An enzyme of the urea cycle which splits argininosuccinate to fumarate plus arginine. Its absence leads to the metabolic disease ARGININOSUCCINIC ACIDURIA in man. EC 4.3.2.1.
An enzyme of the urea cycle that catalyzes the formation of argininosuccinic acid from citrulline and aspartic acid in the presence of ATP. Absence or deficiency of this enzyme causes the metabolic disease CITRULLINEMIA in humans. EC 6.3.4.5.
Rare autosomal recessive disorder of the urea cycle which leads to the accumulation of argininosuccinic acid in body fluids and severe HYPERAMMONEMIA. Clinical features of the neonatal onset of the disorder include poor feeding, vomiting, lethargy, seizures, tachypnea, coma, and death. Later onset results in milder set of clinical features including vomiting, failure to thrive, irritability, behavioral problems, or psychomotor retardation. Mutations in the ARGININOSUCCINATE LYASE gene cause the disorder.
This amino acid is formed during the urea cycle from citrulline, aspartate and ATP. This reaction is catalyzed by argininosuccinic acid synthetase.
A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.
A ureahydrolase that catalyzes the hydrolysis of arginine or canavanine to yield L-ornithine (ORNITHINE) and urea. Deficiency of this enzyme causes HYPERARGININEMIA. EC 3.5.3.1.
A heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. The presence of these proteins accounts for the transparency of the lens. The family is composed of four major groups, alpha, beta, gamma, and delta, and several minor groups, which are classed on the basis of size, charge, immunological properties, and vertebrate source. Alpha, beta, and delta crystallins occur in avian and reptilian lenses, while alpha, beta, and gamma crystallins occur in all other lenses.
An essential amino acid that is physiologically active in the L-form.
Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.
The sodium salt of BENZOIC ACID. It is used as an antifungal preservative in pharmaceutical preparations and foods. It may also be used as a test for liver function.
A group of diseases related to a deficiency of the enzyme ARGININOSUCCINATE SYNTHASE which causes an elevation of serum levels of CITRULLINE. In neonates, clinical manifestations include lethargy, hypotonia, and SEIZURES. Milder forms also occur. Childhood and adult forms may present with recurrent episodes of intermittent weakness, lethargy, ATAXIA, behavioral changes, and DYSARTHRIA. (From Menkes, Textbook of Child Neurology, 5th ed, p49)
A urea cycle enzyme that catalyzes the formation of orthophosphate and L-citrulline (CITRULLINE) from CARBAMOYL PHOSPHATE and L-ornithine (ORNITHINE). Deficiency of this enzyme may be transmitted as an X-linked trait. EC 2.1.3.3.
A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.
An amino acid produced in the urea cycle by the splitting off of urea from arginine.
A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
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.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Glucocorticoids mediate the enhanced expression of intestinal type II arginase and argininosuccinate lyase in postweaning pigs. (1/123)

Arginine metabolism is enhanced in the small intestine of weanling pigs, but the molecular mechanism(s) involved is not known. The objectives of this study were to determine the following: 1) whether glucocorticoids play a role in induction of intestinal arginine metabolic enzymes during weaning; 2) whether the induction of enzyme activities was due to increases in corresponding mRNA levels; and 3) the identity of the arginase isoform(s) expressed in the small intestine. Jejunum was obtained from 29-d-old weaned pigs that were or were not treated with 17-beta-hydroxy-11beta-(4-dimethylaminophenyl)17alpha-(prop- 1-ynyl)es tra-4,9-dien-3-one (RU486, an antagonist of glucocorticoid receptors), or from age-matched suckling pigs. Activities and mRNA levels for type I and type II arginases, argininosuccinate synthase (ASS) and argininosuccinate lyase (ASL) were determined. Activities of arginase, ASL and ASS increased by 635, 56 and 106%, respectively, in weanling pigs, compared with suckling pigs. RU486 treatment attenuated the increase in arginase activity by 74% and completely prevented the ASL induction in weanling pigs, but had no effect on ASS activity. Pig intestine expresses both type I and type II arginases. On the basis of immunoblot analyses, there was no significant difference in levels of intestinal type I arginase among these three groups of pigs, indicating that changes in arginase activity were due only to type II arginase. The mRNA levels for type II arginase and ASL increased by 135 and 198%, respectively, in weanling pigs compared with suckling pigs, and this induction was completely prevented by RU486. In contrast, ASS mRNA levels did not differ between suckling and weanling pigs. These results suggest that intestinal type II arginase, ASS and ASL are regulated differentially at transcriptional and post-translational levels and that glucocorticoids play a major role in the induction of type II arginase and ASL mRNAs in the small intestine of weanling pigs.  (+info)

