An enzyme that catalyzes the conversion of aspartic acid to ammonia and fumaric acid in plants and some microorganisms. EC 4.3.1.1.
An enzyme that catalyzes the deamination of PHENYLALANINE to form trans-cinnamate and ammonia.
A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.
A species of ANABAENA that can form SPORES called akinetes.
Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA. EC 4.3.1.
An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.
3-(p-Fluorophenyl)-alanine.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
A red yeast-like mitosporic fungal genus generally regarded as nonpathogenic. It is cultured from numerous sources in human patients.
A phylum of fungi that produce their sexual spores (basidiospores) on the outside of the basidium. It includes forms commonly known as mushrooms, boletes, puffballs, earthstars, stinkhorns, bird's-nest fungi, jelly fungi, bracket or shelf fungi, and rust and smut fungi.
An enzyme that catalyzes the conversion of carbamoyl phosphate and L-aspartate to yield orthophosphate and N-carbamoyl-L-aspartate. (From Enzyme Nomenclature, 1992) EC 2.1.3.2.
A compound obtained from the bark of the white willow and wintergreen leaves. It has bacteriostatic, fungicidal, and keratolytic actions.
Phenylpropionates are a class of organic compounds, including certain drugs such as ephedrine and pseudoephedrine, which contain a phenylethanoic acid structure with a propionate substitution.
An enzyme that, in the presence of ATP and COENZYME A, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and ORTHOPHOSPHATE. This reaction represents an important step in fatty acid biosynthesis. This enzyme was formerly listed as EC 4.1.3.8.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
Diseases of plants.

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.

The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction L-aspartate ⇌ {\displaystyle \rightleftharpoons ... and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism. As of late ... The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). Other names in common use include ... This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. ...
Threo-3-hydroxy-D-aspartate+ammonia-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: ... threo-3-Hydroxy-D-aspartate ammonia-lyase (EC 4.3.1.27, D-threo-3-hydroxyaspartate dehydratase) is an enzyme with systematic ... name threo-3-hydroxy-D-aspartate ammonia-lyase (oxaloacetate-forming). This enzyme catalyses the following chemical reaction ... threo-3-hydroxy-D-aspartate ⇌ {\displaystyle \rightleftharpoons } oxaloacetate + NH3 This enzyme is a pyridoxal-phosphate ...
... erythro-3-hydroxy-Ls-aspartate hydro-lyase (deaminating); erythro-3-hydroxy-Ls-aspartate ammonia-lyase. It employs one cofactor ... The systematic name of this enzyme class is erythro-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in ... The enzyme erythro-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.20) catalyzes the chemical reaction erythro-3-hydroxy-L-aspartate ... displaystyle \rightleftharpoons } oxaloacetate + NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, ...
The systematic name of this enzyme class is threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in ... and threo-3-hydroxy-L-aspartate ammonia-lyase. Wada M, Matsumoto T, Nakamori S, Sakamoto M, Kataoka M, Liu JQ, Itoh N, Yamada H ... NH3 This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. ... The enzyme threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) is an enzyme that catalyzes the chemical reaction threo-3- ...
Aspartate ammonia-lyase, EC 4.3.1.1 (aspartase), which catalyzes the reversible conversion of aspartate to fumarate and ammonia ... Fumarate lyase belongs to the lyase class of enzymes. These proteins use fumarate as a substrate. They have been shown to share ... This reaction is analogous to that catalyzed by fumarase, except that ammonia rather than water is involved in the trans- ... Delta-crystallin shares around 90% sequence identity with arginosuccinate lyase, showing that it is an example of a 'hijacked' ...
Industrially, aspartate is produced by amination of fumarate catalyzed by L-aspartate ammonia-lyase. Racemic aspartic acid can ... The conversion of aspartate to these other amino acids begins with reduction of aspartate to its "semialdehyde", O2CCH(NH2) ... It carries reducing equivalents in the malate-aspartate shuttle, which utilizes the ready interconversion of aspartate and ... such as magnesium aspartate) The sweetener aspartame, which is made from an aspartic acid and phenylalanine Aspartate ...
