Aspartate ammonia lyase. Medical search

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.

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.

An enzyme that catalyzes the first step of histidine catabolism, forming UROCANIC ACID and AMMONIA from HISTIDINE. Deficiency of this enzyme is associated with elevated levels of serum histidine and is called histidinemia (AMINO ACID METABOLISM, INBORN ERRORS).

Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).

The type species of the genus NITROSOMONAS, a gram-negative chemolithotroph that oxidizes ammonia to nitrite. It is found in soil, sewage, freshwater, and on building walls, and especially in polluted areas where air contains high levels of nitrogen compounds.

A genus of gram-negative, rod-shaped bacteria that oxidizes nitrites to nitrates. Its organisms occur in aerobic environments where organic matter is being mineralized, including soil, fresh water, and sea water.

A genus of gram-negative, ellipsoidal or rod-shaped bacteria whose major source of energy and reducing power is from the oxidation of ammonia to nitrite. Its species occur in soils, oceans, lakes, rivers, and sewage disposal systems.

A plant genus of the family LAMIACEAE. The common names of beebalm or lemonbalm are also used for MONARDA.

Systems that provide all or most of the items necessary for maintaining life and health. Provisions are made for the supplying of oxygen, food, water, temperature and pressure control, disposition of carbon dioxide and body waste. The milieu may be a spacecraft, a submarine, or the surface of the moon. In medical care, usually under hospital conditions, LIFE SUPPORT CARE is available. (From Webster's New Collegiate Dictionary)

Systems that provide for the maintenance of life in an isolated living chamber through reutilization of the material available, in particular, by means of a cycle wherein exhaled carbon dioxide, urine, and other waste matter are converted chemically or by photosynthesis into oxygen, water, and food. (NASA Thesaurus, 1988)

Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.

A glycoprotein that is central in both the classical and the alternative pathway of COMPLEMENT ACTIVATION. C3 can be cleaved into COMPLEMENT C3A and COMPLEMENT C3B, spontaneously at low level or by C3 CONVERTASE at high level. The smaller fragment C3a is an ANAPHYLATOXIN and mediator of local inflammatory process. The larger fragment C3b binds with C3 convertase to form C5 convertase.

Organized activities related to the storage, location, search, and retrieval of information.

Materials that have a limited and usually variable electrical conductivity. They are particularly useful for the production of solid-state electronic devices.

An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.

A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.

A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.

A genus of protozoa, formerly also considered a fungus. Its natural habitat is decaying forest leaves, where it feeds on bacteria. D. discoideum is the best-known species and is widely used in biomedical research.

A group of naturally occurring amines derived by enzymatic decarboxylation of the natural amino acids. Many have powerful physiological effects (e.g., histamine, serotonin, epinephrine, tyramine). Those derived from aromatic amino acids, and also their synthetic analogs (e.g., amphetamine), are of use in pharmacology.

One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

Substances that reduce the growth or reproduction of BACTERIA.

The ability of bacteria to resist or to become tolerant to chemotherapeutic agents, antimicrobial agents, or antibiotics. This resistance may be acquired through gene mutation or foreign DNA in transmissible plasmids (R FACTORS).

A serotype of Salmonella enterica that is a frequent agent of Salmonella gastroenteritis in humans. It also causes PARATYPHOID FEVER.

A subgenus of Salmonella containing several medically important serotypes. The habitat for the majority of strains is warm-blooded animals.

Infections in animals with bacteria of the genus SALMONELLA.

Infections with bacteria of the genus SALMONELLA.

The degree of pathogenicity within a group or species of microorganisms or viruses as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host. The pathogenic capacity of an organism is determined by its VIRULENCE FACTORS.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.

The terms, expressions, designations, or symbols used in a particular science, discipline, or specialized subject area.

A species of bacteria that resemble small tightly coiled spirals. Its organisms are known to cause abortion in sheep and fever and enteritis in man and may be associated with enteric diseases of calves, lambs, and other animals.

A genus of bacteria found in the reproductive organs, intestinal tract, and oral cavity of animals and man. Some species are pathogenic.

Infections with bacteria of the genus CAMPYLOBACTER.

A species of bacteria present in man and many kinds of animals and birds, often causing infertility and/or abortion.

A species of gram-negative, rod-shaped bacteria isolated from the intestinal tract of swine, poultry, and man. It may be pathogenic.

High molecular weight mucoproteins that protect the surface of EPITHELIAL CELLS by providing a barrier to particulate matter and microorganisms. Membrane-anchored mucins may have additional roles concerned with protein interactions at the cell surface.

Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.

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, EC 4.3.1.1 (aspartase), which catalyzes the reversible conversion of aspartate to fumarate and ammonia ... Fumarate lyase is a substrate of the lyase class of enzymes. It been shown to share a short conserved sequence around a ... 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' ...

https://en.wikipedia.org/wiki/Fumarate_lyase

In enzymology, an aspartate ammonia-lyase (EC 4.3.1.1) is an enzyme that catalyzes the chemical reaction L-aspartate ⇌ {\ ... 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. ...

https://en.wikipedia.org/wiki/Aspartate_ammonia-lyase

The systematic name of this enzyme class is threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in ... This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. ... and threo-3-hydroxy-L-aspartate ammonia-lyase. Wada M, Matsumoto T, Nakamori S, Sakamoto M, Kataoka M, Liu JQ, Itoh N, Yamada H ... In enzymology, a threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) is an enzyme that catalyzes the chemical reaction threo-3 ...

https://en.wikipedia.org/wiki/Threo-3-hydroxyaspartate_ammonia-lyase

... erythro-3-hydroxy-Ls-aspartate hydro-lyase (deaminating), and erythro-3-hydroxy-Ls-aspartate ammonia-lyase. It employs one ... The systematic name of this enzyme class is erythro-3-hydroxy-Ls-aspartate ammonia-lyase (oxaloacetate-forming). Other names in ... This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. ... In enzymology, an erythro-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.20) is an enzyme that catalyzes the chemical reaction ...

https://en.wikipedia.org/wiki/Erythro-3-hydroxyaspartate_ammonia-lyase

... (EC 4.3.1.27, D-threo-3-hydroxyaspartate dehydratase) is an enzyme with systematic ... Threo-3-hydroxy-D-aspartate+ammonia-lyase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal ... 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 ...

