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.

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)

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TY - JOUR. T1 - Microbial aspartase and its activity on deamination of L-aspartyl-L-phenylalanine methyl ester. AU - Chung, Wonyoon. AU - Goo, Yang Mo. PY - 1988/6. Y1 - 1988/6. N2 - Examination of many microorganisms and soil isolates for the activity of aspartase proved that R. rubra, G. suboxydans, A. versicolor, P. purpurogenum, E. coli, Ps. aeruginosa, A. gigantus, A. unguis, A. parasiticus and a soil isolate(S-90) had high activity of aspartase. Comparision of the activity of the aspartase by cell free extracts of these micro-organisms with the activity of the enzyme catalyzing the deamination of aspartame by the same cell free extracts showed similar kinetic characteristics. The aspartase existing in the cell free extracts seemed to catalyze the deamination of aspartame, too.. AB - Examination of many microorganisms and soil isolates for the activity of aspartase proved that R. rubra, G. suboxydans, A. versicolor, P. purpurogenum, E. coli, Ps. aeruginosa, A. gigantus, A. unguis, A. ...
The nucleotide sequences of two segments of DNA (2250 and 2921 base-pairs) containing the functionally related fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12 were determined. The fumC structural gene comprises 1398 base-pairs (466 codons, excluding the initiation codon), and it encodes a polypeptide of Mr 50353 that resembles the fumarases of Bacillus subtilis 168 (citG-gene product), rat liver and pig heart. The fumC gene starts 140 base-pairs downstream of the structurally-unrelated fumA gene, but there is no evidence that both genes form part of the same operon. The aspA structural gene comprises 1431 base-pairs (477 codons excluding the initiation codon), and it encodes a polypeptide of Mr 52190, similar to that predicted from maxicell studies and for the enzyme from E. coli W. Remarkable homologies were found between the primary structures of the fumarase (fumC and citG) and aspartase (aspA) genes and their products, suggesting close structural and evolutionary ...
Cloning and nucleotide sequence of the Bacillus subtilis ansR gene, which encodes a repressor of the ans operon coding for L-asparaginase and L-aspartase.: Prev
Nasdaq DM ASPA Ex Japan Large Cap Index Net Total Return Index im Überblick: Aktuelle Kurse (Realtimekurs), Chart, Nachrichten und Diskussionen zum Nasdaq DM ASPA Ex Japan Large Cap Index Net Total Return (NQDMASPAXJPL)
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is definitely a leading cause of fatal sepsis and meningitis worldwide. severe sepsis. The organism asymptomatically colonizes the nasopharyngeal mucosa especially in young adults. In susceptible individuals hyper‐invasive strains of meningococci may invade the nasopharyngeal submucosa and consequently enter the bloodstream (Stephens 2009). Diverse bacterial factors involved in adhesion invasion dissemination and safety of the organism from your innate human immune system are indicated by fimbriae (Kukkonen et?al. 1998) aspartase (Sj?str?m et?al. 1997) and protein E (Barthel et?al. 2012b). Sequestered plg contributes to processes such as ECM degradation fibrinolysis degradation of immune effectors and adherence therefore enhancing bacterial colonization MK-0812 of and dissemination within the sponsor (Bhattacharya et?al. 2012). We previously reported that FBA is definitely a nonessential surface‐localized protein in was shown to be an essential enzyme and partly localized to the bacterial ...
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ASPA兔多克隆抗体(ab97454)可与人样本反应并经WB, IP, IHC, ICC/IF实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
mouse Asph protein: 26-kDa protein isolated from cardiac junctional sarcoplasmic reticulum; hydroxylates ASP or ASN residues in EGF domains of some proteins; RefSeq NM_023066
The Leica 35mm f/1.4 Summilux-M ASPH is a versatile wide-angle lens designed for the Leica M-mount system. This makes the lens ideal for street, travel, and indoor use. The design includes one aspherical lens element to reduce spherical aberrations
Surrey data 50% of the population is Vitamin D deficient 150,000 potential cases Exponential rise in ordering of Vitamin D testing Cost per test - £2.90 ASPH
The lens is in good condition except the little red dot is missing. However, this is only cosmetic. The glass is perfect. Come with hood (no cap), len
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Canavan disease (CD) is a rare leukodystrophy caused by mutations in the ASPA gene, leading to severe neurodegeneration and short life expectancy. To date, the exact disease mechanism is poorly understood and therapeutic options are scarce. The ASPA gene encodes aspartoacylase, an enzyme catalyzing the degradation of N-acetylaspartate (NAA). Despite NAA being the second-most abundant metabolite in the mammalian brain, its functional role is poorly understood. Recently, several independent groups found NAA metabolism to also play important roles in non-nervous tissues, e.g. in adipocytes, immune cells, lung and prostate cancer cells, pointing towards a previously overlooked wide relevance of peripheral NAA metabolism.. In the PeriNAA junior research alliance, clinical, experimental and computational groups are collaborating to generate a computational model around NAA metabolism and inferring model parameters from stable isotope-assisted metabolomics data, RNA-seq data, and other experimental ...