Competitive inactivation of a double-strand DNA break site involves parallel suppression of meiosis-induced changes in chromatin configuration. (2/123)

In Saccharomyces cerevisiae, DNA double-strand breaks (DSBs) initiate meiotic recombination at open sites in chromatin, which display a meiosis-specific increase in micrococcal nuclease (MNase) sensitivity. The arg4 promoter contains such a DSB site. When arg4 sequences are placed in a pBR322-derived insert at HIS4 (his4 :: arg4 ), the presence of strong DSB sites in pBR322 sequences leads to an almost complete loss of breaks from the insert-borne arg4 promoter region. Most of the MNase-sensitive sites occurred at similar positions in insert-borne and in normal ARG4 sequences, indicating that hotspot inactivation is not a consequence of changes in nucleosome positioning. However, a meiosis-specific increase in MNase hypersensitivity was no longer detected at the inactive insert-borne arg4 DSB site. Elimination of pBR322 sequences restored DSBs to the insert-borne arg4 promoter region and also restored the meiotic induction of MNase hypersensitivity. Thus, the meiotic induction of MNase hypersensitivity at the DSB sites is suppressed and activated in parallel to DSBs themselves, without changes in the underlying DNA sequence or nucleosome positioning. We suggest that meiosis-specific changes in chromatin at a DSB site are a signal reflecting a pivotal step in DSB formation.  (+info)

Expression of Escherichia coli K-12 arginine genes in Pseudomonas fluorescens. (3/123)

Escherichia coli argE and argH gene products were detected in Pseudomonas fluorescens argH122 carrying the E. coli F110 plasmid.  (+info)

Use of a recombination reporter insert to define meiotic recombination domains on chromosome III of Saccharomyces cerevisiae. (4/123)

In Saccharomyces cerevisiae, meiotic recombination is initiated by DNA double-strand breaks (DSBs). DSBs usually occur in intergenic regions that display nuclease hypersensitivity in digests of chromatin. DSBs are distributed nonuniformly across chromosomes; on chromosome III, DSBs are concentrated in two "hot" regions, one in each chromosome arm. DSBs occur rarely in regions within about 40 kb of each telomere and in an 80-kb region in the center of the chromosome, just to the right of the centromere. We used recombination reporter inserts containing arg4 mutant alleles to show that the "cold" properties of the central DSB-deficient region are imposed on DNA inserted in the region. Cold region inserts display DSB and recombination frequencies that are substantially less than those seen with similar inserts in flanking hot regions. This occurs without apparent change in chromatin structure, as the same pattern and level of DNase I hypersensitivity is seen in chromatin of hot and cold region inserts. These data are consistent with the suggestion that features of higher-order chromosome structure or chromosome dynamics act in a target sequence-independent manner to control where recombination events initiate during meiosis.  (+info)

(CA/GT)(n) microsatellites affect homologous recombination during yeast meiosis. (5/123)

One of the most common microsatellites in eukaryotes consists of tandem arrays of the dinucleotide GT. Although the study of the instability of such repetitive DNA has been extremely fruitful over the last decade, no biological function has been demonstrated for these sequences. We investigated the genetic behavior of a region of the yeast Saccharomyces cerevisiae genome containing a 39-CA/GT dinucleotide repeat sequence. When the microsatellite sequence was present at the ARG4 locus on homologous chromosomes, diploid cells undergoing meiosis generated an excess of tetrads containing a conversion of the region restricted to the region of the microsatellite close to the recombination-initiation double-strand break. Moreover, whereas the repetitive sequence had no effect on the frequency of single crossover, its presence strongly stimulated the formation of multiple crossovers. The combined data strongly suggest that numerous recombination events are restricted to the initiation side of the microsatellite as though progression of the strand exchange initiated at the ARG4 promoter locus was impaired by the repetitive sequence. This observation corroborates in vitro experiments that demonstrated that RecA-promoted strand exchange is inhibited by CA/GT dinucleotide tracts. Surprisingly, meiotic instability of the microsatellite was very high (>0.1 alterations per tetrad) in all the spores with parental and recombinant chromosomes.  (+info)

