Aspartate ammonia ligase. Medical search

An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2.

An enzyme that catalyzes the conversion of aspartic acid to ammonia and fumaric acid in plants and some microorganisms. EC 4.3.1.1.

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.

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.

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.

An enzyme that catalyzes the conversion of linear RNA to a circular form by the transfer of the 5'-phosphate to the 3'-hydroxyl terminus. It also catalyzes the covalent joining of two polyribonucleotides in phosphodiester linkage. EC 6.5.1.3.

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.

A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.

Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD).

A family of gram-positive bacteria in the order Lactobacillales. Lactic acid is the main product of their carbohydrate metabolism.

An order of gram-positive bacteria in the class Bacilli, that have the ability to ferment sugars to lactic acid. They are widespread in nature and commonly used to produce fermented foods.

An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.

The systematic study of the complete DNA sequences (GENOME) of organisms.

A plasma membrane exchange glycoprotein transporter that functions in intracellular pH regulation, cell volume regulation, and cellular response to many different hormones and mitogens.

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.

The genetic complement of a BACTERIA as represented in its DNA.

A species of gram-negative bacteria causing chronic respiratory disease in POULTRY.

A genus of gram-negative, mostly facultatively anaerobic bacteria in the family MYCOPLASMATACEAE. The cells are bounded by a PLASMA MEMBRANE and lack a true CELL WALL. Its organisms are pathogens found on the MUCOUS MEMBRANES of humans, ANIMALS, and BIRDS.

All of the divisions of the natural sciences dealing with the various aspects of the phenomena of life and vital processes. The concept includes anatomy and physiology, biochemistry and biophysics, and the biology of animals, plants, and microorganisms. It should be differentiated from BIOLOGY, one of its subdivisions, concerned specifically with the origin and life processes of living organisms.

A publication issued at stated, more or less regular, intervals.

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

Lists of persons or organizations, systematically arranged, usually in alphabetic or classed order, giving address, affiliations, etc., for individuals, and giving address, officers, functions, and similar data for organizations. (ALA Glossary of Library and Information Science, 1983)

A genus of gram-negative, anaerobic, rod-shaped bacteria. Its organisms are normal inhabitants of the oral, respiratory, intestinal, and urogenital cavities of humans, animals, and insects. Some species may be pathogenic.

Gram-negative bacteria occurring in the lower intestinal tracts of man and other animals. It is the most common species of anaerobic bacteria isolated from human soft tissue infections.

Infections with bacteria of the genus BACTEROIDES.

A genus of gram-negative, anaerobic, nonsporeforming, nonmotile rods. Organisms of this genus had originally been classified as members of the BACTEROIDES genus but overwhelming biochemical and chemical findings in 1990 indicated the need to separate them from other Bacteroides species, and hence, this new genus was established.

Nonsusceptibility of bacteria to the action of TETRACYCLINE which inhibits aminoacyl-tRNA binding to the 30S ribosomal subunit during protein synthesis.

A parasexual process in BACTERIA; ALGAE; FUNGI; and ciliate EUKARYOTA for achieving exchange of chromosome material during fusion of two cells. In bacteria, this is a uni-directional transfer of genetic material; in protozoa it is a bi-directional exchange. In algae and fungi, it is a form of sexual reproduction, with the union of male and female gametes.

A class of plasmids that transfer antibiotic resistance from one bacterium to another by conjugation.

Cell surface proteins that bind lipoproteins with high affinity. Lipoprotein receptors in the liver and peripheral tissues mediate the regulation of plasma and cellular cholesterol metabolism and concentration. The receptors generally recognize the apolipoproteins of the lipoprotein complex, and binding is often a trigger for endocytosis.

A class of lipoproteins of small size (4-13 nm) and dense (greater than 1.063 g/ml) particles. HDL lipoproteins, synthesized in the liver without a lipid core, accumulate cholesterol esters from peripheral tissues and transport them to the liver for re-utilization or elimination from the body (the reverse cholesterol transport). Their major protein component is APOLIPOPROTEIN A-I. HDL also shuttle APOLIPOPROTEINS C and APOLIPOPROTEINS E to and from triglyceride-rich lipoproteins during their catabolism. HDL plasma level has been inversely correlated with the risk of cardiovascular diseases.

A membrane-bound or cytosolic enzyme that catalyzes the synthesis of CYCLIC ADP-RIBOSE (cADPR) from nicotinamide adenine dinucleotide (NAD). This enzyme generally catalyzes the hydrolysis of cADPR to ADP-RIBOSE, as well, and sometimes the synthesis of cyclic ADP-ribose 2' phosphate (2'-P-cADPR) from NADP.

