of sporulation but then showed a small increase, which was mirrored by changes in the level of beta-galactosidase from an ansB-lacZ fusion. The increase in the activities of ans operon enzymes between t2 and t5 of sporulation was found primarily in the forespore, and the great majority of the increased was found in the mature spore. However, throughout sporulation the only ans transcript detected was the -73 form, and no sporulation-specific RNA polymerase tested yielded a -73 transcript in vitro. (+info)A missense mutation causes aspartase deficiency in Yersinia pestis. (8/36)
(+info)Aspartate ammonia-lyase is an enzyme that plays a role in the metabolism of certain amino acids. Its systematic name is L-aspartate ammonia-lyase (ADI), and it is also known as aspartase. This enzyme is responsible for catalyzing the conversion of L-aspartic acid to fumaric acid and ammonia.
L-aspartic acid + H2O → fumaric acid + NH3
Aspartate ammonia-lyase is found in various organisms, including bacteria, fungi, and plants. In bacteria, this enzyme is involved in the biosynthesis of several essential amino acids. In plants, aspartate ammonia-lyase plays a role in the synthesis of certain aromatic compounds. The human body does not produce this enzyme, so it is not relevant to medical definitions in the context of human health and disease.
Phenylalanine Ammonia-Lyase (PAL) is a enzyme that catalyzes the non-oxidative deamination of phenylalanine to trans-cinamic acid, releasing ammonia in the process. This reaction is a key step in the biosynthesis of various aromatic compounds in plants and microorganisms. In humans, PAL is not normally present, but its introduction through gene therapy has been studied as a potential treatment for phenylketonuria (PKU), a genetic disorder characterized by an inability to metabolize phenylalanine properly, leading to its accumulation in the body and potential neurological damage.
Ammonia is a colorless, pungent-smelling gas with the chemical formula NH3. It is a compound of nitrogen and hydrogen and is a basic compound, meaning it has a pH greater than 7. Ammonia is naturally found in the environment and is produced by the breakdown of organic matter, such as animal waste and decomposing plants. In the medical field, ammonia is most commonly discussed in relation to its role in human metabolism and its potential toxicity.
In the body, ammonia is produced as a byproduct of protein metabolism and is typically converted to urea in the liver and excreted in the urine. However, if the liver is not functioning properly or if there is an excess of protein in the diet, ammonia can accumulate in the blood and cause a condition called hyperammonemia. Hyperammonemia can lead to serious neurological symptoms, such as confusion, seizures, and coma, and is treated by lowering the level of ammonia in the blood through medications, dietary changes, and dialysis.
Anabaena variabilis is a species of cyanobacteria (blue-green algae) that can form filamentous colonies. It is capable of fixing atmospheric nitrogen, making it an important contributor to the nitrogen cycle in aquatic environments. The term 'variabilis' refers to the variable size and shape of its cells.
Here's a simple medical definition:
Anabaena variabilis: A species of filamentous cyanobacteria known for its ability to fix nitrogen, contributing to the nitrogen cycle in aquatic environments. Its cells can vary in size and shape.
Ammonia-lyases are a class of enzymes that catalyze the removal of an amino group from a substrate, releasing ammonia in the process. These enzymes play important roles in various biological pathways, including the biosynthesis and degradation of various metabolites such as amino acids, carbohydrates, and aromatic compounds.
The reaction catalyzed by ammonia-lyases typically involves the conversion of an alkyl or aryl group to a carbon-carbon double bond through the elimination of an amine group. This reaction is often reversible, allowing the enzyme to also catalyze the addition of an amino group to a double bond.
Ammonia-lyases are classified based on the type of substrate they act upon and the mechanism of the reaction they catalyze. Some examples of ammonia-lyases include aspartate ammonia-lyase, which catalyzes the conversion of aspartate to fumarate, and tyrosine ammonia-lyase, which converts tyrosine to p-coumaric acid.
These enzymes are important in both plant and animal metabolism and have potential applications in biotechnology and industrial processes.
Ethanolamine ammonia-lyase (EAL) is an enzyme that plays a role in the breakdown and metabolism of certain compounds in the body. Its primary function is to catalyze the conversion of ethanolamine, a type of amino alcohol, into acetaldehyde and ammonia. This reaction is an important step in the catabolism of phosphatidylethanolamines, which are major components of cell membranes.