Guanidine hydrochloride induced reversible dissociation and denaturation of duck delta2-crystallin. (6/123)

The tetrameric delta2-crystallin from duck lens exhibits a reversible dissociation-denaturation process in solutions containing guanidine hydrochloride (GdnHCl). Sigmoidal or biphasic curves for the dissociation/denaturation processes, obtained using different methods of structural analysis, as a function of GdnHCl concentration were not coincidental with each other. delta2-crystallin in 0.91 M GdnHCl existed primarily as a monomer, which had no endogenous argininosuccinate lyase activity. After dilution of the GdnHCl-treated protein, the monomers reassociated into tetramers with concomitant recovery of enzyme activity. The sigmoidal recovery of enzyme activity demonstrates a cooperative hysteretic reactivation process. When the concentration of GdnHCl was higher than 1.2 M, various partially unfolded soluble forms of delta2-crystallin were produced from the dissociated monomers as shown by size-exclusion chromatography. The formation of a partially unfolded intermediate during the dissociation-denaturation process is proposed.  (+info)

Regulation of diaphragmatic nitric oxide synthase expression during hypobaric hypoxia. (7/123)

Nitric oxide (NO) is normally synthesized inside skeletal muscle fibers by both endothelial (eNOS) and neuronal (nNOS) nitric oxide synthases. In this study, we evaluated the influence of hypobaric hypoxia on the expression of NOS isoforms, argininosuccinate synthetase (AS), argininosuccinate lyase (AL), and manganese superoxide dismutase (Mn SOD) in the ventilatory muscles. Rats were exposed to hypobaric hypoxia ( approximately 95 mmHg) from birth for 60 days or 9-11 mo. Age-matched control groups of rats also were examined. Sixty days of hypoxia elicited approximately two- and ninefold increases in diaphragmatic eNOS and nNOS protein expression (evaluated by immunoblotting), respectively, and about a 50% rise in diaphragmatic NOS activity. In contrast, NOS activity and the expression of these proteins declined significantly in response to 9 mo of hypoxia. Hypoxia elicited no significant alterations in AS, AL and Mn SOD protein expression. Moreover, the inducible NOS (iNOS) was not detected in normoxic and hypoxic diaphragmatic samples. We conclude that diaphragmatic NOS expression and activity undergo significant adaptations to hypobaric hypoxia and that iNOS does not participate in this response.  (+info)

Accumulation of arginine precursors in Escherichia coli: effects on growth, enzyme repression, and application to the forward selection of arginine auxotrophs. (8/123)

The accumulation or ornithine, citrulline, and possibly acetylornithine by Escherichia coli K-12 arginineless mutants provided with acetylarginine as source of arginine causes severe growth inhibition. This occurs under conditions where comparable derivatives of E. coli W (Bollon and Vogel, 1973) show little or no growth inhibition. The same conditions, which have been reported to cause noncorrelative synthesis of acetylornithinase and argininosuccinase in E. coli W (Bollon and Vogel, 1973), do not alter the correlative pattern of enzyme synthesis observed in E. coli K-12. Moreover, previously reported effects of ornithine and citrulline on repression of the arginine regulon in E. coli W are not observed in the K-12 strains examined. The bearing of these observations on possible differences between the mechanism of enzyme repression operating in the two types of strains cannot yet be fully evaluated; it is, however, clear that considerable care should be exercised before extrapolating the results obtained with one type of strain to the other one. The particularly strong inhibition of acetylarginine utilization exerted by ornithine in E. coli K-12 allows the forward selection of several classes of arginine auxotrophs from strains deficient in carbamoylphosphate biosynthesis and thus capable of ornithine accumulation. Possible applications of this technique to the genetic analysis of the bipolar argECBH operon are discussed.  (+info)

Symptoms of argininosuccinic aciduria typically appear during infancy or early childhood and may include seizures, developmental delays, intellectual disability, vision loss, and poor muscle tone. Treatment for this condition involves a strict diet that limits the intake of certain amino acids, as well as medication to manage seizures and other symptoms. In some cases, liver transplantation may be necessary.