https://en.wikipedia.org/wiki/Threo-3-hydroxy-D-aspartate_ammonia-lyase

... aspartate is produced by amination of fumarate catalyzed by L-aspartate ammonia-lyase. Racemic aspartic acid can be synthesized ... aspartate and ammonia donate amino groups leading to the formation of urea.[citation needed] Aspartate has many other ... D-Aspartate is one of two D-amino acids commonly found in mammals.[3] In proteins aspartate sidechains are often hydrogen ... The conversion of aspartate to these other amino acids begins with reduction of aspartate to its "semialdehyde", O2CCH(NH2) ...

https://en.wikipedia.org/wiki/Aspartic_acid

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, pI = 1/2(pKa1 + pKa(R)), where pKa(R) is the side chain pKa. ... Aspartate, glycine, and glutamine are precursors of nucleotides. However, not all of the functions of other abundant ...

https://en.wikipedia.org/wiki/Amino_acid

Deprotonation of the lysine residue causes ammonia to leave, thus completing the catalytic cycle. Cystathionine gamma lyase ... and methionine gamma lyase. It is also a member of the broader aspartate aminotransferase family. Like many other PLP-dependent ... and ammonia. Pyridoxal phosphate is a prosthetic group of this enzyme. Cystathionine gamma-lyase also catalyses the following ... Cystathionine gamma-lyase (CTH or CSE; also cystathionase) is an enzyme which breaks down cystathionine into cysteine, α- ...

https://en.wikipedia.org/wiki/Cystathionine_gamma-lyase

"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 ...

https://en.wikipedia.org/wiki/Argininosuccinate_lyase

... isochorismate lyase EC 4.3.1.1: aspartate ammonia-lyase EC 4.3.1.2: methylaspartate ammonia-lyase EC 4.3.1.3: histidine ammonia ... threo-3-hydroxyaspartate ammonia-lyase EC 4.3.1.17: L-serine ammonia-lyase EC 4.3.1.18: D-serine ammonia-lyase EC 4.3.1.19: ... phenylalanine/tyrosine ammonia-lyase) EC 4.3.1.6: b-alanyl-CoA ammonia-lyase EC 4.3.1.7: ethanolamine ammonia-lyase EC 4.3.1.8 ... tyrosine ammonia-lyase EC 4.3.1.24: phenylalanine ammonia-lyase EC 4.3.1.25: phenylalanine/tyrosine ammonia-lyase EC 4.3.1.26: ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)

... 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 ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)

... aspartate-ammonia ligase EC 6.3.1.2: glutamate-ammonia ligase EC 6.3.1.3: Now EC 6.3.4.13 EC 6.3.1.4: aspartate-ammonia ligase ... 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-tRNA ligase EC 6.1.1.13: D-alanine-poly(phosphoribitol) ligase EC 6.1.1.14: glycine-tRNA ligase EC 6.1.1.15: proline- ... D-aspartate ligase EC 6.3.1.13: L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase EC 6.3.1.14: ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)

Oxaloacetic acid + Glutamate ↔ α-Ketoglutarate + Aspartate ( Catalysed by Aspartate Aminotransferase) 2) Synthesis of ammonia ( ... Aspartate + IMP + GTP → Adenylosuccinate + GDP + Pi Finally, Adenylosuccinate is cleaved by the enzyme adenylosuccinate lyase ... The purine nucleotide cycle is a metabolic pathway in which ammonia and fumarate are generated from aspartate and inosine ... OAA either enters into TCA cycle or converts into aspartate in the mitochondria. Aspartate can re-enter purine nucleotide cycle ...

https://en.wikipedia.org/wiki/Purine_nucleotide_cycle

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 ...

https://en.wikipedia.org/wiki/Argininosuccinate_synthase

... 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 ...

https://en.wikipedia.org/wiki/Cystathionine_beta-lyase

... or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is ... The overall B6 enzymes diverged into four independent evolutionary lines: α family (i.e. aspartate aminotransferase), β family ... Serine Dehydratase is also known as: L-serine ammonia-lyase Serine deaminase L-hydroxyaminoacid dehydratase L-serine deaminase ... The β enzymes are all lyases and catalyze reactions where Cα and Cβ participate. Overall, in the PLP-dependent enzymes, the PLP ...

https://en.wikipedia.org/wiki/Serine_dehydratase

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. The liver is the major organ of de novo synthesis of all four nucleotides. De novo ... This new carbon is modified by the addition of a third NH2 unit, this time transferred from an aspartate residue. Finally, a ...

https://en.wikipedia.org/wiki/Nucleotide

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 ...

https://en.wikipedia.org/wiki/Amino_acid_synthesis

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 ...

https://en.wikipedia.org/wiki/Biosynthesis

Food portal Medicine portal Aspartame controversy Phenylalanine ammonia lyase Stevia Budavari S, ed. (1989). "861. Aspartame". ... Aspartic acid (aspartate) is one of the most common amino acids in the typical diet. As with methanol and phenylalanine, intake ...

https://en.wikipedia.org/wiki/Aspartame

... pegylated Phenylalanine ammonia-lyase) as treatments for mild and classical phenylketonuria (PKU). In 2008, Stevens started ... in the chemistry department at Harvard University where he focused on the large allosteric enzyme aspartate ... Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase J Mol Biol 380: ... Phenylalanine ammonia lyase for phenylketonuria, Mol Genet Metab 99: 4-9. https://www.nationalmssociety.org/About-the-Society/ ...

https://en.wikipedia.org/wiki/Raymond_C._Stevens

... is converted to cinnamic acid by the enzyme phenylalanine ammonia-lyase. The genetic disorder phenylketonuria ( ... "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 ...

https://en.wikipedia.org/wiki/Phenylalanine

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 ...

https://en.wikipedia.org/wiki/List_of_enzymes

Phenylalanine ammonia lyase. *Stevia. References[edit]. *^ Budavari S, ed. (1989). "861. Aspartame". The Merck Index (11th ed ... Aspartate[edit]. Aspartic acid (aspartate) is one of the most common amino acids in the typical diet. As with methanol and ... Beta-aspartame differs from aspartame based upon which carboxyl group of aspartate binds to the nitrogen of phenylalanine. ... although a small increase in aspartate time-effect scores was noted over the four-hour postabsorptive period, no significant ...