ASS argininosuccinate synthetase ASL argininosuccinate lyase ARG1 arginase 1 Before the urea cycle begins ammonia is converted ... The entire process converts two amino groups, one from NH+ 4 and one from aspartate, and a carbon atom from HCO− 3, to the ... The conversion from ammonia to urea happens in five main steps. The first is needed for ammonia to enter the cycle and the ... Organisms that cannot easily and safely remove nitrogen as ammonia convert it to a less toxic substance, such as urea, via the ...
Aspartic acid is produced by the addition of ammonia to fumarate using a lyase. In plants, nitrogen is first assimilated into ... For example, aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate. Other ... Thus for aspartate or glutamate with negative side chains, the terminal amino group is essentially entirely in the charged form ... Aspartate, glycine, and glutamine are precursors of nucleotides. However, not all of the functions of other abundant ...
Deprotonation of the lysine residue causes ammonia to leave, thus completing the catalytic cycle. Cystathionine gamma lyase ... and methionine γ lyase. It is also a member of the broader aspartate aminotransferase family. Like many other PLP-dependent ... The enzyme cystathionine γ-lyase (EC 4.4.1.1, CTH or CSE; also cystathionase; systematic name L-cystathionine cysteine-lyase ( ... Cystathionine γ-lyase is a member of the Cys/Met metabolism PLP-dependent enzymes family. Other members include cystathionine γ ...
"ASL gene argininosuccinate lyase". NIH. U.S. Department of Health & Human Services. 2007. Jack, JJB (1982). "Actions of ammonia ... While ASS catalyzes the formation of argininosuccinate from citrulline and aspartate, ASL breaks the newly formed ... Ammonia is toxic in part because it affects the nervous system. There is biochemical evidence that shows rises in ammonia can ... ASL is a key enzyme in the conversion of ammonia to urea through the urea cycle. Ammonia builds to toxic levels, resulting in ...
... ammonia-lyases MeSH D08.811.520.232.400.200 - aspartate ammonia-lyase MeSH D08.811.520.232.400.350 - ethanolamine ammonia-lyase ... aspartate-ammonia ligase MeSH D08.811.464.259.200.600 - glutamate-ammonia ligase MeSH D08.811.464.259.300 - argininosuccinate ... chondroitin lyases MeSH D08.811.520.241.700.350.500.500 - chondroitin abc lyase MeSH D08.811.520.241.700.512 - heparin lyase ... tyrosine phenol-lyase MeSH D08.811.520.232.300 - amidine-lyases MeSH D08.811.520.232.300.200 - adenylosuccinate lyase MeSH ...
D-serine ammonia-lyase EC 4.3.1.19: threonine ammonia-lyase EC 4.3.1.20: erythro-3-hydroxy-L-aspartate ammonia-lyase EC 4.3. ... diaminopropionate ammonia-lyase EC 4.3.1.16: threo-3-hydroxy-L-aspartate ammonia-lyase EC 4.3.1.17: L-serine ammonia-lyase EC ... aspartate ammonia-lyase EC 4.3.1.2: methylaspartate ammonia-lyase EC 4.3.1.3: histidine ammonia-lyase EC 4.3.1.4: ... phenylalanine/tyrosine ammonia-lyase) EC 4.3.1.6: β-alanyl-CoA ammonia-lyase EC 4.3.1.7: ethanolamine ammonia-lyase EC 4.3.1.8 ...
Aspartate + IMP + GTP → Adenylosuccinate + GDP + Pi Finally, adenylosuccinate is cleaved by the enzyme adenylosuccinate lyase ... As the purine nucleotide cycle produces ammonia (see below in ammonia synthesis), skeletal muscle needs to synthesize glutamate ... Glutamate is then used to produce aspartate. The aspartate enters the purine nucleotide cycle, where it is used to convert IMP ... Aspartate (catalyzed by aspartate aminotransferase) When skeletal muscle is at rest (ADP. ATP), the purine nucleotide cycle ...