EAL is also known as "ethanolamine deaminase" or "N-ethanolamine deaminase." It requires the cofactor pyridoxal phosphate (PLP) to facilitate the reaction. The enzyme's activity has been identified in various organisms, including bacteria, archaea, and plants, but not in mammals. In some bacterial species, EAL is involved in the biosynthesis of certain amino acids and other biomolecules.
The reaction catalyzed by ethanolamine ammonia-lyase:
Ethanolamine + H2O + PLP → Acetaldehyde + Ammonia + Methylglyoxal + PLP
P-Fluorophenylalanine (p-FPA) is not a medical term, but a chemical compound used in research and medical fields. It's a type of amino acid that is used as a building block for proteins, similar to the naturally occurring amino acid phenylalanine. However, p-FPA has a fluorine atom attached to its para position (one of the possible positions on the phenyl ring).
This compound can be used in various research applications, including the study of protein synthesis and enzyme function. It's also been explored as a potential therapeutic agent for certain medical conditions, such as cancer and neurological disorders. However, more research is needed to establish its safety and efficacy for these uses.
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.
Rhodotorula is a genus of unicellular, budding yeasts that are commonly found in the environment, particularly in damp and nutrient-rich places such as soil, water, and vegetation. They are characterized by their ability to produce carotenoid pigments, which give them a distinctive pinkish-red color.
While Rhodotorula species are not typically associated with human disease, they can occasionally cause infections in people with weakened immune systems or underlying medical conditions. These infections can occur in various parts of the body, including the respiratory tract, urinary tract, and skin.
Rhodotorula infections are usually treated with antifungal medications, such as fluconazole or amphotericin B. Preventing exposure to sources of Rhodotorula, such as contaminated medical equipment or water supplies, can also help reduce the risk of infection.
Basidiomycota is a phylum in the kingdom Fungi that consists of organisms commonly known as club fungi or club mushrooms. The name Basidiomycota is derived from the presence of a characteristic reproductive structure called a basidium, which is where spores are produced.
The basidiomycetes include many familiar forms such as mushrooms, toadstools, bracket fungi, and other types of polypores. They have a complex life cycle that involves both sexual and asexual reproduction. The sexual reproductive stage produces a characteristic fruiting body, which may be microscopic or highly visible, depending on the species.
Basidiomycota fungi play important ecological roles in decomposing organic matter, forming mutualistic relationships with plants, and acting as parasites on other organisms. Some species are economically important, such as edible mushrooms, while others can be harmful or even deadly to humans and animals.
Aspartate carbamoyltransferase (ACT) is a crucial enzyme in the urea cycle, which is the biochemical pathway responsible for the elimination of excess nitrogen waste from the body. This enzyme catalyzes the second step of the urea cycle, where it facilitates the transfer of a carbamoyl group from carbamoyl phosphate to aspartic acid, forming N-acetylglutamic semialdehyde and releasing phosphate in the process.
The reaction catalyzed by aspartate carbamoyltransferase is as follows:
Carbamoyl phosphate + L-aspartate → N-acetylglutamic semialdehyde + P\_i + CO\_2
This enzyme plays a critical role in maintaining nitrogen balance and preventing the accumulation of toxic levels of ammonia in the body. Deficiencies or mutations in aspartate carbamoyltransferase can lead to serious metabolic disorders, such as citrullinemia and hyperammonemia, which can have severe neurological consequences if left untreated.
Salicylic Acid is a type of beta hydroxy acid (BHA) that is commonly used in dermatology due to its keratolytic and anti-inflammatory properties. It works by causing the cells of the epidermis to shed more easily, preventing the pores from becoming blocked and promoting the growth of new skin cells. Salicylic Acid is also a potent anti-inflammatory agent, which makes it useful in the treatment of inflammatory acne and other skin conditions associated with redness and irritation. It can be found in various over-the-counter skincare products, such as cleansers, creams, and peels, as well as in prescription-strength formulations.
Phenylpropionates are a group of organic compounds that contain a phenyl group and a propionate group. In the context of pharmaceuticals, phenylpropionates often refer to a specific type of esterified hormone, such as testosterone phenylpropionate or nandrolone phenylpropionate. These esters are used in some forms of anabolic-androgenic steroids and are created by attaching a phenylpropionate group to the parent hormone molecule. This modification allows for a slower release and longer duration of action when administered intramuscularly.