Argininosuccinic aciduria is diagnosed through a combination of clinical evaluation, laboratory tests, and genetic analysis. Treatment is usually coordinated by a multidisciplinary team of healthcare professionals, including pediatricians, neurologists, metabolism specialists, dietitians, and psychologists. With appropriate treatment and management, many individuals with argininosuccinic aciduria are able to lead active and fulfilling lives.

Overall, argininosuccinic aciduria is a rare and complex genetic disorder that requires careful management and monitoring to prevent complications and improve quality of life for affected individuals.

There are several types of inborn errors of amino acid metabolism, including:

1. Phenylketonuria (PKU): This is the most common inborn error of amino acid metabolism and is caused by a deficiency of the enzyme phenylalanine hydroxylase. This enzyme is needed to break down the amino acid phenylalanine, which is found in many protein-containing foods. If phenylalanine is not properly broken down, it can build up in the blood and brain and cause serious health problems.
2. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
3. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
4. Arginase deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid arginine. Arginine is important for the body's production of nitric oxide, a compound that helps to relax blood vessels and improve blood flow.
5. Citrullinemia: This is a rare genetic disorder that affects the breakdown of the amino acid citrulline. Citrulline is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
6. Tyrosinemia: This is a rare genetic disorder that affects the breakdown of the amino acid tyrosine. Tyrosine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
7. Maple syrup urine disease (MSUD): This is a rare genetic disorder that affects the breakdown of the amino acids leucine, isoleucine, and valine. These amino acids are important for growth and development, but if they are not properly broken down, they can build up in the blood and cause serious health problems.
8. PKU (phenylketonuria): This is a rare genetic disorder that affects the breakdown of the amino acid phenylalanine. Phenylalanine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
9. Methionine adenosyltransferase (MAT) deficiency: This is a rare genetic disorder that affects the breakdown of the amino acid methionine. Methionine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.
10. Homocystinuria: This is a rare genetic disorder that affects the breakdown of the amino acid homocysteine. Homocysteine is important for the body's production of proteins and other compounds, but if it is not properly broken down, it can build up in the blood and cause serious health problems.

It is important to note that these disorders are rare and affect a small percentage of the population. However, they can be serious and potentially life-threatening, so it is important to be aware of them and seek medical attention if symptoms persist or worsen over time.

Without enough citrulline synthase, citrulline builds up in the blood and urine, leading to a range of symptoms including seizures, developmental delays, and abnormal brain function. Citrullinemia can be diagnosed through a combination of blood tests and genetic analysis, and is typically treated with a diet that restricts protein intake and includes supplements to support the urea cycle. In some cases, medication or a liver transplant may also be necessary.

The prognosis for citrullinemia varies depending on the severity of the condition and the effectiveness of treatment. Some individuals with mild forms of the disorder may lead relatively normal lives with proper management, while those with more severe forms may experience significant cognitive and physical impairments. Early diagnosis and intervention are key to improving outcomes for individuals with citrullinemia.

Here are some key points to remember about citrullinemia:

* It is a rare genetic disorder that affects the urea cycle, leading to a build-up of citrulline in the blood and urine.
* Symptoms can include seizures, developmental delays, and abnormal brain function.
* Diagnosis is typically made through a combination of blood tests and genetic analysis.
* Treatment typically involves a protein-restricted diet and supplements to support the urea cycle.
* The prognosis varies depending on the severity of the condition and the effectiveness of treatment.

Overall, citrullinemia is a rare and complex disorder that requires careful management to prevent complications and improve outcomes for individuals affected by the condition.