https://en.wikipedia.org/wiki/E951

Carboxy phosphate reacts with ammonia to give carbamic acid. In turn, carbamic acid reacts with a second ATP to give carbamoyl ... The small subunit contains the glutamine binding site and catalyses the hydrolysis of glutamine to glutamate and ammonia, which ... The carboxylphosphate then reacts with ammonia to form carbamic acid, releasing inorganic phosphate. ... or ammonia (EC 6.3.4.16) and bicarbonate.[1] This enzyme catalyzes the reaction of ATP and bicarbonate to produce carboxy ...

https://en.wikipedia.org/wiki/Carbamoyl_phosphate_synthetase

The enzyme is not a serine protease, as thought previously, but an aspartate protease EC 3.4.21.88: Repressor LexA EC 3.4.21.89 ... The activity is most probably attributable to EC 4.4.1.21, S-ribosylhomocysteine lyase EC 3.13.1.3: 2'-hydroxybiphenyl-2- ... glutamate-ammonia ligase) hydrolase EC 3.1.4.16: 2',3'-cyclic-nucleotide 2'-phosphodiesterase EC 3.1.4.17: 3',5'-cyclic- ... N-acyl-D-aspartate deacylase EC 3.5.1.84: biuret amidohydrolase EC 3.5.1.85: (S)-N-acetyl-1-phenylethylamine hydrolase EC 3.5. ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)

... aspartate kinase EC 2.7.2.5: now EC 6.3.4.16 EC 2.7.2.6: formate kinase EC 2.7.2.7: butyrate kinase EC 2.7.2.8: acetylglutamate ... 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. ... lyase) S-acetyltransferase EC 2.3.1.50: serine C-palmitoyltransferase EC 2.3.1.51: 1-acylglycerol-3-phosphate O-acyltransferase ... aspartate transaminase EC 2.6.1.2: alanine transaminase EC 2.6.1.3: cysteine transaminase EC 2.6.1.4: glycine transaminase EC ...

https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)

... which reacts with ammonia, forming glutamine and inorganic phosphate. ADP and Pi do not dissociate until ammonia binds and ... EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list). *EC7 Translocases (list) ... Aspartic acid (aspartate). *DIDS. *Direct blue 71. *Erythro-4-methyl-L-glutamic acid ... glutamate-ammonia ligase. Active site between two monomers of glutamine synthetase from Salmonella typhimurium. Cation binding ...

https://en.wikipedia.org/wiki/Glutamine_synthetase

... belongs to the class V group of aspartate aminotransferase superfamily of structurally homologous pyridoxal 5'- ... Histidine ammonia-lyase. *Urocanate hydratase. *Formiminotransferase cyclodeaminase. proline→. *Proline oxidase. *Pyrroline-5- ...

https://en.wikipedia.org/wiki/Kynureninase

The ammonia generated by the glycine cleavage system, is assimilated by the Glutamine synthetase-Glutamine oxoglutarate ... HMG-CoA lyase. *HMG-CoA reductase. *Isovaleryl coenzyme A dehydrogenase. *α-Ketoisocaproate dioxygenase ... The H-protein forms a complex with the T-protein that uses tetrahydrofolate and yields ammonia and 5,10- ...

https://en.wikipedia.org/wiki/Glycine_cleavage_system

The gene that encodes for Histidine ammonia-lyase (HAL) spans a roughly 25 kb and consists of 21 exons[4] located at the 12q22- ... the result of an inborn error of metabolism that may result in either an inactive or a severely reduced Histidine ammonia-lyase ... aspartate). *Argininemia. *Argininosuccinic aciduria. *Carbamoyl phosphate synthetase I deficiency. *Citrullinemia. *N- ...

https://en.wikipedia.org/wiki/Histidinemia

Histidine ammonia-lyase. *Urocanate hydratase. *Formiminotransferase cyclodeaminase. proline→. *Proline oxidase. *Pyrroline-5- ... Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ...

https://en.wikipedia.org/wiki/Creatine_kinase

Category:EC 4.3 (carbon-nitrogen lyases)Edit. *Category:EC 4.3.1 *Phenylalanine ammonia-lyase (EC 4.3.1.24) ... Aspartate transaminase EC 2.6.1.1. Category:EC 2.7 (transfer phosphorus-containing groups)Edit. *Category:EC 2.7.2 *Butyrate ... Category:Lyases (EC 4) (Lyase)Edit. Category:EC 4.1 (carbon-carbon lyases)Edit. *Category:EC 4.1.1 *Ornithine decarboxylase (EC ... 4 Category:Lyases (EC 4) (Lyase) *4.1 Category:EC 4.1 (carbon-carbon lyases) ...

https://en.m.wikipedia.org/wiki/List_of_enzymes

The cystathionine is then converted to hypotaurine by the sequential action of three enzymes: cystathionine gamma-lyase, ... In the laboratory taurine can be produced by alkylation of ammonia with bromoethanesulfonate salts.[9] ...

https://en.wikipedia.org/wiki/Taurine

Histidine ammonia-lyase. *Urocanate hydratase. *Formiminotransferase cyclodeaminase. proline→. *Proline oxidase. *Pyrroline-5- ...

https://en.wikipedia.org/wiki/L-dopa

Histidine ammonia-lyase. *Urocanate hydratase. *Formiminotransferase cyclodeaminase. proline→. *Proline oxidase. *Pyrroline-5- ...

https://en.wikipedia.org/wiki/Tyrosinase

Biomarin is currently conducting clinical trials to investigate PEG-PAL (PEGylated recombinant phenylalanine ammonia lyase or ' ... aspartate). *Argininemia. *Argininosuccinic aciduria. *Carbamoyl phosphate synthetase I deficiency. *Citrullinemia. *N- ...

https://en.wikipedia.org/wiki/Phenylketonuria

A number of enzymes, belonging to the lyase class, for which fumarate is a substrate have been shown [PMID: 3282546] to share a ... Aspartate ammonia-lyase catalyses the conversion of aspartate to fumarate.. Woods SA, Schwartzbach SD, Guest JR. Two ... GO:0006531 aspartate metabolic process Molecular Function. GO:0008797 aspartate ammonia-lyase activity ...