... grouped together because one of them can be synthesized from the other using the enzyme phenylalanine/tyrosine ammonia-lyase. ... Alanine and aspartate are synthesized by the transamination of pyruvate and oxaloacetate, respectively. Glutamine is ...
Ammonia is toxic, particularly to the nervous system. An accumulation of ammonia during the first few days of life leads to ... Attack by aspartate is the rate-limiting step of the reaction. This step produces free AMP and L-argininosuccinate. ... Argininosuccinate synthetase and argininosuccinate lyase recycle citrulline, a byproduct of nitric oxide production, into ... As a result, nitrogen (in the form of ammonia) and other byproducts of the urea cycle (such as citrulline) build up in the ...
... and ammonia. Found in plants, bacteria, and yeast, cystathionine beta-lyase is an essential part of the methionine biosynthesis ... and methionine gamma lyase. Additionally, these structures exhibit a type I fold and belong to the aspartate aminotransferase ( ... The enzyme also belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this ... Cystathionine beta-lyase (EC 4.4.1.8), also commonly referred to as CBL or β-cystathionase, is an enzyme that primarily ...
The β enzymes are all lyases and catalyze reactions where Cα and Cβ participate. Overall, in the PLP-dependent enzymes, the PLP ... Fold Type I - aspartate aminotransferase family Fold Type II - tryptophan synthase family Fold Type III - alanine racemase ... PdxS catalyzes the condensation of ribulose 5-phosphate, glyceraldehyde-3-phosphate, and ammonia, this latter molecules is ... The overall B6 enzymes diverged into four independent evolutionary lines: α family (i.e. aspartate aminotransferase), β family ...
... aspartate-ammonia ligase (ADP-forming) EC 6.3.1.5: NAD+ synthase EC 6.3.1.6: glutamate-ethylamine ligase EC 6.3.1.7: 4- ... lyase] ligase EC 6.2.1.23: dicarboxylate-CoA ligase EC 6.2.1.24: phytanate-CoA ligase EC 6.2.1.25: benzoate-CoA ligase EC 6.2. ... aspartate-ammonia ligase EC 6.3.1.2: glutamine synthetase EC 6.3.1.3: Now EC 6.3.4.13, phosphoribosylamine-glycine ligase EC ... aspartate-tRNAAsn ligase EC 6.1.1.24: glutamate-tRNAGln ligase EC 6.1.1.25: The tRNAPyl is now known only to be charged with ...
Next, aspartate carbamoyltransferase catalyzes a condensation reaction between aspartate and carbamoyl phosphate to form ... This step is catalyzed by adenylosuccinate lyase. Inosine monophosphate is converted to guanosine monophosphate by the ... and from ammonia and carbon dioxide. Recently it has been also demonstrated that cellular bicarbonate metabolism can be ... This new carbon is modified by the addition of a third NH2 unit, this time transferred from an aspartate residue. Finally, a ...
Aspartic acid is produced by the addition of ammonia to fumarate using a lyase. Annigan, Jan. "How Many Amino Acids Does the ... Aspartate kinase becomes downregulated by the presence of threonine or lysine. Lysine is synthesized from aspartate via the ... The formation of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into ... The synthesis of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into ...
SAICAR lyase removes the carbon skeleton of the added aspartate, leaving the amino group and forming 5-aminoimidazole-4- ... asparagine synthetase catalyzes the addition of nitrogen from glutamine or soluble ammonia to aspartate to yield asparagine. ... The biosynthesis of aspartate is a one step reaction that is catalyzed by a single enzyme. The enzyme aspartate ... The aspartate family of amino acids includes: threonine, lysine, methionine, isoleucine, and aspartate. Lysine and isoleucine ...