The Panasonic Leica DG Nocticron 42.5mm f/1.2 ASPH. Features 14 elements in 11 groups. There are 9 diaphragm blades in a rounded configuration which is suited to the beautiful, rounded spherical highlights you see in the out of focus areas of the image. Bokeh has always been a difficult idea for me for many reasons. Its a term thats become part of the photography vocabulary in recent years and it refers to the pleasing quality of what is out of focus. While I understand the obsession, I think many photographers over use it to compensate for their lack of compositional skills and its easy. Just shoot wide open and forget about it.. Photography is about contrasts, its about give and take. And bokeh is also dependent on what is in focus in the image. Im fairly sure the MTF chart is theoretical and not taken from a production lens, but I feel that after using this lens extensively its a good indication of the performance. Sharp areas are sharp. This is the key to a great bokeh feel - you need ...
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One of the presentations of interest in SIDR OPS WG was on the efforts to perform some form of AS Path validation using the Autonomous System Provider Authorization (ASPA) objects.. This is a variation of the earlier soBGP AS adjacency object, where with ASPAs topological AS adjacency is combined with inter-AS policy. It relies on a coarse taxonomy of inter-AS relationships where, within a particular routed protocol, two ASes can either be peers to each other or one can be a provider for the other. In the ASPA framework, each customer AS lists the complete set of providers that are authorized to propagate routes that this AS has passed to it as a provider.. If you assume that no AS is willing to incur costs on behalf of non-customer AS neighbors, then we can arrive at the valley-free view of AS Paths. If you think about AS Paths as an ordered sequence of paired relationships, and we use the concept of elevation to describe the customer-provider relationship, then we can define a policy ...
Cyclists were about an hour ahead of schedule today as they rode into Colorado Springs on the 5th stage of the USA Pro Challenge…. Colorado Highway 67 between Florence and Wetmore has reopened…. Colorado health officials are reporting 12 people hospitalized for West Nile virus.. Audio clip: Adobe Flash Player (version 9 or above) is required to play this audio clip. Download the latest version here. You also need to have JavaScript enabled in your browser.. ...
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L-aspartic Acid found in: L-Ornithine-L-Aspartate, L Ornithine L Aspartate is a key metabolite in liver function crucial in converting ammonia to urea and glutamine thereby supporting healthy levels of ammonia
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C Aspa Scorb was formulated as a mineral transporter based on the results of studies by several researchers, principally Hans Neiper, M.D., West Germany.
If you are looking to improve indoor air quality. This product category consists of uv air purification systems designed to sterilize & destroy biological & chemical contaminants which circulate throughout the building or facility. ...
Se vaaiga i le aufaigaluega a le Pulega o le Eletise ma le Suavai (ASPA) sa gafa ma le fausiaina o le galuega tele i Faleasao, Manua, o le faaaogaina lea o le malosi o le la e maua mai ai le eletise, faatasi ai ma taitai o le atunuu e aofia ai le Faipule i le laumua i Uosigitone ia Aumua Amata, faapea ai le Taitaifono o le Komiti Faafoe a le ASPA, Fonoti Perelini. [ata AF ...
The American Academy of Certified Public Managers® (AACPM) is a professional association of public sector managers established in 1984 to promote a high professional, educational and ethical standard in public management. The AACPM is an organizational member of American Society for Public Administration (ASPA).
L-ASPARTIC ACID MAGNESIUM SALT 18962-61-3 NMR spectrum, L-ASPARTIC ACID MAGNESIUM SALT H-NMR spectral analysis, L-ASPARTIC ACID MAGNESIUM SALT C-NMR spectral analysis ect.
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35/1,4 Leica Aspheric: Used to be the bench mark lens for fast 35s. I have had mine since it was announced long time ago. Very sharp and contrasty, but not very well corrected for flare. Mine went back to Solms for a rebuild in 1998 after it started to flare badly enough to be useless. I never got an explanation what had happened, but after 6 months it was back in my hands and has behaved well ever since. Still you have to watch for strong lights at the edges. Wide-open performance is very good, sharp and contrasty, but that also means some burning and dodging when printing black/white as the contrast is almost too high. Less dramatic drop-off of sharpness than the 35/1,2 and a fairly unpleasant Bokeh. It almost looks like digital pixilation and lacks smoothness. The 35/1,4 Asph. weighs less than the 35/1,2, but not by much and it is a bit smaller. However, it does have a focusing tab which makes it quick to focus. I am not sure that the benefits of the 35/1,2 outweighs those of the 35/1,4 ...
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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 Formimidoyltetrahydrofolate cyclodeaminase 4.3.1.5 Transferred entry: 4.3.1.23, 4.3.1.24 and 4.3.1.25 4.3.1.6 Beta-alanyl-CoA ammonia-lyase 4.3.1.7 Ethanolamine ammonia-lyase 4.3.1.8 Transferred entry: 2.5.1.61 4.3.1.9 Glucosaminate ammonia-lyase 4.3.1.10 Serine-sulfate ammonia-lyase 4.3.1.11 Deleted entry 4.3.1.12 Ornithine cyclodeaminase 4.3.1.13 Carbamoyl-serine ammonia-lyase 4.3.1.14 3-aminobutyryl-CoA ammonia-lyase 4.3.1.15 Diaminopropionate ammonia-lyase 4.3.1.16 Threo-3-hydroxy-L-aspartate ammonia-lyase 4.3.1.17 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 ammonia-lyase 4.3.1.21 Transferred entry: 4.3.1.9 4.3.1.22 3,4-dihydroxyphenylalanine reductive deaminase 4.3.1.23 Tyrosine ammonia-lyase 4.3.1.24 Phenylalanine ammonia-lyase 4.3.1.25 Phenylalanine/tyrosine ammonia-lyase 4.3.1.26 Transferred entry: ...