http://www.ebi.ac.uk/interpro/entry/IPR004708

https://en.wikipedia.org/wiki/Aspartate_ammonia-lyase

Threo-3-hydroxy-D-aspartate ammonia-lyase (EC 4.3.1.27, D-threo-3-hydroxyaspartate dehydratase) is an enzyme with systematic ... Threo-3-hydroxy-D-aspartate+ammonia-lyase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal ... 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 ...

https://en.wikipedia.org/wiki/Threo-3-hydroxy-D-aspartate_ammonia-lyase

Recombinant Protein and Aspartate ammonia-lyase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are ... Aspartate ammonia-lyase. Aspartate ammonia-lyase ELISA Kit. Aspartate ammonia-lyase Recombinant. Aspartate ammonia-lyase ... CATALYTIC ACTIVITY: L-aspartate = fumarate + NH(3).. Below are the list of possible Aspartate ammonia-lyase products. If you ... Also known as Aspartate ammonia-lyase (Aspartase).. aspA ELISA Kit. aspA Recombinant. aspA Antibody. Cgl1503 ELISA Kit. Cgl1503 ...

https://www.mybiosource.com/protein_family.php?root=aspartate-ammonia-lyase

SYN: aspartate ammonia-lyase. aspartate (as-par′tat). A salt or ester of aspartic acid. a. aminotransferase (AST) an enzyme ... aspartate 1-decarboxylase. SYN: glutamate decarboxylase. aspartate 4-decarboxylase. Aspartate β-decarboxylase;a carboxy-lyase ... a. ammonia-lyase a nonmammalian enzyme catalyzing the conversion of l-aspartic acid to fumaric acid, splitting out ammonia. SYN ... a. ligase an acid:ammonia ligase (amide synthetase) forming l-a. and l-glutamate from l-aspartate and l-glutamine, with the ...

https://theodora.com/medical_dictionary/ascaridata_aspartyl.html

Aspartase (L-aspartate ammonia-lyase; EC 4.3.1.1) catalyzes the reversible amination of fumaric acid to produce L-aspartic acid ... The ammonia-oxidizing bacteria (Nitrosomonas europaea) realize the oxidation of ammonia to nitrite, and the nitrite-oxidizing ... The optimum temperature was determined to be 35 °C. The enzyme showed apparent K m and V max values for L-aspartate as 2.01 mM ...

https://chemweb.com/articles/SV12010/0016700005

Catalytic mechanisms and biocatalytic applications of aspartate and methylaspartate ammonia lyases.. de Villiers M, Puthan ... Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids. ... Structural Basis for the Catalytic Mechanism of Ethylenediamine- N, N-disuccinic Acid Lyase, a Carbon-Nitrogen Bond-Forming ... resolution and stereoselective synthesis of 3-substituted aspartic acids by using engineered methylaspartate ammonia lyases. ...

https://www.ncbi.nlm.nih.gov/pubmed?cmd=search&term=de+Villiers+J%5Bau%5D&dispmax=50

aspartate ammonia-lyase Pseudomonas aeruginosa UCBPP-PA14 PA14_71650 aspartate ammonia-lyase 474 100.0 ...

http://pseudomonas.com/rbbh/pairs?query_strain_id=107&queryStrain=Pseudomonas+aeruginosa+PAO1+%28Reference%29&hit_strain_id=109&hitStrain=Pseudomonas+aeruginosa+UCBPP-PA14&max=100&sort=gene.locusTag&order=asc&offset=5300

Lactoylglutathione lyase. −3.046. APL_1925. tpiA Triosephosphate isomerase. −3.023. APL_1091. aspA Aspartate ammonia-lyase. − ...

https://iai.asm.org/content/77/4/1426/figures-only

Aspartate ammonia-lyase, EC:4.3.1.1 (aspartase), which catalyses the reversible conversion of aspartate to fumarate and ammonia ... Fumarate lyase, conserved site (IPR020557). Short name: Fumarate_lyase_CS Description. A number of enzymes, belonging to the ... This reaction is analogous to that catalyzed by fumarase, except that ammonia rather than water is involved in the trans- ... P25739: Adenylosuccinase, EC:4.3.2.2 (adenylosuccinate lyase) [PMID: 1574589], which catalyses the eighth step in the de novo ...

https://www.ebi.ac.uk/interpro/entry/IPR020557

Aspartate ammonia-lyase. aspA 2,100,543-2,100,845. +. Urease subunit gamma. ureA 2,100,861-2,101,229 ... Ammonia measurement assay. Ammonia concentration during incubation of YS11 in YL medium was measured using ammonia assay kit ( ... The increase of ammonia concentration in accordance with pH increase suggested that ammonia production might be a major way for ... Ammonia measurement in YL medium showed an increase in ammonia production, suggesting that strain YS11 could utilize amino ...

https://link.springer.com/article/10.1186%2Fs13568-019-0773-x

... l-aspartate may also be produced directly from ammonia, as several genes with some similarities to an aspartate-ammonia lyase ... Also, NCFM appears to be capable of assimilating ammonia by conversion into l-glutamate via l-glutamine as intermediates (glnA ... The proposed model for nitrogen assimilation is supported by the presence of amtB (La473), an ammonia permease. Assimilation of ... and aspartate) de novo. From these three amino acids, a series of seven other derivatives could be generated. No de novo or ...

https://www.pnas.org/content/102/11/3906?ijkey=2439fdd673a4bca9e882fa9afc6353cbb36ba195&keytype2=tf_ipsecsha

Aspartate ammonia lyases (standard format). Order Enquiry AMTESK-100. Aminotransferase (standard format). ...

https://www.almacgroup.com/api-chemical-development/enzyme_kits/amine-manipulation/?cc=US

The two enzymes are aspartate ammonia-lyase and ketol-acid reductoisomerase (also known as acetohydroxy acid isomeroreductase ... The structure of aspartate ammonia-lyase is well underway and we are now interpreting electron density maps. For ketol-acid ...

https://www.searlescholars.net/people/gregory-k-farber

... both His141 and Glu275 are in adenylosuccinate lyase numbering), acts as the general base in most fumarase class II superfamily ... Catalytic mechanisms and biocatalytic applications of aspartate and methylaspartate ammonia lyases.. *Marianne de Villiers, ...