Food portal Medicine portal Alitame Aspartame controversy Neotame Phenylalanine ammonia lyase Stevia Budavari S, ed. (1989). " ... Aspartic acid (aspartate) is one of the most common amino acids in the typical diet. As with methanol and phenylalanine, intake ...
... aspartate kinase EC 2.7.2.5: Now EC 6.3.4.16, carbamoyl-phosphate synthase (ammonia) EC 2.7.2.6: formate kinase EC 2.7.2.7: ... lyase) S-acetyltransferase EC 2.3.1.50: serine C-palmitoyltransferase EC 2.3.1.51: 1-acylglycerol-3-phosphate O-acyltransferase ... ammonia kinase EC 2.7.3.9: phosphoenolpyruvate-protein phosphotransferase EC 2.7.3.10: agmatine kinase EC 2.7.3.11: now EC 2.7. ... aspartate transaminase EC 2.6.1.2: alanine transaminase EC 2.6.1.3: cysteine transaminase EC 2.6.1.4: glycine transaminase EC ...
Phenylalanine ammonia lyase for phenylketonuria, Mol Genet Metab 99: 4-9. "UPDATE: FDA-Approved Oral Zeposia® (Ozanimod) for ... in the chemistry department at Harvard University where he focused on the large allosteric enzyme aspartate ... pegylated Phenylalanine ammonia-lyase) as treatments for mild and classical phenylketonuria (PKU). In 2008, Stevens started ... Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase J Mol Biol 380: ...
EC 4.3.1 Phenylalanine ammonia-lyase (EC 4.3.1.24) Category:EC 4.4.1 Cystathionine gamma-lyase Cystathionine beta-lyase ... EC 2.1.3 Aspartate transcarbamoylase EC 2.1.3.2 Ornithine transcarbamoylase EC 2.1.3.3 Category:EC 2.2.1 Transketolase EC 2.2. ... lyase) ligase EC 6.2.1.23: Dicarboxylate-CoA ligase EC 6.2.1.24: Phytanate-CoA ligase EC 6.2.1.25: Benzoate-CoA ligase EC 6.2. ... EC 2.6.1 Alanine transaminase EC 2.6.1.2 Aspartate transaminase EC 2.6.1.1 Category:EC 2.7.2 Butyrate kinase (EC 2.7.2.7) EC ...
... is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase. Phenylalanine is biosynthesized via the ... "Specific inhibition of N-methyl-D-aspartate receptor function in rat hippocampal neurons by L-phenylalanine at concentrations ... In 1882, Erlenmeyer and Lipp first synthesized phenylalanine from phenylacetaldehyde, hydrogen cyanide, and ammonia. The ...
D-aspartate) oxidase EC 1.4.3.16: L-aspartate oxidase EC 1.4.3.17: Now EC 1.3.3.10, tryptophan α,β-oxidase EC 1.4.3.18: Not ... ammonia-forming) EC 1.7.2.3: trimethylamine-N-oxide reductase EC 1.7.2.4: nitrous-oxide reductase EC 1.7.2.5: nitric oxide ... chlorite O2-lyase EC 1.13.11.50: acetylacetone-cleaving enzyme EC 1.13.11.51: 9-cis-epoxycarotenoid dioxygenase EC 1.13.11.52: ... D-aspartate oxidase EC 1.4.3.2: L-amino-acid oxidase EC 1.4.3.3: D-amino-acid oxidase EC 1.4.3.4: monoamine oxidase EC 1.4.3.5 ...
The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction L-aspartate ⇌ {\displaystyle \rightleftharpoons ... and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism. As of late ... The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). Other names in common use include ... This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. ...
L-aspartate ammonia lyase [48559] (2 species). *. Species Bacillus sp., ym55-1 [TaxId:1409] [89153] (3 PDB entries). ... Argininosuccinate lyase/delta-crystallin [48564] (4 species). *. Species Domestic duck (Anas platyrhynchos), delta-crystallin [ ...