The report focuses on United States major leading industry players providing information such as company profiles, product picture and specification, capacity, production, price, cost, revenue and contact information. Upstream raw materials and equipment and downstream demand analysis is also carried out. The L-aspartic acid industry development trends and marketing channels are analyzed. Finally the feasibility of new investment projects are assessed and overall research conclusions offered ...
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Geologist Edo V writes:. Striations are scratches into rock surfaces, made by ice (containing rocks), or inside rocks on fault planes (strict geological use of the word). I do not see them in your photo.. The orange and gray bands run down the dip of the rock surface and are probably due to water run-off (melting snow?).. The two bands that run nearly vertical in the photo are intruded sheets (dikes) of late-stage magma, probably aplitic dikes.. The NW-SE bands in the photo are edges of exfoliation sheets, layers of granite that peel off due to repeated expansion and shrinkage with temperature variations and freezing.. You are in good company. Ansel Adams has photo of a rock surface with magmatic inclusions, with dark rims which he described as shadows, but they seem to be magmatic selvedges, which are rims of dark minerals that surround the magmatic inclusions, foreign rocks which sink into a magmatic chamber from the roof of an intrusion. (I do not have the photo at hand, and may be wrong ...
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L-Aspartic acid (L-Asp) was produced using Escherichia coli (ATCC 11303), and its recovery from the reaction mixture was studied using reverse micelle and gas hydrate methods. The effect of initial substrate concentration on L-Asp production was also investigated, and inhibition was shown to occur above 0.75 mol L-1. The values of the kinetic constants were determined as r(max) = 2.33 x 10(-4) mol L-1 min(-1), K-M = 0.19 mol L-1, and K-ss = 3.98 mol L-1. The reverse micelle phase used for extraction contained Aliquat-336, 1-decanol and isooctane, and a micro-injection technique was used for extraction of L-Asp. The reverse micelle system is a useful technique for obtaining small particle sizes, which can be used for the synthesis of nanoparticle biomolecules. Recovery of L-Asp from reverse micelles using CO2 hydrates was carried out, giving a recovery of 55%. The formation of CO2 hydrate from the reverse micelle solution breaks the micelle by reducing the amount of water in the micelle ...
China Polyaspartic Acid (PASP) , Fertilizer Synergist, Find details about China Polyaspartic Acid, Poly L-Aspartic Acid Salts from Polyaspartic Acid (PASP) , Fertilizer Synergist - Qingdao Reach International Inc.
Synonyms Zinc dihydrogen di-L-aspartate; L-Aspartic acid zinc salt; Zinc (3S)-3-amino-4-hydroxy-4-oxobutanoate. Molecular Formula: 2(C4H6NO4).Zn. Molecular Weight: 329.60. CAS Registry Number: 36393-20-1. EINECS: 253-012-5. ...
Adenine 10 mg/L; L-Arginine HCl 50 mg/L; L-Aspartic Acid 80 mg/L; L-Histidine HCl 20 mg/L; L-Isoleucine 50 mg/L; L-Lysine HCl 50 mg/L; L-Methionine 20 mg/L; L-Phenylalanine 50 mg/L; L-Threonine 100 mg/L; L-Tyrosine 50 mg/L; L-Valine 140 mg/L ...
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Antevenio, graphique historique - logiciel danalyse technique de bourse en ligne, paramétrable avec sauvegarde de votre travail - affichage de 1 jour à 25 ans
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In this work, a novel and extra sensitive method for on-line continues monitoring of Clarithromycin in whole blood sample was introduced based on coupling of electro-membrane extraction (EME) and stripping fast Fourier transform continuous cyclic voltammetry (SFFTCCV). In this method, the potential waveform was continuously applied on a Poly(L-Aspartic Acid)/Graphite Oxide/Pristine Graphene/Glassy Carbon Electrode and the electrode response was obtained by detracting the background current and in the following integrating the current in the specific potential range of oxidation of the analyte. This method was performed by applying a DC potential and migration of Clarithromycin from the sample solution into a layer of 4-methyl-2-pentanol that is immobilized in the pores of the sheet membrane and then migration into the acceptor solution. A low and valuable detection limit of 1.0 ng ml-1 and quantification limit of 6.0 ng ml-1 are considered as a part of the sensible results of this experiment.
The UK has long been hailed as one of the world leaders in animal welfare. Within the UK, animals used in experiments are provided some protection under the Animals (Scientific Procedures) Act 1986 (ASPA). This Act was impacted by European Union (EU) Directive 2010/63/EU, and subsequently the ASPA was updated to reflect any changes required. While the Directive is very similar to the protection the UK already afforded to animals used in experiments, there were some advances that the Directive provided that were not present in the ASPA. On paper, the changes introduced were promising but may not have been achieved in practice. In 2016, the British public voted to leave the EU, which presented concerns over animal welfare protection and legislation provided by EU law. With the completion of Brexit, there may be an opportunity to diverge from the Directive to advance protection for animals used in experiments. This article explores the influence that the EU has had on animal experimentation in the ...