https://www.semanticscholar.org/paper/Crystal-structure-of-3-carboxy-cis%2Ccis-muconate-a-Yang-Wang/9997f868c68260cac77e25b97f37f252de1c4852

Biocatalytic enantioselective synthesis of N-substituted aspartic acids by aspartate ammonia lyase. Chemistry-A European ...

https://www.rug.nl/research/zernike/publications/publications_kanweg/2008/synorjournals

aby:ABAYE1921 aspartate ammonia-lyase (aspartase) K01744 471 100 ( -) 29 0.346 78 -, 1 abz:ABZJ_01929 Aspartate ammonia-lyase( ... abk:LX00_08765 aspartate ammonia-lyase K01744 471 100 ( -) 29 0.346 78 -, 1 abn:AB57_1955 aspartate ammonia-lyase K01744 472 ... abw:BL01_08080 aspartate ammonia-lyase K01744 471 100 ( -) 29 0.346 78 -, 1 abx:ABK1_2221 Aspartate ammonia-lyase K01744 472 ... abc:ACICU_01762 Aspartate ammonia-lyase K01744 471 100 ( -) 29 0.346 78 -, 1 abd:ABTW07_1975 aspartate ammonia-lyase K01744 472 ...

http://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=kaf:KAFR_0I02020

... of fumarate respiration was further supported by the reduced intracellular survival rate of an aspartate ammonia-lyase aspA ... The latter is generated from aspartate by the activity of an aspartate alpha-decarboxylase PanD (Cj0296c) and serves as ... jejuni as it directly fuels the TCA cycle by the aspartate ammonia lyse AspA (Cj0087) catalyzing the deamination to fumarate ( ... that interact with aspartate. The uptake of aspartate is convoluted and involves various transporters: While the periplasmic ...

https://www.frontiersin.org/articles/10.3389/fcimb.2014.00137/full

... a missense point mutation affecting amino acid 363 in the aspartate ammonia lyase (aspA) of Y. pestis likely accounting for the ... Noteworthy among this group are genes of purine and aspartate metabolism as well as genes of the methionine salvage pathway (32 ... aspartate aminotransferase, enolase-phosphatase E1, and 5-methylthioribose kinase, respectively. These differences in metabolic ...

https://www.pnas.org/content/101/38/13826.long

... analysis using a real-time PCR assay targeting the aspartate ammonia lyase gene of L. intracellularis. Purified DNA samples ... KEYWORDS: aspartate aminotransferase, AST, creatine kinase, CK, exertional myopathy, grizzly bear, leghold snare, Ursus arctos ... Nevertheless, comparison of serum aspartate aminotransferase and creatine kinase concentrations and survival between the ... Published values for aspartate aminotransferase (AST) concentration are both higher and lower than observed in this study. In ...

https://bioone.org/journals/journal-of-wildlife-diseases/volume-44/issue-4

... aspartate ammonia lyase), fxsA (F exclusion of bacteriophage T7), and STM14_5203, encoding a hypothetical protein of unknown ...

https://jb.asm.org/content/192/2/560?ijkey=f1276c279e8bb6640cee4591700f41bb50ffc467&keytype2=tf_ipsecsha

Conversion of aspartate into fumarate by the AspA aspartate ammonia lyase produces the volatile compound ammonia (NH3) as a by- ... aspartate aminotransferase), purA (adenylosuccinate synthetase) or aspA (aspartate ammonia lyase) grown in presence of fumarate ... 4C). Moreover, addition of l-aspartate into growth medium resulted in an increased production of ammonia by E. coli, P. ... Decreased ammonia import and assimilation impairs E. coli response to volatile ammonia. A. Metabolic pathways involved in ...

http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2011.07724.x/full

SUMMARY: The aspartase (l-aspartate ammonia-lyase, EC. 4.3.1.1) structural gene, aspA, was mapped by two-factor and three- ... The Effect of Cyclic AMP on Catabolite Repression of Isocitrate Lyase in Nocardia salmonicolor (NCIB9701) A. W. Westwood and I ... ammonia, acetate and butyrate, which are also produced by fermentation of nucleosides, purines and ribose, thus supporting our ... pyruvate-CO2 exchange and pyruvate formate lyase to be active. ...

https://www.microbiologyresearch.org/content/journal/micro/97/1

... "aspartate ammonia-lyase" FT /gene_family="HOG000061737" [ FAMILY / ALN / TREE ] FT /codon_start="1" FT /locus_tag="VVM_00383" ... pyruvate lyase" FT /gene_family="HOG000137785" [ FAMILY / ALN / TREE ] FT /codon_start="1" FT /locus_tag="VVM_00261" FT /EC_ ... "L-aspartate oxidase" FT /gene_family="HOG000160476" [ FAMILY / ALN / TREE ] FT /codon_start="1" FT /locus_tag="VVM_00912" FT / ... "aspartate carbamoyltransferase" FT /gene_family="HOG000022685" [ FAMILY / ALN / TREE ] FT /codon_start="1" FT /locus_tag="VVM_ ...

http://pbil.univ-lyon1.fr/cgi-bin/acnuc-search-id?query=VIVUL2_1&db=HOGENOMDNA&ident=ACNUC8465

Aspartate Ammonia-Lyase * Alleles * Epigenetic Repression * Poxviridae * Histone Methyltransferases * Brain Stem Neoplasms ...

https://www.scholars.northwestern.edu/en/persons/elizabeth-thomas-bartom/fingerprints/

Jin, Q., Martinez, C. A., Arcipowski, K. M., Zhu, Y., Gutierrez-Diaz, B. T., Wang, K. K., Johnson, M. R., Volk, A. G., Wang, F., Wu, J., Grove, C., Wang, H., Sokirniy, I., Thomas, P. M., Goo, Y. A., Abshiru, N. A., Hijiya, N., Peirs, S., Vandamme, N., Berx, G. & 27 others, Goosens, S., Marshall, S. A., Rendleman, E. J., Takahashi, Y. H., Wang, L., Rawat, R., Bartom, E. T., Collings, C. K., Van Vlierberghe, P., Strikoudis, A., Kelly, S., Ueberheide, B., Mantis, C., Kandela, I., Bourquin, J. P., Bornhauser, B., Serafin, V., Bresolin, S., Paganin, M., Accordi, B., Basso, G., Kelleher, N. L., Weinstock, J., Kumar, S., Crispino, J. D., Shilatifard, A. & Ntziachristos, P., Jan 1 2019, In : Clinical Cancer Research. 25, 1, p. 222-239 18 p.. Research output: Contribution to journal › Article ...