... and reduces ammonia build-up in patients with cirrhosis, a pilot study found. ... particularly aspartate ammonia-lyase, with 17 high-confident peptides also enhanced (FMT vs placebo, P = .031), and likewise ... Beneficial Proteins, Ammonia Metabolism, and Cytokines After FMT, fecal proteomics detected 301 proteins composed of 154 of ... After 1 month, ammonia levels in the plasma were lower but higher in the feces, findings that were further enhanced at 3 months ...
aspartate ammonia-lyase YP_178106 normal 1 n/a Campylobacter jejuni RM1221 Bacteria -. ... aspartate racemase, putative YP_178104 normal 0.28039 n/a Campylobacter jejuni RM1221 Bacteria -. ... adenylosuccinate lyase YP_178050 normal 1 n/a Campylobacter jejuni RM1221 Bacteria -. ...
aspartate ammonia-lyase 124, 261. DVU1767. biotin synthase 95, 261. DVU1768. GTP-binding protein 95, 261. ...
Putative aspartate ammonia-lyase. 96.77%. PM0083678. 104. A0A0D5C7M7. Putative transcriptional regulator. 96.83%. PM0083580. ... Adenylosuccinate lyase. 97.01%. PM0084011. 112. A0A6S6I560. dTDP-4-dehydrorhamnose 3,5-epimerase family protein. 97.16%. ... DNA-(apurinic or apyrimidinic site) lyase MutM. 97%. PM0084000. 111. A0A6M2Y1J5. ...
L-aspartate ammonia-lyase. Sama_0789. Sama_0822. braC. ABC transporter for glutamate, histidine, arginine, and other amino ... pathway II via aspartate ammonia-lyase (link), and pathway VI via glutamate mutase (link). Several other MetaCyc pathways are ... the lyase mal forms 2-methylfumarate (mesaconate), the hydratase fumD forms (S)-2-methylmalate (citramalate), and a lyase forms ... glutamate and oxaloacetate are transaminated to 2-oxoglutarate and aspartate, and the aspartate is cleaved to fumarate and ...
L-aspartate ammonia-lyase. AO356_11090. AO356_07075. braC. ABC transporter for glutamate, histidine, arginine, and other amino ... pathway II via aspartate ammonia-lyase (link), and pathway VI via glutamate mutase (link). Several other MetaCyc pathways are ... the lyase mal forms 2-methylfumarate (mesaconate), the hydratase fumD forms (S)-2-methylmalate (citramalate), and a lyase forms ... glutamate and oxaloacetate are transaminated to 2-oxoglutarate and aspartate, and the aspartate is cleaved to fumarate and ...
Funciton: Aspartate ammonia-lyase (EC 4.3.1.1) Locus tag: VF_2354. Name: dcuA. Funciton: C4-dicarboxylate transporter ... Funciton: Cytochrome c-type biogenesis protein CcmC, putative heme lyase for CcmE ...
Structure-based engineering of aspartate ammonia lyase * Design of new enzymes for carbon-carbon bond formation ...
delta-crystallins MeSH D08.811.520.232.400 - ammonia-lyases MeSH D08.811.520.232.400.200 - aspartate ammonia-lyase MeSH D08.811 ... Argininosuccinate lyase. δ-crystallins are the major structural eye lens water-soluble proteins of most birds, reptiles, and ... Amides are derived from acids by replacement of -OH by -NH2 or from ammonia by the replacement of H by an acyl group. (From ... Argininosuccinate Lyase. An enzyme of the urea cycle which splits argininosuccinate to fumarate plus arginine. Its absence ...