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

A class of lipoproteins of small size (18-25 nm) and light (1.019-1.063 g/ml) particles with a core composed mainly of CHOLESTEROL ESTERS and smaller amounts of TRIGLYCERIDES. The surface monolayer consists mostly of PHOSPHOLIPIDS, a single copy of APOLIPOPROTEIN B-100, and free cholesterol molecules. The main LDL function is to transport cholesterol and cholesterol esters to extrahepatic tissues.

Lipid-protein complexes involved in the transportation and metabolism of lipids in the body. They are spherical particles consisting of a hydrophobic core of TRIGLYCERIDES and CHOLESTEROL ESTERS surrounded by a layer of hydrophilic free CHOLESTEROL; PHOSPHOLIPIDS; and APOLIPOPROTEINS. Lipoproteins are classified by their varying buoyant density and sizes.

Receptors on the plasma membrane of nonhepatic cells that specifically bind LDL. The receptors are localized in specialized regions called coated pits. Hypercholesteremia is caused by an allelic genetic defect of three types: 1, receptors do not bind to LDL; 2, there is reduced binding of LDL; and 3, there is normal binding but no internalization of LDL. In consequence, entry of cholesterol esters into the cell is impaired and the intracellular feedback by cholesterol on 3-hydroxy-3-methylglutaryl CoA reductase is lacking.

Common name for the largest birds in the order PASSERIFORMES, family Corvidae. These omnivorous black birds comprise most of the species in the genus Corvus, along with ravens and jackdaws (which are often also referred to as crows).

The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)

Copies of a work or document distributed to the public by sale, rental, lease, or lending. (From ALA Glossary of Library and Information Science, 1983, p181)

State plans prepared by the State Health Planning and Development Agencies which are made up from plans submitted by the Health Systems Agencies and subject to review and revision by the Statewide Health Coordinating Council.

"The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.

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.

An essential amino acid that is physiologically active in the L-form.

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.

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 cell line derived from cultured tumor cells.

A family of hoofed MAMMALS consisting of HORSES, donkeys, and zebras. Members of this family are strict herbivores and can be classified as either browsers or grazers depending on how they feed.

Therapeutic approach tailoring therapy for genetically defined subgroups of patients.

Organized systems for providing comprehensive prepaid health care that have five basic attributes: (1) provide care in a defined geographic area; (2) provide or ensure delivery of an agreed-upon set of basic and supplemental health maintenance and treatment services; (3) provide care to a voluntarily enrolled group of persons; (4) require their enrollees to use the services of designated providers; and (5) receive reimbursement through a predetermined, fixed, periodic prepayment made by the enrollee without regard to the degree of services provided. (From Facts on File Dictionary of Health Care Management, 1988)

The study of the patterns of ridges of the skin of the fingers, palms, toes, and soles.

A technique for identifying individuals of a species that is based on the uniqueness of their DNA sequence. Uniqueness is determined by identifying which combination of allelic variations occur in the individual at a statistically relevant number of different loci. In forensic studies, RESTRICTION FRAGMENT LENGTH POLYMORPHISM of multiple, highly polymorphic VNTR LOCI or MICROSATELLITE REPEAT loci are analyzed. The number of loci used for the profile depends on the ALLELE FREQUENCY in the population.

Critical and exhaustive investigation or experimentation, having for its aim the discovery of new facts and their correct interpretation, the revision of accepted conclusions, theories, or laws in the light of newly discovered facts, or the practical application of such new or revised conclusions, theories, or laws. (Webster, 3d ed)

An activity in which the organism plunges into water. It includes scuba and bell diving. Diving as natural behavior of animals goes here, as well as diving in decompression experiments with humans or animals.

L-Asparagine synthetase in serum as a marker for neoplasia. (1/128)

L-Asparagine synthetase appears in serum approximately 7 days after the s.c. implantation of 1 X 10(5) cells of Leukemia 5178Y/AR (resistant to L-asparaginase) and increases in activity as the neoplasm grows and metastasizes. The principal source of the enzyme is the primary tumor. After intravranial inoculation of tumor, the rate of leakage of the enzyme is more pronounced than when the subcutaneous, intramuscular, or intraperitoneal routes are used. 1-(2-Chloroethyl)-3-cyclohexyl-1-nitrosourea (NSC 79037), a nitro-sourea effective in the palliation of L5178Y/AR, temporarily halts the influx of enzyme into the blood stream, as does surgical excision of the s.c. tumor nodules. Treatment of mice with L-asparaginase within 24 hr of inoculation of the tumor markedly augments both tumor growth and the rate of penetration of L-asparagine synthetase into the circulation. Several other L-asparagine synthetase into the circulation. Several other L-asparaginase-resistant tumors also were found to spill L-asparagine synthetase into the serum, but the correlation between this phenomenon and the specific activity of the enzyme in homogenates of the tumor was imperfect. (+info)