The enzyme argininosuccinate lyase (EC 4.3.2.1, ASL, argininosuccinase; systematic name 2-(N ω-L-arginino)succinate arginine- ... Disorders Overview GeneReviews/NCBI/NIH/UW entry on Argininosuccinate Lyase Deficiency OMIM entries on Argininosuccinate Lyase ... lyase (fumarate-forming)) catalyzes the reversible breakdown of argininosuccinate: 2-(N ω-L-arginino)succinate = fumarate + L- ... Argininosuccinate lyase is an intermediate enzyme in the urea synthesis pathway and its function is imperative to the ...
Nagamani SC, Erez A, Lee B (May 2012). "Argininosuccinate lyase deficiency". Genetics in Medicine. 14 (5): 501-507. doi:10.1038 ...
"Gene sharing by delta-crystallin and argininosuccinate lyase". Proceedings of the National Academy of Sciences of the United ...
In humans, argininosuccinate lyase (ASL) is a homotetrameric enzyme that can undergo intragenic complementation. An ASL ... Turner MA, Simpson A, McInnes RR, Howell PL (August 1997). "Human argininosuccinate lyase: a structural basis for intragenic ... Yu B, Howell PL (October 2000). "Intragenic complementation and the structure and function of argininosuccinate lyase". ... "Mechanisms for intragenic complementation at the human argininosuccinate lyase locus". Biochemistry. 40 (51): 15581-15590. doi: ...
... the enzyme argininosuccinate lyase, involved in the conversion of arginino succinate to arginine within the urea cycle, is ... "Detection of neonatal argininosuccinate lyase deficiency by serum tandem mass spectrometry". J Inherit Metab Dis. 24 (3): 370-8 ...
Argininosuccinate synthetase and argininosuccinate lyase recycle citrulline, a byproduct of nitric oxide production, into ... Argininosuccinate synthase or synthetase (ASS; EC 6.3.4.5) is an enzyme that catalyzes the synthesis of argininosuccinate from ... In humans, argininosuccinate synthase is encoded by the ASS gene located on chromosome 9. ASS is responsible for the third step ... Expression of argininosuccinate synthetase in the intestines ceases after two to three years of life. It is thought that ...
... is a precursor to fumarate in the citric acid cycle via argininosuccinate lyase. Argininosuccinate ... The enzyme that catalyzes the reaction is argininosuccinate synthetase. ...
... in the urea cycle by the sequential action of the cytosolic enzymes argininosuccinate synthetase and argininosuccinate lyase. ... This is an energetically costly process, because for each molecule of argininosuccinate that is synthesized, one molecule of ...
Ants quickly lost the ability to synthesize arginine by losing the argininosuccinate lyase gene, the final step in the arginine ...
... argininosuccinate lyase), which catalyzes the formation of arginine and fumarate from argininosuccinate, the last step in the ... Fumarate lyase is a substrate of the lyase class of enzymes. It been shown to share a short conserved sequence around a ... Aspartate ammonia-lyase, EC 4.3.1.1 (aspartase), which catalyzes the reversible conversion of aspartate to fumarate and ammonia ... Delta-crystallin shares around 90% sequence identity with arginosuccinate lyase, showing that it is an example of a 'hijacked' ...
... and argininosuccinate lyase (ASL). Elia, Ilaria; Broekaert, Dorien; Christen, Stefan; Boon, Ruben; Radaelli, Enrico; Orth, ... is then synthesized from citrulline in the urea cycle by the sequential action of the cytosolic enzymes argininosuccinate ...
... former name of the Lymphology Association of North America Argininosuccinate lyase, an enzyme Arterial spin labelling, a ...
1 carbamoyl phosphate synthetase I OTC Ornithine transcarbamoylase ASS argininosuccinate synthetase ASL argininosuccinate lyase ... This reaction is ATP dependent and is catalyzed by argininosuccinate synthetase. Argininosuccinate undergoes cleavage by ... The reactions of the urea cycle 1 L-ornithine 2 carbamoyl phosphate 3 L-citrulline 4 argininosuccinate 5 fumarate 6 L-arginine ... Deficiency of argininosuccinic acid lyase) Argininemia (Deficiency of arginase) Hyperornithinemia, hyperammonemia, ...