It is important to note that these substances have medical uses, but they also carry risks and potential side effects, especially when used inappropriately or without medical supervision. They are controlled substances in many countries due to their potential for misuse and abuse.
Aspartic acid is an α-amino acid with the chemical formula HO2CCH(NH2)CO2H. It is one of the twenty standard amino acids, and it is a polar, negatively charged, and hydrophilic amino acid. In proteins, aspartic acid usually occurs in its ionized form, aspartate, which has a single negative charge.
Aspartic acid plays important roles in various biological processes, including metabolism, neurotransmitter synthesis, and energy production. It is also a key component of many enzymes and proteins, where it often contributes to the formation of ionic bonds and helps stabilize protein structure.
In addition to its role as a building block of proteins, aspartic acid is also used in the synthesis of other important biological molecules, such as nucleotides, which are the building blocks of DNA and RNA. It is also a component of the dipeptide aspartame, an artificial sweetener that is widely used in food and beverages.
Like other amino acids, aspartic acid is essential for human health, but it cannot be synthesized by the body and must be obtained through the diet. Foods that are rich in aspartic acid include meat, poultry, fish, dairy products, eggs, legumes, and some fruits and vegetables.
I believe there may be a slight misunderstanding in your question. "Plant leaves" are not a medical term, but rather a general biological term referring to a specific organ found in plants.
Leaves are organs that are typically flat and broad, and they are the primary site of photosynthesis in most plants. They are usually green due to the presence of chlorophyll, which is essential for capturing sunlight and converting it into chemical energy through photosynthesis.
While leaves do not have a direct medical definition, understanding their structure and function can be important in various medical fields, such as pharmacognosy (the study of medicinal plants) or environmental health. For example, certain plant leaves may contain bioactive compounds that have therapeutic potential, while others may produce allergens or toxins that can impact human health.
A plant disease is a disorder that affects the normal growth and development of plants, caused by pathogenic organisms such as bacteria, viruses, fungi, parasites, or nematodes, as well as environmental factors like nutrient deficiencies, extreme temperatures, or physical damage. These diseases can cause various symptoms, including discoloration, wilting, stunted growth, necrosis, and reduced yield or productivity, which can have significant economic and ecological impacts.
Aspartate ammonia-lyase
Threo-3-hydroxy-D-aspartate ammonia-lyase
Erythro-3-hydroxyaspartate ammonia-lyase
Threo-3-hydroxyaspartate ammonia-lyase
Fumarate lyase
Aspartic acid
Urea cycle
Amino acid
Cystathionine gamma-lyase
Argininosuccinate lyase
List of MeSH codes (D08)
List of EC numbers (EC 4)
Purine nucleotide cycle
Essential amino acid
Argininosuccinate synthase
Cystathionine beta-lyase
Pyridoxal phosphate
List of EC numbers (EC 6)
Nucleotide
Amino acid synthesis
Biosynthesis
Aspartame
List of EC numbers (EC 2)
Raymond C. Stevens
List of enzymes
Phenylalanine
List of EC numbers (EC 1)
Aspartate ammonia-lyase - Wikipedia
SCOPe 2.08: Family a.127.1.1: L-aspartase/fumarase
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MMTB
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Nucleotide metabolism
Biochem block 3, wk 3- AA degradation and urea cycle Flashcards
Pyruvate5
- In pathway VI, the mutase glmSE converts glutamate to (2S,3S)-3-methylaspartate, the lyase mal forms 2-methylfumarate (mesaconate), the hydratase fumD forms (S)-2-methylmalate (citramalate), and a lyase forms acetate and pyruvate. (lbl.gov)
- In the liver, alanine transaminase transfers the ammonia to α-KG and regenerates pyruvate. (medmuv.com)
- pyruvate formate-lyase 1 [Ensembl]. (ntu.edu.sg)
- Glycine radical, Pyruvate formate lyase-like [Interproscan]. (ntu.edu.sg)
- protein_coding" "AAC74323","adhE","Escherichia coli","fused acetaldehyde-CoA dehydrogenase/iron-dependent alcohol dehydrogenase/pyruvate-formate lyase deactivase [Ensembl]. (ntu.edu.sg)