New series of Fe(II) complexes and Schiff base amino acids have been designed and synthesized from the bioactive ligands by condensation of 5-bromo-2-hydroxybenzaldehyde and α-amino acids (l-alanine (ala), l-phenylalanine (phala), l-aspartic acid (aspa), l-histidine (his) and l-arginine (arg)). Elemental analyses, infrared, ultraviolet-visible spectra, as well as conductivity and magnetic susceptibility measurements are used to elucidate the structure of the newly ... Read more. ...
Es pe ci a study by Shchelochkov et al. Predictably,. Abbreviations: TGFβ Tumor Growth Factor Beta; ASPN Asporin; CAF, Cancer-associated Fibroblasts; DCN Decorin; ECM, Extracellular Matrix. Liquids empty more slowly and chewing your food thoroughly before ingesting it. Tricyclic antidepressants. Heartburn or reflux into the chest when swallowing nausea fever and pain after. Struggles: Sixty-eight weeks is the backing. TEA CONFERENCE CALL & Price Here Pros of STIOLTO.. NON-SLIP BOTTOM & ELASTIC STRAPSThis - seat massager be designed with soft and travels easily. Lifeway Mitigating these symptoms stop taking your medicine and the proper position. L-aspartic acid. ACID. Exceptions were the inverse association between low stomach acid relieving that burning pain in. comAbout Global Market Monitor is a term I dont disturb one another I change. Chaulai ka Saag.. Closely Prz Gastroenterol 9(5): 297-301. L-aspartic acid. Pharmacological measures will include tightness or pressure in check.. Undergoed ...
©SHRM 2012 About SHRM Founded as the American Society for Personnel Administration (ASPA) in ASPA became the Society for Human Resource Management in 1989 to reflect the organizations broadening scope. Since SHRMs 50th anniversary in 1998, the membership has grown from 90,000 to more than 258,000 today. Members represent all functional areas, industries and titles. Membership is individual. Discounted student membership is available for individuals enrolled in a minimum of 6 credit hours per semester in HR coursework. Active members who may be transitioning between jobs and are up for renewal may qualify for a one-year free membership. There are more than 575 chapters nationally and over 6000 volunteers participating in SHRM activities. 3
Under mild conditions, the reaction of alkylidene, arylidene, and heteroarylidene malonates with tosylhydrazone salts in the presence of catalytic amount of Rh-2(OAc)(4) and triphenylarsine affords trans-2,3- disubstituted cyclopropane 1,1-dicarboxylic esters in high yields and high diastereoselectivities. (C) 2008 Elsevier Ltd. All rights reserved ...
Name L-Aspartate Magnesium. Synonyms Magnesium dihydrogen di-L-aspartate; L-Aspartic acid magnesium salt; Magnesium (3S)-3-amino-4-hydroxy-4-oxobutanoate. Molecular Formula: 2(C4H6NO4).Mg. Molecular Weight: 288.49. CAS Registry Number: 288.49. EINECS: 218-191-6. ...
0.05% w/v L-Citrulline, 0.05% w/v Glycine, 0.05% w/v L-(-)-Threonine, 0.05% w/v L-(+)-Lysine, 0.05% w/v L-Alanine, 0.05% w/v L-Arginine, 0.05% w/v L-Asparagine monohydrate, 0.05% w/v L-Aspartic acid, 0.05% w/v L-Glutamic acid, 0.05% w/v L-Glutamine, 0.05% w/v L-Histidine, 0.05% w/v L-Isoleucine, 0.05% w/v L-Leucine, 0.05% w/v L-Methionine, 0.05% w/v L-Phenylalanine, 0.05% w/v L-Proline, 0.05% w/v L-Serine, 0.05% w/v L-Tryptophan, 0.05% w/v L-Tyrosine, 0.05% w/v L-Valine, 0.02 M HEPES sodium pH ...
0.05% w/v Glycine, 0.05% w/v L-(-)-Threonine, 0.05% w/v L-(+)-Lysine, 0.05% w/v L-Alanine, 0.05% w/v L-Arginine, 0.05% w/v L-Asparagine, 0.05% w/v L-Aspartic acid, 0.05% w/v L-Glutamic acid, 0.05% w/v L-Glutamine, 0.05% w/v L-Histidine, 0.05% w/v L-Isoleucine, 0.05% w/v L-Leucine, 0.05% w/v L-Methionine, 0.05% w/v L-Phenylalanine, 0.05% w/v L-Proline, 0.05% w/v L-Serine, 0.05% w/v L-Tryptophan, 0.05% w/v L-Tyrosine, 0.05% w/v L-Valine, 0.02 M HEPES sodium pH ...
Bodyflex AM contains Cold Processed Whey Protein Isolate, L-Lysine, L-Glutamine, L-Threonine, L-Proline, L-Aspartic Acid, a Multi-Vitamin and many more!
The noroviruses (former called Norwalk virus), members of the Caliciviridaefamily, are pathogens with a world wide distribution. Due to the induction of short-term immunity, the human population is very susceptible to infections with these viruses. Outbreaks of norovirus gastroenteritis are typically caused by food and drinking water contaminated with faeces or sewage ...
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' ...
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. ...
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- ...
... 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, ...
... (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) 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 ...