https://www.scholars.northwestern.edu/en/persons/elizabeth-thomas-bartom/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle

... ammonia-lyases explanation free. What is ammonia-lyases? Meaning of ammonia-lyases medical term. What does ammonia-lyases mean? ... Looking for online definition of ammonia-lyases in the Medical Dictionary? ... hence lyases, EC class 4), by rupture of a C-N bond leaving a double bond (EC subgroup 4.3), for example, aspartate ammonia- ... Ammonia-lyases , definition of ammonia-lyases by Medical dictionary https://medical-dictionary.thefreedictionary.com/ammonia- ...

http://medical-dictionary.thefreedictionary.com/ammonia-lyases

Aspartate ammonia-lyase (substance). Code System Preferred Concept Name. Aspartate ammonia-lyase (substance). ... Enzyme (substance) {90668006 , SNOMED-CT } Substance with lyase mechanism of action (substance) {21533003 , SNOMED-CT } ... Aspartate ammonia-lyase Current Synonym true false 134957019 Aspartase Current Synonym true false ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=81357007

... aspartate ammonia lyase) were shown to be deficient in serine and aspartate utilization respectively but both were still able ... Peptides containing either two or four aspartate residues supported some growth but this was less than when aspartate was ... It would appear then that C. jejuni can utilize peptides containing aspartate and serine as carbon sources. Mutants deficient ... L-aspartate, L-asparagine and L-glycine as sole carbon sources. Amongst the sugars tested fucose, ribose and D-glucosamine ...

http://epubs.surrey.ac.uk/843806/

4.3.1.1 Aspartate ammonia-lyase 4.3.1.2 Methylaspartate ammonia-lyase 4.3.1.3 Histidine ammonia-lyase 4.3.1.4 ... L-serine ammonia-lyase 4.3.1.18 D-serine ammonia-lyase 4.3.1.19 Threonine ammonia-lyase 4.3.1.20 Erythro-3-hydroxy-L-aspartate ... 3-aminobutyryl-CoA ammonia-lyase 4.3.1.15 Diaminopropionate ammonia-lyase 4.3.1.16 Threo-3-hydroxy-L-aspartate ammonia-lyase ... Tyrosine ammonia-lyase 4.3.1.24 Phenylalanine ammonia-lyase 4.3.1.25 Phenylalanine/tyrosine ammonia-lyase 4.3.1.26 Transferred ...

https://enzyme.expasy.org/EC/4.3.-.-

Exogenous l -Glu also caused induction of the aspA gene, most likely due to its conversion to l -Asp by the aspartate transaminase AspC. (microbiologyresearch.org)
Mutants deficient in SdaC (serine transporter) and in AspA (aspartate ammonia lyase) were shown to be deficient in serine and aspartate utilization respectively but both were still able to utilize mucin suggesting that the liberation of serine and asparate from mucin is not important for its use as a carbon source. (surrey.ac.uk)

Glutamine synthase, glutamate synthetase and dehydrogenase, alanine aminotransferase (AlaAT) and aspartate aminotransferase (AspAT) were markedly induced by the addition of NaCl. (conicyt.cl)
The activities of alanine aminotransferase (AlaAT) and aspartate aminotransferase (AspAT) showed varying changes following the copper treatments. (conicyt.cl)
Kynurenine aminotransferase 3 (KAT3) catalyzes the transamination of Kynurenine to kynurenic acid, and is identical to cysteine conjugate beta-lyase 2 (CCBL2) and glutamine transaminase L (GTL). (pubmedcentralcanada.ca)

A number of enzymes, belonging to the lyase class, for which fumarate is a substrate have been shown [ PMID: 3282546 ] to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes. (ebi.ac.uk)
The two enzymes are aspartate ammonia-lyase and ketol-acid reductoisomerase (also known as acetohydroxy acid isomeroreductase). (searlescholars.net)
Several ammonia lyases were considered as interesting enzymes to study since these enzymes are able to do a deamination on aminoacids, though different than than lysine. (chalmers.se)
The assays provided the kinetic constants of the conversion of the natural substrate, 3‐methyl aspartate, by the mutated enzymes and their plausible activity on lysine by detecting the theoretical conversion products: 6‐aminohex‐2‐enoic acid and ammonia. (chalmers.se)
Disorders of any urea cycle enzymes lead to accumulation of ammonia and it precursors (thus the high ammonia level of the infant). (love-pet.net)

Aspartate ammonia-lyase catalyses the conversion of aspartate to fumarate. (ebi.ac.uk)
In enzymology, an aspartate ammonia-lyase (EC 4.3.1.1) is an enzyme that catalyzes the chemical reaction L-aspartate ⇌ {\displaystyle \rightleftharpoons } fumarate + NH3 Hence, this enzyme has one substrate, L-aspartate, and two products, fumarate and NH3. (wikipedia.org)
The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). (wikipedia.org)
Arginosuccinase, EC:4.3.2.1 (argininosuccinate lyase), which catalyses the formation of arginine and fumarate from argininosuccinate, the last step in the biosynthesis of arginine. (ebi.ac.uk)
Aspartate ammonia-lyase, EC:4.3.1.1 (aspartase), which catalyses the reversible conversion of aspartate to fumarate and ammonia. (ebi.ac.uk)
Adenylosuccinase, EC:4.3.2.2 (adenylosuccinate lyase) [ PMID: 1574589 ], which catalyses the eighth step in the de novo biosynthesis of purines, the formation of 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide and fumarate from 1-(5-phosphoribosyl)-4-(N-succino-carboxamide). (ebi.ac.uk)
ASLD is caused by reduced or absent activity of argininosuccinate lyase (ASL), which catalyzes the hydrolytic cleavage of ASA into arginine and fumarate [ 2 , 3 ]. (hindawi.com)

Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. (wikipedia.org)
Also known as Aspartate ammonia-lyase (Aspartase). (mybiosource.com)