Despite the broad substrate spectrum of methylaspartate lyase (MAL), some bulky substrates, such as caffeic acid, cannot be ... Structural basis for the catalytic mechanism of aspartate ammonia lyase. Biochemistry 50:6053-6062. https://doi.org/10.1021/ ... 2015), ammonia lyase (AL) (Zhang et al. 2020b), lipase (Zeng et al. 2018), and tautomerase (Liu et al. 2020). However, based on ... Turner NJ (2011) Ammonia lyases and aminomutases as biocatalysts for the synthesis of α-amino and β-amino acids. Curr Opin Chem ...
A dual-enzyme cascade route with aspartate-1-decarboxylases (ADC) from Bacillus subtilis and native aspartate ammonia-lyase ( ... aspartate aminotransferase and aspartate ammonia-lyase enhanced DPA concentration to 2.56 ± 0.05 g/L at shake flasks level. Fed ...
4.3.1.1 aspartate ammonia-lyase 4.3.1.23 tyrosine ammonia-lyase 4.3.1.24 phenylalanine ammonia-lyase 4.3.1.25 phenylalanine/ ... tyrosine ammonia-lyase 4.3.1.31 L-tryptophan ammonia lyase 4.3.1.5 phenylalanine ammonia-lyase - - - - - - ...
Aspartate aminotransferase; aspartate kinase; aspartate-ammonia ligase; aspartate ammonia-lyase; aspartate dehydrogenase; ... aspartate-semialdehyde dehydrogenase; L-aspartate oxidase; aspartate 1-decarboxylase; aspartate carbamoyltransferase. Glutamate ... ammonia-lyase, dehydrogenase, decarboxylase etc. that were related to the metabolism of aspartate (average 66,030 genes), ... Tyrosine decarboxylase; protein-tyrosine phosphatase; protein-tyrosine kinase; tyrosine phenol-lyase. Phenylalanine. 930. 824. ...
diaminopropionate ammonia-lyase (TIGR03528; EC 4.3.1.15; HMM-score: 58.8) Metabolism Energy metabolism Other diaminopropionate ... Metabolism Amino acid biosynthesis Aspartate family threonine synthase (TIGR00260; EC 4.2.3.1; HMM-score: 59.1) ... Metabolism Amino acid biosynthesis Pyruvate family threonine ammonia-lyase (TIGR01127; EC 4.3.1.19; HMM-score: 306.6) ... Metabolism Amino acid biosynthesis Pyruvate family threonine ammonia-lyase, biosynthetic (TIGR01124; EC 4.3.1.19; HMM-score: ...
Because the urea cycle cannot continue without ornithine inside the mitochondria, ammonia disposal slows, and blood ammonia ... It is then cleaved to produce fumarate and arginine by a lyase enzyme. Urea and ornithine are produced by arginase. Under ... Argininosuccinic acid is produced from the condensation of citrulline and aspartate by a synthetase enzyme. ... Ammonia Control in Children Ages 2 Months through 5 Years with Urea Cycle Disorders: Comparison of Sodium Phenylbutyrate and ...
Deaminases remove ammonia, for example, in the removal of amino groups from amino acids: ... 4. Formation or removal of a double bond with group transfer. The functional groups transferred by these lyase enzymes include ... For example, alanine aminotransferase shuffles the alpha‐amino group between alanine and aspartate: ... amino groups, water, and ammonia. For example, decarboxylases remove CO 2 from alpha‐ or beta‐keto acids: Dehydratases remove ...
Ammonia. Recycling. Purine. Metabolism. Glucose-Alanine. Cycle. Aspartate. Metabolism. Citric Acid. Cycle. Arginine and. ... lyase. Argininosuccinate. synthase. L-Glutamine. L-Alanine. Oxoglutaric acid. L-Glutamic acid. Oxalacetic acid. NH. 3. L- ... Ammonia. L-Aspartic acid. Fumaric acid. L-Arginine. Ornithine. L-Glutamine. L-Alanine. Ornithine. Citrulline. Citrulline. L- ... Ammonia. Recycling. Purine. Metabolism. Glucose-Alanine. Cycle. Aspartate. Metabolism. Citric Acid. Cycle. Arginine and. ...