Industrially, aspartate is produced by amination of fumarate catalyzed by L-aspartate ammonia-lyase. Racemic aspartic acid can ... 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) ... It carries reducing equivalents in the malate-aspartate shuttle, which utilizes the ready interconversion of aspartate and ...
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 ... Notice that aspartate and glutamate are the principal groups that act as Brønsted bases, and the common references to these as ... Thus for aspartate or glutamate with negative side chains, the terminal amino group is essentially entirely in the charged form ...
Industrially, aspartate is produced by amination of fumarate catalyzed by L-aspartate ammonia-lyase.[10] ... The conversion of aspartate to these other amino acids begins with reduction of aspartate to its "semialdehyde", O2CCH(NH2)CH2 ... It carries reducing equivalents in the malate-aspartate shuttle, which utilizes the ready interconversion of aspartate and ... Aspartic acid (symbol Asp or D;[4] the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis ...
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 ...
... 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 ...
The purine nucleotide cycle is a metabolic pathway in which ammonia and fumarate are generated from aspartate and inosine ... Aspartate + IMP + GTP → Adenylosuccinate + GDP + Pi Finally, adenylosuccinate is cleaved by the enzyme adenylosuccinate lyase ... Aspartate can re-enter purine nucleotide cycle. Oxaloacetic acid + Glutamate ↔ α-Ketoglutarate + Aspartate (catalysed by ... Lowenstein J.M. (1972). "Ammonia Production in Muscle and Other Tissues: the Purine Nucleotide Cycle". Physiological Reviews. ...
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 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 ...
... 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 ...
EC 6.3.1.1 aspartate-ammoniaque ligase EC 6.3.1.2 glutamate-ammoniaque ligase EC 6.3.1.3 maintenant EC 6.3.4.13 EC 6.3.1.4 ... 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 6.2.1.26 ... ammonia) EC 6.3.4.17 formate-dihydrofolate ligase EC 6.3.4.18 5-(carboxyamino)imidazole ribonucleotide synthase EC 6.3.4.19 ... L-aspartate-adding) EC 6.3.2.30 cyanophycine synthase (L-arginine-adding) EC 6.3.2.31 coenzyme F420-0:L-glutamate ligase EC 6.3 ...
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. ...
Aspartate ammonia lyases. (standard format). *Standard format: bottle format (50mg). *Kit contents: 9 enzymes ...
Aspartate ammonia-lyase. 79. SEQF2940,KI515728.1. SEQF2940_00081 jb [NA] [AA] 846/281. 81359-80514. ATP ... Aspartate--tRNA(Asp/Asn) ligase. 186. SEQF2940,KI515728.1. SEQF2940_00189 jb [NA] [AA] 933/310. 191067-191999. hypothetical ... Aspartate carbamoyltransferase. 155. SEQF2940,KI515728.1. SEQF2940_00158 jb [NA] [AA] 609/202. 164974-164366. Bifunctional ...
aspartate ammonia-lyase. 33. SEQF3513,VSEI01000019.1. TYA32046.1 jb [NA] [AA] 1038/345. 5779-6816. glycosyltransferase family 9 ... threonine ammonia-lyase. 64. SEQF3513,VSEI01000017.1. TYA32077.1 jb [NA] [AA] 936/311. 12451-11516. cell division protein FtsX ... aspartate--ammonia ligase. 100. SEQF3513,VSEI01000015.1. TYA32113.1 jb [NA] [AA] 984/327. 15105-14122. tRNA dihydrouridine(20/ ...
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 ...
aspartate ammonia-lyase. 47. SEQF3493,VSEW01000019.1. TYA87105.1 jb [NA] [AA] 483/160. 4416-4898. membrane protein FxsA. ... aspartate--ammonia ligase. 136. SEQF3493,VSEW01000015.1. TYA87311.1 jb [NA] [AA] 453/150. 18498-18950. transcriptional ...
L-aspartate ammonia-lyase. Psest_4074. Psest_2682. 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 ...
"Aspartate ammonia-lyase [Ensembl]. Lyase, Fumarase C C-terminus [Interproscan].","protein_coding" "AKP14235","WX61_00146"," ... "ethanolamine ammonia-lyase, large subunit, heavy chain [Ensembl]. Ethanolamine ammonia lyase large subunit (EutB) [Interproscan ... ","pyruvate formate-lyase 1 activating enzyme [Ensembl]. 4Fe-4S single cluster domain [Interproscan].","protein_coding" " ... ","L-aspartate oxidase [Ensembl]. FAD binding domain [InterProScan].","protein_coding" "AGT23149","N559_1389","Klebsiella ...
Aspartate ammonia-lyase (EC 4.3.1.1) (aspartase), which catalyzes the reversible conversion of aspartate to fumarate and ... FUMARATE_LYASES, PS00163; Fumarate lyases signature (PATTERN). * Consensus pattern:. G-S-x(2)-M-x-{RS}-K-x-N ... A number of enzymes, belonging to the lyase class, for which fumarate is a substrate have been shown [1,2] to share a short ... This reaction is analogous to that catalyzed by fumarase, except that ammonia rather than water is involved in the trans- ...
Industrially, aspartate is produced by amination of fumarate catalyzed by L-aspartate ammonia-lyase.[10] ... The conversion of aspartate to these other amino acids begins with reduction of aspartate to its "semialdehyde", O2CCH(NH2)CH2 ... It carries reducing equivalents in the malate-aspartate shuttle, which utilizes the ready interconversion of aspartate and ... Aspartic acid (symbol Asp or D;[4] the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis ...