Aminotransferase1
- 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)
Enzyme8
- The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction L-aspartate ⇌ {\displaystyle \rightleftharpoons } fumarate + NH3 The reaction is the basis of the industrial synthesis of aspartate. (wikipedia.org)
- This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. (wikipedia.org)
- The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). (wikipedia.org)
- This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism. (wikipedia.org)
- They are inactive forms of the enzyme argininosuccinate lyase. (lookformedical.com)
- Argininosuccinic acid is produced from the condensation of citrulline and aspartate by a synthetase enzyme. (medscape.com)
- It is then cleaved to produce fumarate and arginine by a lyase enzyme. (medscape.com)
- In addition, L-cysteine can be converted into hydrogen sulfide and pyruvic acid through the action of the enzyme cystathionine gamma-lyase. (cannabisdatabase.ca)
Fumarate1
- In pathway II, glutamate and oxaloacetate are transaminated to 2-oxoglutarate and aspartate, and the aspartate is cleaved to fumarate and ammonium by aspA. (lbl.gov)
Argininosuccinate lyase1
- Argininosuccinate is cleaved in the cytosol by argininosuccinate lyase ( AL ), which is coded on human chromosome 7 ( Fig. 44-6 , reaction 4). (nih.gov)
Metabolism2
- VIENNA, Austria - Fecal microbiota transplants (FMT) can reset gut microbiota leading to strengthened gut barrier function and mucosal immunity, along with improved ammonia metabolism in patients with cirrhosis, show data from a pilot study now expanded into a large multisite UK trial. (medscape.com)
- Edwards explained that FMT modifies the gut microbiome, which metabolically reprograms by replenishing enzymes sourced from commensal bacteria that were previously depleted, causing a rise in ammonia metabolism such that it produces energy for the immune system and gut barrier. (medscape.com)
Cytosol2
- A total of 5 enzymes in 2 subcellular compartments (mitochondrial matrix and cytosol) convert ammonia into urea, which is excreted by the kidney (see image below). (medscape.com)
- Citrulline is released to the cytosol, where it condenses with aspartate to form argininosuccinate via argininosuccinate synthetase ( AS ) ( Fig. 44-6 , reaction 3). (nih.gov)
Glutamate dehydrogenase4
- GapMind represents glutamate degradation using MetaCyc pathways L-glutamate degradation I (glutamate dehydrogenase, link ), pathway II via aspartate ammonia-lyase ( link ), and pathway VI via glutamate mutase ( link ). (lbl.gov)
- Comment: GdhA is glutamate dehydrogenase (forming 2-oxoglutarate and ammonia). (lbl.gov)
- Ammonia incorporation in animals occurs through the actions of glutamate dehydrogenase and glutamine synthase. (medmuv.com)
- A pair of principal enzymes, glutamate dehydrogenase and glutamine synthatase, are found in all organisms and effect the conversion of ammonia into the amino acids glutamate and glutamine, respectively. (medmuv.com)
Urea1
- The urea cycle ( Fig. 44-6 ) mediates the removal of ammonia as urea in the amount of 10 to 20 g per day in the healthy adult. (nih.gov)
Amino acids1
- Reduced nitrogen enters the human body as dietary free amino acids, protein, and the ammonia produced by intestinal tract bacteria. (medmuv.com)
Ornithine1
- Carbamoyl phosphate is produced from ammonia and bicarbonate by carbamoylphosphate synthetase I. This reaction is stimulated by ornithine. (medscape.com)
Fumaric1
- Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. (wikipedia.org)
Citrulline2
- The diagnosis of citrin deficiency is established in an individual with characteristic biochemical findings (in general, increased blood or plasma concentration of ammonia, plasma or serum concentration of citrulline and arginine, plasma or serum threonine-to-serine ratio, and serum concentration of pancreatic secretory trypsin inhibitor) and identification of biallelic pathogenic variants in SLC25A13 . (nih.gov)
- Periodic measurement of plasma concentration of ammonia and citrulline, and serum concentration of PSTI for all phenotypes associated with citrin deficiency. (nih.gov)
Protein1
- Ammonia the highly toxic product of protein catabolism, is rapidly inactivated by a variety of reactions. (medmuv.com)
Enzymes1