These results, together with those obtained with enzyme preparations, indicated pyruvate synthase, pyruvate-CO 2 exchange and pyruvate formate lyase to be active. (microbiologyresearch.org)
Isocitrate lyase (AOLE_14300) and malate synthase G (AOLE_10740) constituting the glyoxylate shunt had been previously discovered (16). (perlierusa.com)
Aspartate-ammonia lyase and asparagine synthase weren't identified in the Additionally. (perlierusa.com)
The kidney is the major organ for circulating L-Arg synthesis, utilizing citrulline conversion by argininosuccinate synthase (ASS) and lyase (ASL). (ufl.edu)
The specific disorders are: N-acetylglutamate synthase (NAGS) deficiency, Carbamyl phosphate synthetase I (CPSI) deficiency, Ornithine transcarbamylase (OTC) deficiency, Argininosuccinate synthetase (AS) deficiency (Citrullinemia), Argininosuccinate lyase (AL) deficiency (Argininosuccinic aciduria), Arginase (ARG) deficiency (Argininemia), Hyperornithinemia, hyperammonemia, homocitrullinuria (HHH) syndrome (or mitochondrial ornithine carrier deficiency-ORNT), and Citrullinemia type II (mitochondrial aspartate/glutamate carrier deficiency-CITR). (pubmedcentralcanada.ca)
Both cystathionine-γ-synthase and cystathionine-β-lyase require Pyridoxyl-5'-phosphate as a cofactor, whereas homocysteine methyltransferase requires Vitamin B 12 as a cofactor (Lehninger 2000). (newworldencyclopedia.org)

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. (wikipedia.org)
This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism. (wikipedia.org)
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). (wikipedia.org)
This enzyme catalyses the following chemical reaction threo-3-hydroxy-D-aspartate ⇌ {\displaystyle \rightleftharpoons } oxaloacetate + NH3 This enzyme is a pyridoxal-phosphate protein. (wikipedia.org)
Structural Basis for the Catalytic Mechanism of Ethylenediamine- N, N'-disuccinic Acid Lyase, a Carbon-Nitrogen Bond-Forming Enzyme with a Broad Substrate Scope. (nih.gov)
Delta-crystallin shares around 90% sequence identity with arginosuccinate lyase, showing that it is an example of a 'hijacked' enzyme - accumulated mutations have, however, rendered the protein enzymatically inactive. (ebi.ac.uk)
The enzyme studied in this research project is 3‐methylaspartate ammonia lyase (MAL) which catalyses the deamination reaction on 3methylaspartic acid. (chalmers.se)
Chronic exposure to high glucose induces the expression of cystathionine gamma-lyase (CSE), a hydrogen sulfide-producing enzyme, in pancreatic beta-cells, thereby suppressing apoptosis. (jove.com)
The third step is catalyzed by an enzyme called argininosuccinate synthetase, which uses citrulline and ATP to form a citrullyl-AMP intermediate, which reacts with an amino group from aspartate to produce argininosuccinate. (news-medical.net)
The dependence of the enzyme on pyridoxal 5′-phosphate and the production of 3H4P with the release of ammonia indicate that it is a carbon-nitrogen lyase. (plantphysiol.org)

Catalytic mechanisms and biocatalytic applications of aspartate and methylaspartate ammonia lyases. (semanticscholar.org)
Van Havere2017, author={Van Havere, Robin}, title={Engineering of 3 methylaspartate ammonia-lyases for biobased adipic acid production}, abstract={The current traditional adipic acid production is a highly polluting process. (chalmers.se)

Argininosuccinate lyase deficiency (ASLD), which is also called argininosuccinic aciduria (ASA), is the second most common urea-cycle disorder, with an estimated incidence of 1:70,000 live births in the USA [ 1 ]. (hindawi.com)
Argininosuccinate (ASA) lyase deficiency results in defective cleavage of ASA, which leads to accumulation in cells and excessive excretion in urine. (love-pet.net)

In hepatocytes, the addition of carbon dioxide and ammonia to ornithine synthesizes L-citrulline during the urea cycle. (citrullis.com)
The urea cycle or ornithine cycle converts excess ammonia into urea in the mitochondria of liver cells. (news-medical.net)
arginase is responsible for the hydrolysis of arginine into ornithine and urea, thus playing an essential role in hepatic and intestinal urea synthesis from ammonia as well as providing ornithine for the synthesis of polyamines, proline, and glutamate ( 13 , 29 , 36 ). (physiology.org)

1 ) glutaminase, ( 2 ) L-serine deaminase, ( 3 ) aspartate-ammonia lyase, ( 4 ) L-asparaginase II, ( 5 ) urease, ( 6 ) formamidase, ( 7 ) aliphatic amidase. (asmscience.org)

Phenylalanine Ammonia-lyase, Tyrosine Ammonia-lyase, and Lignin in Wheat Inoculated with Erysiphe graminis f. sp. (apsnet.org)
The preparation of phenylalanine from cinnamic acid using immobilized cells having phenylalanine ammonia lyase activity is also disclosed. (google.ca)
16. A process for preparing phenylalanine which comprises contacting cinnamic acid with immobilized cells having phenylalanine ammonia lyase actibity, said cells being immobilized with a polyazetidine polymer. (google.ca)

KAT1 is identical to glutamine transaminase K (GTK), a kidney type transaminase and cysteine conjugate beta-lyase 1 (CCBL1). (pubmedcentralcanada.ca)
Recently, it was demonstrated that KAT3 is not only identical to cysteine conjugate beta-lyase 2 (CCBL2), but also to glutamine transaminase L (GTL), a liver type glutamine transaminase [15] . (pubmedcentralcanada.ca)

In addition to 3H4P , we also identified pyruvate and ammonia as other degradation products. (plantphysiol.org)

It is a hyper-ammonia producing bacterium and is able to catabolize amino acids as important carbon and energy sources via Stickland reactions and the development of the specific pathways. (cyberleninka.org)
heparin because it has shown its capability to reduce red blood cell ammonia production, c.) a chilled heparinized vacuum tube that is immediately placed in ice, d.) the plasma should be separated within 15 minutes if allowed to sit, blood and ammonia concentration will spontaneously increase secondary to ongoing production of ammonia from red blood cells and the deamination of amino acids especially glutamine. (love-pet.net)