... ammonia and cysteine by cystathionine gamma-lyase. All the reactions resulting in 2-KB formation happen outside mitochondria, 2 ... aspartate aminotransferase; KGDHC: ketoglutarate dehydrogenase complicated; MCM: methylmalonyl mutase; MCEE: methylmalonyl ...
Ammonia. Recycling. Purine. Metabolism. Glucose-Alanine. Cycle. Aspartate. Metabolism. Citric Acid. Cycle. Arginine and. ... lyase. Argininosuccinate. synthase. L-Glutamine. L-Alanine. Oxoglutaric acid. L-Glutamic acid. Oxalacetic acid. NH. 3. L- ... Ammonia. L-Aspartic acid. Fumaric acid. Accumulation. L-Arginine. Ornithine. L-Glutamine. L-Alanine. Ornithine. Citrulline. ... Ammonia. Recycling. Purine. Metabolism. Glucose-Alanine. Cycle. Aspartate. Metabolism. Citric Acid. Cycle. Arginine and. ...
44-6) mediates the removal of ammonia as urea in the amount of 10 to 20 g per day in the healthy adult. The absence of a fully ... High ammonia concentrations impair the malate-aspartate shuttle, which mediates the transport of NADH from the cytosol to ... Argininosuccinate is cleaved in the cytosol by argininosuccinate lyase (AL), which is coded on human chromosome 7 (Fig. 44-6, ... Excretion of ammonia as phenylacetylglutamine is more efficient than excretion as hippurate because 2 mol of ammonia are ...
Because the urea cycle cannot continue without ornithine inside the mitochondria, ammonia disposal slows, and blood ammonia ... It is then cleaved to produce fumarate and arginine by a lyase enzyme. Urea and ornithine are produced by arginase. Under ... Argininosuccinic acid is produced from the condensation of citrulline and aspartate by a synthetase enzyme. ... Ammonia Control in Children Ages 2 Months through 5 Years with Urea Cycle Disorders: Comparison of Sodium Phenylbutyrate and ...
... activated for substitution by ammonia (released from glutamine) or by the amino group of aspartate. ... adenylosuccinate lyase after the reaction depicted here. ... In the first step, an aspartate is acquired to form ... One of the amide bonds in the uracil ring is opened through hydrolysis, and ammonia and CO2 are cleaved off to produce β- ... In the second reaction, aspartate transcarbamylase transfers the carbamoyl group of carbamoylphosphate to the α-amino group of ...
release free ammonia from AAs. Definition. lyases. Term. remove ammonia from purines and pyrimidines. ... Aspartate displaces AMP on citrullyl-AMP intermediate to form what molec. Definition. argininosuccinate. ... ammonia released in cytosol or mitoch. Definition. mitoch- this is how it looks in figure, not sure if it is only placed ... converts ammonia and bicarb to carbomoyl phosphate (where does this occur. What are the two things it reqs. ...
L-aspartate and carrying about 100 copies of the CAD (carbamoyl-phosphate synthetase/aspartate carbamoyltransferase/ ... and the percentage of the internally derived ammonia that is channeled through the ammonia tunnel [38]. ... Arginosuccinate Synthetase and Arginosuccinate Lyase were functionally expressed at levels comparable to cultured primary human ... Function of serine-52 and serine-80 in the catalytic mechanism of Escherichia coli aspartate transcarbamoylase. Xu, W., ...
Asparaginase is also widely distributed within the body, where it converts asparagine into ammonia and aspartate. Aspartate ... Genetic defects are known for both the synthase and the lyase. Missing or impaired cystathionine synthase leads to ... Aspartate is formed in a transamintion reaction catalyzed by aspartate transaminase, AST. This reaction uses the aspartate α- ... The former catalyzed by glutamate dehydrogenase and the latter by aspartate aminotransferase, AST. Aspartate is also derived ...