... aspartate ammonia-lyase , iron(III) dicitrate transport protein (fecA) , bifunctional 3,4-dihydroxy-2-butanone 4-phosphate ... hypothetical protein , S-ribosylhomocysteinase , cystathionine gamma-synthase/cystathionine beta-lyase , cysteine synthetase ( ... aspartate aminotransferase , ipid-A-disaccharide synthase , exonuclease VII-like protein (xseA) , chemotaxis protein (cheY) , ... cystathionine gamma-synthase/cystathionine beta-lyase , cysteine synthetase (cysK) , ferredoxin , glutamate-1-semialdehyde ...
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 - - - - - - ...
HINTZ, H.F., LOWE, J.E., CLIFFORD, A.J. & VISEK, W.J. (1970). Ammonia intoxication resulting from urea ingestion by ponies. J. ... Carbamyl phosphate reacts with ornithine to form citrulline which combines with aspartate to form argininosuccinate. This ... arginine-lyase. The fetal liver was capable of synthesizing urea 28 days (in pigs), and 19 days (in rats) after gestation ( ... This is a cyclic process in which the initial step is the reaction between carbon dioxide and ammonia to yield carbamyl ...
It is a hyper-ammonia producing bacterium and is able to catabolize amino acids as important carbon and energy sources via ... Aspartate yhdR 2.6.1.1 Aspartate transaminase. D-Serine dsdA 4.3.1.18 D-Serine ammonia-lyase ... is able to catabolize both D-serine and L-serine due to its genome contains D-serine ammonia-lyase and D-serine ammonia-lyase. ... A putative L-cysteine sulfide lyase found to degrade L-cysteine into pyruvate, ammonia and hydrogen sulfide. Methionine ...
We found that l-cysteine desulfidase, an enzyme that catalyzes the production of H2S and ammonia from l-cysteine24, was ... 4b). We found that 7 out of the 8 O-acetylhomoserine (thiol)-lyase proteins (including one from Faecalibacterium) and all 5 ... including 8 aspartate aminotransferase (AST) proteins (K00812 or K00813) and 6 malate dehydrogenase (MDH) proteins (K00024) ( ... lyase proteins (K01740) and 5 cysteine synthase A proteins (K01738) (Fig. ...
Ammonia is a normal constituent of all body fluids. At physiologic pH, it exists mainly as ammonium ion. ... Ammonia-induced activation of p53 in cultured astrocytes: role in cell swelling and glutamate uptake. Neurochem Int. 2009 Jul- ... Argininosuccinic lyase (AL) deficiency: This enzyme cleaves argininosuccinic acid to yield fumarate and arginine. The lack of ... Argininosuccinic acid synthetase (AS) deficiency: Citrulline combines with aspartate to form argininosuccinic acid. The AS ...
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 ...
Aspartic acid is produced by the addition of ammonia to fumarate using a lyase.[122] ... Aspartate Asp D Anion Brønsted base Negative −3.5 133.104 5.49 GAY Cysteine Cys C Thiol Brønsted acid Neutral 2.5 250 0.3 ... For example, aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate.[123] Other ... Aspartate ("aspartic acid", Asp, D, p. K. a. =. 4.1. {\displaystyle \mathrm {p} K_{\mathrm {a} }=4.1}. ): -O2CCH2− ...
Aspartate N-acetyltransferase. Aspartate ammonia-lyase. Aspartate carbamoyltransferase. Aspartate kinase. Aspartate racemase. ... Aspartate--ammonia ligase. Aspartate--ammonia ligase (ADP-forming). Aspartate--phenylpyruvate transaminase. Aspartate--tRNA ... 3-aminobutyryl-CoA ammonia-lyase. 3-beta(or 20-alpha)-hydroxysteroid dehydrogenase. 3-beta-hydroxy-5-alpha-steroid ... Adenylosuccinate lyase. Adenylosuccinate synthase. Adenylyl sulfate reductase (thioredoxin). Adenylyl-[glutamate--ammonia ...
Toxic ammonia is transformed into harmless urea. It eliminates two waste products: ammonia and CO2. ... NH4+ + CO2 + Aspartate + 3ATP → Urea+ Fumarate + 2ADP + 2 Pi + AMP + PPi ... whereas the cytoplasm contains argininosuccinate synthetase and argininosuccinate lyase. ... If the urea cycle fails, the level of ammonia in the blood rises, resulting in hyperammonemia. Ammonia has the ability to pass ...
... was found to be produced from arginine and fumarate by the reverse activity of the urea cycle enzyme argininosuccinate lyase ( ... However, cells were maintained in DMEM, which does not contain aspartate and no net uptake of the small amount of aspartate ... 20 mM ammonia carbonate plus 0.1% ammonia hydroxide in water. Mobile phase D: acetonitrile. The flow rate was kept at 100 μL/ ... Zheng, L., MacKenzie, E.D., Karim, S.A. et al. Reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer ...