SUMMARY: The principal products of endogenous metabolism of the obligate anaerobe Peptococcus prévotii were carbon dioxide, ammonia, acetate and butyrate, which are also produced by fermentation of nucleosides, purines and ribose, thus supporting our previous finding that RNA is the only cellular component to undergo substantial degradation under starvation conditions. (microbiologyresearch.org)
Nitrogen metabolism in H. pylori generates considerable amounts of free ammonia that either could be incorporated into proteins via the glutamine synthetase (GS-ase) pathway or released into the external environment by diffusion in its NH 3 form. (asmscience.org)
Ammonia is a toxic product of nitrogen metabolism which should be removed from our body. (news-medical.net)

Using this media C. jejuni NCTC 11168 was shown to be able to utilise mucin, L- serine, L-proline, L-glutamic acid, L-valine, L-glutamine, L-histidine, L-tyrosine, L-aspartate, L-asparagine and L-glycine as sole carbon sources. (surrey.ac.uk)
It would appear then that C. jejuni can utilize peptides containing aspartate and serine as carbon sources. (surrey.ac.uk)

Results in excess production of ammonia. (patientcrossroads.org)

Urea cycle is one in which a series of reactions inside the body converts nitrogen into ammonia and aspartate into urea. (liverdrugs.com)

Citrulline's main function is its ability to remove ammonia and is essential for the excretion of oxidative waste processes. (citrullis.com)

the first waste nitrogen molecule derives from free ammonia in the carbamyl phosphate synthetase (CPS) reaction. (love-pet.net)

The reaction is the basis of the industrial synthesis of aspartate. (wikipedia.org)
This reaction is analogous to that catalyzed by fumarase, except that ammonia rather than water is involved in the trans-elimination reaction. (ebi.ac.uk)

Inborn errors of urea synthesis lead to an accumulation of ammonia in blood and brain, and result in high rates of mortality and neurodevelopmental disability. (pubmedcentralcanada.ca)
Inborn errors of urea synthesis lead to an accumulation of ammonia in blood and brain and clinically present as recurrent episodes of hyperammonemia manifested by vomiting, lethargy and coma. (pubmedcentralcanada.ca)

A urea cycle disorder that results in accumulation of excessive ammonia and citrulline. (patientcrossroads.org)
In mild urea cycle disorders, ammonia accumulation may be triggered by illness or stress at most times, which results to multiple mild elevations of plasma ammonia accumulation. (love-pet.net)

Using Escherichia coli K12 as a model organism, and increased resistance to tetracycline as the phenotypic read-out, we demonstrate that exposure to ammonia generated by the catabolism of l -aspartate increases the level of intracellular polyamines, in turn leading to modifications in membrane permeability to different antibiotics as well as increased resistance to oxidative stress. (wiley.com)

GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. (creativebiomart.net)

Aspartate Transcarbamylase Activity in Healthy and Virus-infected Cowpea and Soybean Leaves. (apsnet.org)

A non-essential amino acid produced in the normal urea cycle by the transfer of a nitrogen atom from aspartate to citrulline. (patientcrossroads.org)

Anatomy1

Organisms16

Diseases3

Chemicals and Drugs19

Analytical, Diagnostic and Therapeutic Techniques and Equipment2

Phenomena and Processes5

Information Science10

Health Care2

Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue. (1/36)

A monomeric L-aspartase obtained by in vitro selection. (2/36)

Thermostable aspartase from a marine psychrophile, Cytophaga sp. KUC-1: molecular characterization and primary structure. (3/36)

Possible physiological roles of aspartase, NAD- and NADP-requiring glutamate dehydrogenases of Pseudomonas fluorescens. (4/36)

Enzymes involved in anaerobic respiration appear to play a role in Actinobacillus pleuropneumoniae virulence. (5/36)

Deletion of the anaerobic regulator HlyX causes reduced colonization and persistence of Actinobacillus pleuropneumoniae in the porcine respiratory tract. (6/36)

Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase. (7/36)

A missense mutation causes aspartase deficiency in Yersinia pestis. (8/36)

Aspartate Ammonia-Lyase

Phenylalanine Ammonia-Lyase

Ammonia

Anabaena variabilis

Ammonia-Lyases

Ethanolamine Ammonia-Lyase

p-Fluorophenylalanine

Aspartate Aminotransferases

Rhodotorula

Basidiomycota

Aspartate Carbamoyltransferase

Salicylic Acid

Phenylpropionates

ATP Citrate (pro-S)-Lyase

Aspartic Acid

Plant Leaves

Plant Diseases

Histidine Ammonia-Lyase

Antibodies

Nitrosomonas europaea

Nitrobacter

Nitrosomonas

Melissa

Life Support Systems

Ecological Systems, Closed

Search Engine

Complement C3

Information Storage and Retrieval

Semiconductors

Aspergillus oryzae

Internet

PubMed

Dictyostelium

Biogenic Amines

Bacteria

Molecular Sequence Data

Anti-Bacterial Agents

Drug Resistance, Bacterial

Salmonella typhimurium

Salmonella enterica

Salmonella Infections, Animal

Salmonella Infections

Virulence

Base Sequence

Dictionaries, Medical

Dictionaries as Topic

Dictionaries, Chemical

Terminology as Topic

Campylobacter jejuni

Campylobacter

Campylobacter Infections

Campylobacter fetus

Campylobacter coli

Mucins

Culture Media

Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue. (1/36)

A monomeric L-aspartase obtained by in vitro selection. (2/36)

Thermostable aspartase from a marine psychrophile, Cytophaga sp. KUC-1: molecular characterization and primary structure. (3/36)

Possible physiological roles of aspartase, NAD- and NADP-requiring glutamate dehydrogenases of Pseudomonas fluorescens. (4/36)

Enzymes involved in anaerobic respiration appear to play a role in Actinobacillus pleuropneumoniae virulence. (5/36)

Deletion of the anaerobic regulator HlyX causes reduced colonization and persistence of Actinobacillus pleuropneumoniae in the porcine respiratory tract. (6/36)

Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase. (7/36)

A missense mutation causes aspartase deficiency in Yersinia pestis. (8/36)

Aspartate ammonia-lyase elisa and antibody

Microbial aspartase and its activity on deamination of L-aspartyl-L-phenylalanine methyl ester<...

Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and...

Cloning and nucleotide sequence of the Bacillus subtilis ansR...

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