... with those from birds and reptiles related to lactate dehydrogenase and argininosuccinate lyase, those of mammals to alcohol ...
... amidine-lyases MeSH D08.811.520.232.300.200 - adenylosuccinate lyase MeSH D08.811.520.232.300.400 - argininosuccinate lyase ... chondroitin lyases MeSH D08.811.520.241.700.350.500.500 - chondroitin abc lyase MeSH D08.811.520.241.700.512 - heparin lyase ... lyase MeSH D08.811.520.241.300 - hydro-lyases MeSH D08.811.520.241.300.050 - aconitate hydratase MeSH D08.811.520.241.300.050. ... oxo-acid-lyases MeSH D08.811.520.224.600.200 - anthranilate synthase MeSH D08.811.520.224.600.700 - isocitrate lyase MeSH ...
... argininosuccinate lyase EC 4.3.2.2: adenylosuccinate lyase EC 4.3.2.3: ureidoglycolate lyase EC 4.3.2.4: purine imidazole-ring ... pectin lyase EC 4.2.2.11: guluronate-specific alginate lyase EC 4.2.2.12: xanthan lyase EC 4.2.2.13: exo-(1→4)-α-D-glucan lyase ... chondroitin AC lyase EC 4.2.2.6: oligogalacturonide lyase EC 4.2.2.7: heparin lyase EC 4.2.2.8: heparin-sulfate lyase EC 4.2. ... alliin lyase EC 4.4.1.5: lactoylglutathione lyase EC 4.4.1.6: Now included in EC 4.4.1.13, cysteine-S-conjugate β-lyase EC 4.4. ...
It is also said that a synthase is a lyase (a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means ... including argininosuccinate synthetase) EC 6.4 includes ligases used to form carbon-carbon bonds EC 6.5 includes ligases used ...
EC 4.3.1 Phenylalanine ammonia-lyase (EC 4.3.1.24) Category:EC 4.4.1 Cystathionine gamma-lyase Cystathionine beta-lyase ... Argininosuccinate synthetase (EC 6.3.4.5) CTP synthase (EC 6.3.4.2) Pyruvate carboxylase (EC 6.4.1.1) Acetyl-CoA carboxylase ( ... 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. ...
The following reaction step, catalyzed by the enzyme O-acetyl serine (thiol) lyase, replaces the acetyl group of O-acetyl-L- ... Then, the enzymes citrulline and argininosuccinate convert ornithine to arginine. There are two distinct lysine biosynthetic ... SAICAR lyase removes the carbon skeleton of the added aspartate, leaving the amino group and forming 5-aminoimidazole-4- ...
... is a rare disease caused by a deficiency in argininosuccinate synthetase, an enzyme involved in excreting excess nitrogen from ... argininosuccinic acid lyase deficiency, ornithine transcarbamylase deficiency, arginase deficiency, and N-Acetylglutamate ...
... anemia due to Adenylosuccinate lyase deficiency Adie syndrome Adiposis dolorosa, aka Dercum's disease Adolescent benign focal ... II Arbovirosis Arc syndrome AREDYLD syndrome Argentine hemorrhagic fever Arginase deficiency Arginemia Argininosuccinate ...
... 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. ... argininosuccinate synthase EC 6.3.4.6: urea carboxylase EC 6.3.4.7: ribose-5-phosphate-ammonia ligase EC 6.3.4.8: ...
Protein target information for Argininosuccinate lyase (Streptococcus pneumoniae R6). Find diseases associated with this ...
inherited deficiency of argininosuccinate lyase * inherited carbamoyl phosphate synthetase deficiency * citrullinemia * ...
ASS = argininosuccinate synthetase;. ASL = argininosuccinate lyase;. ARG = arginase;. NAGS = N-acetylglutamate synthetase. ... argininosuccinate synthetase (ASS), or argininosuccinate lyase (ASL) deficiency. Because hyperchloremic acidosis may develop ... argininosuccinate synthetase (ASS), ornithine transcarbamylase (OTC), argininosuccinate lyase (ASL), or arginase (ARG). ... Abbreviations: CPS - carbamyl phosphate synthetase; OTC - ornithine transcarbamylase; ASS - argininosuccinate synthetase; ASL ...