EC 4.3.1.11 Deleted entry: dihydroxyphenylalanine ammonia-lyase. The entry had been drafted on the basis of a single abstract ... L-aspartate synthase (ambiguous). Systematic name: cyanophycin:L-aspartate ligase (ADP-forming). Comments: Requires Mg2+ for ... Other name(s): α-hydroxynitrile lyase; hydroxynitrile lyase; acetone-cyanhydrin lyase [mis-spelt]; acetone-cyanohydrin acetone- ... Systematic name: 3,4-dihydroxy-L-phenylalanine ammonia-lyase (3,4-dihydroxyphenylpropanoate-forming). Comments: Forms part of ...
EC 6.3.1.1 aspartate-ammoniaque ligase EC 6.3.1.2 glutamate-ammoniaque ligase EC 6.3.1.3 maintenant EC 6.3.4.13 EC 6.3.1.4 ... 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 6.2.1.26 ... ammonia) EC 6.3.4.17 formate-dihydrofolate ligase EC 6.3.4.18 5-(carboxyamino)imidazole ribonucleotide synthase EC 6.3.4.19 ... L-aspartate-adding) EC 6.3.2.30 cyanophycine synthase (L-arginine-adding) EC 6.3.2.31 coenzyme F420-0:L-glutamate ligase EC 6.3 ...
lyase. Carbamoyl-. phosphate. synthase. [ammonia],. mitochondrial. Glutamate. dehydrogenase. 1,. mitochondrial. Ornithine. ... Aspartate. aminotransferase,. cytoplasmic. Nitric oxide. synthase, brain. Bifunctional. glutamate/proline-. -tRNA ligase. ...
PALs, phenylalanine ammonia lyases; PAAS, phenylacetaldehyde synthase; PAR, phenylacetaldehyde reductase; Supplementary Data S1 ... Kirma, M.; Araújo, W.L.; Fernie, A.R.; Galili, G. The multifacted role of aspartate-family amino acids in plant metabolism. J. ... by phenylalanine ammonia lyase (PALs) [75], and then trans-CA is converted into benzaldehyde and benzyl alcohol (Figure S8). ... and trans-cinnamic acids have different effects on the catalytic properties of Arabidopsis phenylalanine ammonia lyases PAL1, ...
S-ribosylhomocysteine lyase. 321. SEQF3500,VSEA01000012.1. TYB19792.1 jb [NA] [AA] 660/219. 6261-5602. bifunctional tRNA ... bifunctional aspartate kinase/homoserine dehydrogenase I. 304. SEQF3500,VSEA01000013.1. TYB19775.1 jb [NA] [AA] 1389/462. 49039 ... type I glutamate--ammonia ligase. 315. SEQF3500,VSEA01000013.1. TYB19786.1 jb [NA] [AA] 1284/427. 57934-56651. adhesin. ...
Ethanolamine Ammonia-Lyase. An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.. ... Aspartate Aminotransferases. Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate ... Pyruvate OxidaseThiamine PyrophosphateCobaltPyruvate DecarboxylaseDithionitrobenzoic AcidEthanolamine Ammonia-LyaseLyases ... Thiamine PyrophosphateCobaltPyruvate DecarboxylaseDithionitrobenzoic AcidEthanolamine Ammonia-LyaseEnzyme StabilityLyases ...
  • 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)
  • The biosynthesis of aspartate is facilitated by an aminotransferase enzyme: the transfer of an amine group from another molecule such as alanine or glutamine yields aspartate and an alpha-keto acid. (wikipedia.org)
  • 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)
  • Argininosuccinate was found to be produced from arginine and fumarate by the reverse activity of the urea cycle enzyme argininosuccinate lyase (ASL), making these cells auxotrophic for arginine. (biomedcentral.com)
  • En biochimie , une ligase est une enzyme qui catalyse la jonction de deux molécules (en anglais ligation ) par de nouvelles liaisons covalentes avec hydrolyse concomitante de l' ATP ou d'autres molécules similaires. (wikipedia.org)
  • An enzyme that catalyzes the conversion of L-tryptophan and water to indole, pyruvate, and ammonia. (lookformedical.com)
  • Oxaloacetate is converted to aspartate using a transaminase enzyme. (smpdb.ca)
  • The enzyme transfers the amino group from glutamate to oxaloacetate producing alpha-ketoglutarate and aspartate. (smpdb.ca)
  • Arginosuccinase (EC 4.3.2.1 ) (argininosuccinate lyase), which catalyzes the formation of arginine and fumarate from argininosuccinate, the last step in the biosynthesis of arginine. (expasy.org)
  • This cycle of reactions involves several enzymes including carbamyl phosphate synthetase, ornithine carbamylase, argininosuccinate synthetase and arginine-lyase. (inchem.org)
  • Adenylosuccinase (EC 4.3.2.2 ) (adenylosuccinate lyase) [ 3 ], which catalyzes the eight 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). (expasy.org)
  • Adenylosuccinate lyase deficiency is a rare, autosomal recessive defect of purine metabolism affecting purinosome assembly and reducing metabolite fluxes through both de novo purine synthesis (DNPS) and purine nucleotide recycling pathways. (medlink.com)
  • The purinosome is a multienzyme complex of DNPS enzymes (including adenylosuccinate lyase) that cells transiently assemble in their cytosol to address both depletion of and increased demand for purines. (medlink.com)
  • Clinically, adenylosuccinate lyase deficiency is generally categorized into three phenotypes: a fatal neonatal form, a severe form (type I), and a milder form (type II). (medlink.com)
  • Neurologic symptoms are the most common and prominent clinical problems associated with adenylosuccinate lyase deficiency. (medlink.com)
  • Diagnosis of adenylosuccinate lyase deficiency may be delayed or missed because patients can present with nonspecific features, such as developmental delay, autism spectrum disorder, or epilepsy. (medlink.com)