Improved production of p-hydroxycinnamic acid from tyrosine using a novel thermostable phenylalanine/tyrosine ammonia lyase ... OAA is an indispensable metabolite for the TCA cycle regeneration and it is precursor of aspartate (Figure 1). It appears that ... tryptophan indole-lyase) converts tryptophan into indole, PYR and ammonia (Figure 1). TnaA specific activity was measured at 1 ... In agreement, the isocitrate lyase specific activity (Icl or AceA, one of the glyoxylate shunt enzyme) was detected in JM101 ...
  • 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)
  • 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)
  • 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)
  • 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)
  • Argininosuccinate is cleaved in the cytosol by argininosuccinate lyase ( AL ), which is coded on human chromosome 7 ( Fig. 44-6 , reaction 4). (nih.gov)
  • 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)
  • 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)
  • 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)
  • 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)
  • Inhibition of the electron transport chain (ETC) prevents the regeneration of mitochondrial NAD+, resulting in cessation of the oxidative tricarboxylic acid (TCA) cycle and a consequent dependence upon reductive carboxylation for aspartate synthesis. (biomed.news)
  • Carbamoyl phosphate is produced from ammonia and bicarbonate by carbamoylphosphate synthetase I. This reaction is stimulated by ornithine. (medscape.com)
  • Ammonia the highly toxic product of protein catabolism, is rapidly inactivated by a variety of reactions. (medmuv.com)
  • Reduced nitrogen enters the human body as dietary free amino acids, protein, and the ammonia produced by intestinal tract bacteria. (medmuv.com)
  • Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. (wikipedia.org)
  • Aspartate decarboxylase [Interproscan]. (ntu.edu.sg)
  • Here, we show that inhibition of the ETC drives reversal of the mitochondrial aspartate transaminase (GOT2) as well as malate and succinate dehydrogenases (MDH2 and SDH) to transfer oxidative NAD+ equivalents into the mitochondrion. (biomed.news)
  • The functional groups transferred by these lyase enzymes include amino groups, water, and ammonia. (cliffsnotes.com)
  • Despite the broad substrate spectrum of methylaspartate lyase (MAL), some bulky substrates, such as caffeic acid, cannot be effectively accepted. (springeropen.com)
  • 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)
  • 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)
  • An enzyme that catalyzes the conversion of aspartic acid to ammonia and fumaric acid in plants and some microorganisms. (nih.gov)
  • In the liver, alanine transaminase transfers the ammonia to α-KG and regenerates pyruvate. (tdmuv.com)
  • Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. (wikipedia.org)
  • 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)
  • Argininosuccinic acid is produced from the condensation of citrulline and aspartate by a synthetase enzyme. (medscape.com)
  • Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma-lyase catalyzes the lower reaction. (iiab.me)
  • We show that a VHL loss-dependent reprogramming of branched-chain amino acid catabolism sustains the de novo biosynthesis of aspartate and arginine enabling tumor cells with the flexibility of partitioning the nitrogen of the amino acids depending on their needs. (biomed.news)
  • Reduced nitrogen enters the human body as dietary free amino acids, protein, and the ammonia produced by intestinal tract bacteria. (tdmuv.com)
  • 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)
  • 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)
  • Carbamoyl phosphate is produced from ammonia and bicarbonate by carbamoylphosphate synthetase I. This reaction is stimulated by ornithine. (medscape.com)
  • 16211) para-aminobenzoate synthetase/4-amino-4-deoxychorismate lyase pabBC BBZA01000002 CDS ARMA_0015 192. (go.jp)
  • This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. (wikipedia.org)
  • 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)
  • There is an alternative pathway for the excretion of ammonia in the body called the glutamine pathway . (nutrifix-health.com)
  • 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)
  • Conclusion Blood ammonia, cholinesterase, and their combined measurement have a potential clinical value in the early diagnosis of liver cirrhosis with MHE. (bvsalud.org)