ASS = argininosuccinate synthetase;. ASL = argininosuccinate lyase;. ARG = arginase;. NAGS = N-acetylglutamate synthetase ... argininosuccinate synthetase (ASS), or argininosuccinate lyase (ASL) deficiency. Because hyperchloremic acidosis may develop ... argininosuccinate synthetase (ASS), ornithine transcarbamylase (OTC), argininosuccinate lyase (ASL), or arginase (ARG). ...
ASL: argininosuccinate lyase. *ASNS: asparagine synthetase (glutamine-hydrolyzing). *ASPA: aspartoacylase. *ASPM: assembly ...
argininosuccinate lyase. This enzyme primarily participates in the urea cycle, a series of reactions that occur in liver cells ...
ASL: argininosuccinate lyase. *ASNS: asparagine synthetase (glutamine-hydrolyzing). *ASPA: aspartoacylase. *ASPM: assembly ...
Argininosuccinate lyase. 4.3.2.1. P04424. Carbamoyl-phosphate synthase deficiency. CPS. Other. 62522004 ...
Argininosuccinate Lyase Deficiency. Sandesh C. Sreenath Nagamani, Ayelet Erez, Brendan Lee. Genet Med. Author manuscript; ...
Argininosuccinate lyase deficiency. Nagamani SC, Erez A, Lee B. Nagamani SC, et al. Genet Med. 2012 May;14(5):501-7. doi: ...
Argininosuccinate Lyase/chemistry; Argininosuccinate Lyase/metabolism; Argininosuccinate Synthase/chemistry; Argininosuccinate ... and argininosuccinate lyase (ASL). Prior work has shown that ASL is present in a NO synthetic complex containing hsp90 and ... pathway in which l-citrulline is recycled to l-arginine by utilizing two important urea cycle enzymes argininosuccinate ...
ASA deficiency; ASL deficiency; Argininosuccinase deficiency; Argininosuccinatelyase deficiency; Argininosuccinic acid lyase ... deficiencyASA deficiency; ASL deficiency; Argininosuccinase deficiency; Argininosuccinatelyase deficiency; Argininosuccinic ...
Project Title: Argininosuccinate Lyase Is an Essential Regulator of Systemic Nitric Oxide Production. Grant ID: R01-GM-090310 ... This project will study a new way that NO production may be regulated in the body by the chemical argininosuccinate lyase (ASL ...
Gene sharing by delta-crystallin and argininosuccinate lyase. Piatigorsky, J.. * Enzyme/crystallins: gene sharing as an ... USA, 114, nate lyase. Proc. Natl. Acad. Sci. USA, 85, 3479-3483. E426-E435. ... USA, 114, nate lyase. Proc. Natl. Acad. Sci. USA, 85, 3479-3483. E426-E435. http://www.deepdyve.com/assets/images/DeepDyve-Logo ...
Argininosuccinate lyase drives activation of mutant TERT promoter in glioblastomas.. Shi Z; Ge X; Li M; Yin J; Wang X; Zhang J ...
Amidine-Lyases [D08.811.520.232.300] * Adenylosuccinate Lyase [D08.811.520.232.300.200] * Argininosuccinate Lyase [D08.811. ... N-(L-Argininosuccinate) arginine-lyase. Previous Indexing. Arginine (1973-1974). Lyases (1973-1974). Succinates (1973-1974). ... Argininosuccinate Lyase Preferred Term Term UI T003396. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1975). ... Argininosuccinate Lyase Preferred Concept UI. M0001687. Registry Number. EC 4.3.2.1. Related Numbers. 9027-34-3. Scope Note. An ...
... due to the silencing of argininosuccinate synthase 1 (ASS1), is a common metabolic vulnerability in cancer, known as arginine ... and argininosuccinate lyase in the urea cycle8, and metabolized by arginase 1 to produce urea and ornithine. Ornithine is a ... ATP-citrate lyase links cellular metabolism to histone acetylation. Science 324, 1076-1080 (2009). ... Defective arginine synthesis, due to the silencing of argininosuccinate synthase 1 (ASS1), is a common metabolic vulnerability ...
... and argininosuccinate lyase (ASL) in the gut and other tissues. However, arginine availability is balanced by arginine ... production from gut-derived citrulline and the action of the rate-limiting enzymes argininosuccinate synthase (ASS) ...
It is endogenously synthesized from citrulline via argininosuccinate synthase and argininosuccinate lyase [33,34], and it is ...
Additional galU genes were found adjacent to the gene argH encoding argininosuccinate lyase in the sequenced genomes from ...