  • Adenylosuccinate lyase deficiency can be diagnosed by detection of elevated metabolites along the DNPS pathway (succinylpurines) in body fluids. (medlink.com)
  • No specific FDA-approved treatment is available for adenylosuccinate lyase deficiency. (medlink.com)
  • The clinical presentation of adenylosuccinate lyase deficiency varies greatly with respect to age of onset, clinical manifestations, and rate of disease progression. (medlink.com)
  • Patients with adenylosuccinate lyase deficiency can present with nonspecific symptoms, such as developmental delay, autism spectrum disorder, or epilepsy, including infantile spasms. (medlink.com)
  • Selective screening for adenylosuccinate lyase deficiency should be performed in infants who have neurologic disease without clear etiology, especially if supportive MRI findings are also present (eg, delayed or lack of myelination, abnormal white matter signal, and atrophy of the cerebrum or cerebellum). (medlink.com)
  • Detection of succinylpurines in body fluids by high-performance liquid chromatography or liquid chromatography-tandem mass spectrometry is the preferred biochemical test for adenylosuccinate lyase deficiency. (medlink.com)
  • 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)
  • In the human body, aspartate is most frequently synthesized through the transamination of oxaloacetate . (wikipedia.org)
  • Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. (lookformedical.com)
  • Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. (wikipedia.org)
  • Aspartate ammonia-lyase (EC 4.3.1.1 ) (aspartase), which catalyzes the reversible conversion of aspartate to fumarate and ammonia. (expasy.org)
  • The urea cycle enzymes ornithine carbamoyltransferase and arginase are also found in the mitochondria, whereas the cytoplasm contains argininosuccinate synthetase and argininosuccinate lyase. (vedantu.com)
  • Carbamyl phosphate reacts with ornithine to form citrulline which combines with aspartate to form argininosuccinate. (inchem.org)
  • Argininosuccinate synthase combines with citrulline and aspartate to generate argininosuccinate. (vedantu.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)
  • 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)
  • Acute urea toxicity in cattle may be due to ammonia formed by the rapid breakdown of urea by rumen microorganisms (Blood & Henderson, 1963). (inchem.org)
  • 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)
  • Because the urea cycle cannot continue without ornithine inside the mitochondria, ammonia disposal slows, and blood ammonia levels rise. (medscape.com)
  • In the mitochondria of liver cells, the urea cycle converts excess ammonia to urea. (vedantu.com)
  • The urea cycle converts highly toxic ammonia to urea, which is then excreted. (vedantu.com)
  • Only the liver has all of the enzymes needed to generate urea from ammonia, and this route is only located in periportal hepatocytes. (vedantu.com)
  • The urea cycle, also known as the "Ammonia Detox Cycle", is the process by which ammonia is removed from the body. (vedantu.com)
  • Toxic ammonia is transformed into harmless urea. (vedantu.com)
  • In the asparagine synthetase reaction, ATP is used to activate aspartate, forming beta-aspartyl-AMP. (smpdb.ca)
  • Threonine catabolism in mammals appears to be due primarily (70-80%) to the activity of threonine dehydrogenase (EC 1.1.1.103) that oxidizes threonine to 2-amino-3-oxobutyrate, which forms glycine and acetyl CoA, whereas threonine dehydratase (EC 4.2.1.16) that catabolizes threonine into 2-oxobutyrate and ammonia, is significantly less active. (smpdb.ca)
  • This reaction is analogous to that catalyzed by fumarase, except that ammonia rather than water is involved in the trans-elimination reaction. (expasy.org)
  • This is a cyclic process in which the initial step is the reaction between carbon dioxide and ammonia to yield carbamyl phosphate. (inchem.org)
  • Carbamoyl phosphate is produced from ammonia and bicarbonate by carbamoylphosphate synthetase I. This reaction is stimulated by ornithine. (medscape.com)
  • In proteins aspartate sidechains are often hydrogen bonded to form asx turns or asx motifs , which frequently occur at the N-termini of alpha helices . (wikipedia.org)
  • Interestingly, methylamine and ammonia levels are reciprocally controlled by a semicarbazide-sensitive amine oxidase activity that deaminates methylamine to formaldehyde with the production of ammonia and hydrogen peroxide. (smpdb.ca)
  • Infants with argininosuccinic lyase deficiency may present with hepatomegaly. (medscape.com)
  • En fait la synthase forme et défait les doubles liaisons d'une protéine. (wikipedia.org)
  • [4] the ionic form is known as aspartate ), is an α- amino acid that is used in the biosynthesis of proteins. (wikipedia.org)
  • D -Aspartate is one of two D -amino acids commonly found in mammals. (wikipedia.org)
  • The conversion of aspartate to these other amino acids begins with reduction of aspartate to its "semialdehyde", O 2 CCH(NH 2 )CH 2 CHO. (wikipedia.org)
  • These symptoms correlate with an ammonia level of 100-150 µmol/L, which is 2-3 times the reference range. (medscape.com)
  • The intermittent nature of the symptoms is due to a periodic exacerbation of ammonia level. (medscape.com)