- The functional groups transferred by these lyase enzymes include amino groups, water, and ammonia. (cliffsnotes.com)
Acid2
- Despite the broad substrate spectrum of methylaspartate lyase (MAL), some bulky substrates, such as caffeic acid, cannot be effectively accepted. (springeropen.com)
- 3-hydroxyisovaleric acid correlated positively with plasma ammonia. (biomedcentral.com)
Synthase1
- Comparative genome analysis of the congeneric species revealed the species-specific evolution of chrysin and apigenin biosynthetic genes, such as the S. baicalensis-specific tandem duplication of genes encoding phenylalanine ammonia lyase and chalcone synthase, and the S. barbata-specific duplication of genes encoding 4-CoA ligase. (big.ac.cn)
Converts1
- converts ammonia and bicarb to carbomoyl phosphate (where does this occur. (flashcardmachine.com)
Plasma2
- After 1 month, ammonia levels in the plasma were lower but higher in the feces, findings that were further enhanced at 3 months. (medscape.com)
- Plasma ammonia for example, is considered the best available biochemical read-out of AMD, but does not provide insight in other pathophysiological processes that may occur during AMD. (biomedcentral.com)
Levels1
- Edwards' co-investigator, Debbie L. Shawcross, MD, also from King's College London, added: "This landmark trial provides evidence that a fecal transplant can improve gut health by modifying the gut microbiome and reducing ammonia levels in patients with cirrhosis. (medscape.com)
Aspartic Acid1
- An enzyme that catalyzes the conversion of aspartic acid to ammonia and fumaric acid in plants and some microorganisms. (nih.gov)
Aminotransferase1
- 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. (tdmuv.com)
Alanine1
- In the liver, alanine transaminase transfers the ammonia to α-KG and regenerates pyruvate. (tdmuv.com)
Aspartase1
- Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. (wikipedia.org)
Reducing ammonia levels1
- Edwards' co-investigator, Debbie L. Shawcross, MD, also from King's College London, added: "This landmark trial provides evidence that a fecal transplant can improve gut health by modifying the gut microbiome and reducing ammonia levels in patients with cirrhosis. (medscape.com)
Reaction2
- Carbamoyl phosphate is produced from ammonia and bicarbonate by carbamoylphosphate synthetase I. This reaction is stimulated by ornithine. (medscape.com)
- Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma-lyase catalyzes the lower reaction. (iiab.me)
Urea cycle3
- The first step of the urea cycle is the conversion of excess nitrogen into ammonia, which is then incorporated into the cycle to be processed. (nutrifix-health.com)
- Because the urea cycle cannot continue without ornithine inside the mitochondria, ammonia disposal slows, and blood ammonia levels rise. (medscape.com)
- In urea cycle disorders, the nitrogen accumulates in the form of ammonia , a highly toxic substance, and is not removed from the body. (wikidoc.org)
Hyperammonemia1
- Childhood episodes of hyperammonemia (high ammonia levels in the blood) may be brought on by viral illnesses including chicken pox , high-protein meals, or even exhaustion . (wikidoc.org)
Synthetase1
- 16211) para-aminobenzoate synthetase/4-amino-4-deoxychorismate lyase pabBC BBZA01000002 CDS ARMA_0015 192. (go.jp)
Nitrogen1
- This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. (wikipedia.org)
Toxic3
- Ammonia is a highly toxic compound, and it is important that it is quickly converted into a less toxic form. (nutrifix-health.com)
- Urea is a less toxic compound than ammonia and can be safely eliminated from the body through the kidneys. (nutrifix-health.com)
- Ammonia the highly toxic product of protein catabolism, is rapidly inactivated by a variety of reactions. (tdmuv.com)
Glutamine1
- There is an alternative pathway for the excretion of ammonia in the body called the glutamine pathway . (nutrifix-health.com)
Liver1
- Modifying the microbial-associated ammonia production and utilization could reduce hepatic encephalopathy and deadly infections, said Lindsey A. Edwards, PhD, from the Institute of Liver Studies, King's College London, England, and co-lead investigator on the PROFIT trial , presenting here at the International Liver Congress of the European Association for the Study of the Liver (EASL) 2023. (medscape.com)