... argininosuccinate lyase. b SCFA-producing metabolic pathways were constructed using the identified KOs. GTP, ... pyruvate formate-lyase; PFOR, pyruvate, ferredoxin oxidoreductase; ACS, acetyl-CoA synthase; ACK, acetate kinase; ACAT, acetyl- ...
Argininosuccinate Lyase - Preferred Concept UI. M0001687. Scope note. An enzyme of the urea cycle which splits ... An enzyme of the urea cycle which splits argininosuccinate to fumarate plus arginine. Its absence leads to the metabolic ... argininosuccinate to fumarate plus arginine. Its absence leads to the metabolic disease ARGININOSUCCINIC ACIDURIA in man. EC ...
Amidine-Lyases [D08.811.520.232.300] * Adenylosuccinate Lyase [D08.811.520.232.300.200] * Argininosuccinate Lyase [D08.811. ... N-(L-Argininosuccinate) arginine-lyase. Previous Indexing. Arginine (1973-1974). Lyases (1973-1974). Succinates (1973-1974). ... Argininosuccinate Lyase Preferred Term Term UI T003396. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1975). ... Argininosuccinate Lyase Preferred Concept UI. M0001687. Registry Number. EC 4.3.2.1. Related Numbers. 9027-34-3. Scope Note. An ...
argininosuccinate lyase 59.21 470 aa 561 1.0000000000000001e-159 Prochlorococcus marinus str. MIT 9303 Bacteria n/a normal 1 - ...
argininosuccinate lyase 220, 251. DVU1095. argG. argininosuccinate synthase 220, 262. DVU1408. hypothetical protein DVU1408 63 ...
Argininosuccinate Lyase 100% * Argininosuccinate Synthase 84% * Proteasome Endopeptidase Complex 60% * Ubiquitin 58% ...
... argininosuccinate synthetase (ASS), or argininosuccinate lyase (ASL) deficiency. Because hyperchloremic acidosis may develop ... argininosuccinate synthetase (ASS), ornithine transcarbamylase (OTC), argininosuccinate lyase (ASL), or arginase (ARG). ... Abbreviations: CPS - carbamyl phosphate synthetase; OTC - ornithine transcarbamylase; ASS -argininosuccinate synthetase; ASL- ... HMG CoA lyase deficiency (1 episode), non-ketotic hyperglycinemia (1 episode), suspected fatty acid oxidation deficiency (1 ...
  • Defective arginine synthesis, due to the silencing of argininosuccinate synthase 1 (ASS1), is a common metabolic vulnerability in cancer, known as arginine auxotrophy. (nature.com)
  • For instance, in non-cancerous cells arginine is synthesized in cells from citrulline via argininosuccinate synthase 1 (ASS1) and argininosuccinate lyase in the urea cycle 8 , and metabolized by arginase 1 to produce urea and ornithine. (nature.com)
  • Arginine availability is dependent on its "de novo" production from gut-derived citrulline and the action of the rate-limiting enzymes argininosuccinate synthase (ASS) and argininosuccinate lyase (ASL) in the gut and other tissues. (usda.gov)
  • Argininosuccinate synthase (Ass1) and argininosuccinate lyase (Asl) are the key enzyme for L-Arginine (L-Arg) biosynthesis. (bvsalud.org)
  • Cortisol treatment increased plasma cortisol concentration, mitochondrial proline oxidase and N-acetylglutamate synthase activities, cytosolic argininosuccinate lyase activity, and the intracellular concentrations of N-acetylglutamate and carbamoyl phosphate for citrulline and arginine synthesis. (utmb.edu)
  • each is referred to by the initials of the missing enzyme: CPS1 (Carbamoyl Phosphate Synthetase), NAGS (N-Acetylglutamate Synthetase), OTC Deficiency (Ornithine Transcarbamylase), AS (Argininosuccinic Acid Synthetase (Citrullinemia)), ASL (Argininosuccinate Lyase (Argininosuccinic Aciduria)), and AG (Arginase). (rohtaknewsmagazine.net)
  • An enzyme of the urea cycle which splits argininosuccinate to fumarate plus arginine. (bvsalud.org)
  • Low prevalence of argininosuccinate lyase deficiency among inherited urea cycle disorders in Korea. (cdc.gov)
  • Feb 2, 2018 - human argininosuccinate lyase enzyme encapsulated into lipid nanoparticles was used in addition to ammonia scavenger products, currently authorized for the treatment of the condition. (pdfkul.com)