Transcriptional regulation of the human asparagine synthetase gene by carbohydrate availability. (2/128)

Transcription of the asparagine synthetase (AS) gene is induced by amino acid deprivation. The present data illustrate that this gene is also under transcriptional control by carbohydrate availability. Incubation of human HepG2 hepatoma cells in glucose-free medium resulted in an increased AS mRNA content, reaching a maximum of about 14-fold over control cells after approx. 12 h. Extracellular glucose caused the repression of the content of AS mRNA in a concentration-dependent manner, with a k1/2 (concentration causing a half-maximal repression) of 1 mM. Fructose, galactose, mannose, 2-deoxyglucose and xylitol were found to maintain the mRNA content of both AS and the glucose-regulated protein GRP78 in a state of repression, whereas 3-O-methylglucose did not. Incubation in either histidine-free or glucose-free medium also resulted in adaptive regulation of the AS gene in BNL-CL.2 mouse hepatocytes, rat C6 glioma cells and human MOLT4 lymphocytes, in addition to HepG2 cells. In contrast, the steady-state mRNA content of GRP78 was unaffected by amino acid availability. Transient transfection assays using a reporter gene construct documented that glucose deprivation increases AS gene transcription via elements within the proximal 3 kbp of the AS promoter. These results illustrate that human AS gene transcription is induced following glucose limitation of the cells. (+info)

RT-PCR cloning, characterization and mRNA expression analysis of a cDNA encoding a type II asparagine synthetase in common bean. (3/128)

Following a RT-PCR strategy based on the design of degenerate oligonucleotides resembling conserved domains of asparagine synthetase (AS; EC 6.3.5.4), we isolated a 2 kb cDNA clone (PVAS2) from root tissue of the common bean (Phaseolus vulgaris). PVAS2 encodes a protein of 584 amino acids with a predicted relative molecular mass of 65810 Da, an isoelectric point of 6.4, and a net charge of -7.2 at pH 7.0. The amino acid sequence of the protein encoded by PVAS2 is very similar to that encoded by the soybean SAS2 asparagine synthetase gene. The amino-terminal residues of the predicted PVAS2 protein are identical to the amino acids that constitute the glutamine-binding (GAT) domain of AS from other plant species, which suggests that the PVAS2 cDNA encodes a type II glutamine-dependent form of asparagine synthetase. Southern blot analysis indicates that the common bean AS is part of a small family composed of at least two genes. Expression analysis by Northern blot revealed that the PVAS2 transcript accumulates to a high level in roots and, to a lesser extent, in nodules and developing pods. Accumulation of the PVAS2 transcript in the root seems to be negatively regulated by light and sucrose, and positively regulated by nitrate. (+info)

Activation of the unfolded protein response pathway induces human asparagine synthetase gene expression. (4/128)

The gene for the amino acid biosynthetic activity asparagine synthetase (AS) is induced by both amino acid and glucose deprivation of cells. The data reported here document that the human AS gene is induced following activation of the Unfolded Response Pathway (UPR), also known as the Endoplasmic Reticulum Stress Response (ERSR) in mammals. Increased AS transcription occurs in response to glucose deprivation, tunicamycin, or azetidine-2-carboxylate, all known to activate the UPR/ERSR pathway. Previously identified ERSR target genes contain multiple copies of a single highly conserved cis-element. In contrast, the human AS gene does not contain the ERSR element, as it has been described for other responsive genes. Instead, AS induction requires an Sp1-like sequence, a sequence previously shown to be associated with amino acid control of transcription, and possibly, a third region containing no consensus sequences for known transcription factors. Oligonucleotides covering each of these regions form DNA-protein complexes in vitro, and for some the amount of these complexes is greater when nuclear extracts from glucose-starved cells are tested. These results document that a wider range of metabolic activities are activated by the UPR/ERSR pathway than previously recognized and that genomic elements other than those already described can serve to enhance transcription of specific target genes. (+info)

Using genomic information to investigate the function of ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis. (5/128)

The gene thiI encodes a protein (ThiI) that plays a role in the transfer of sulfur from cysteine to both thiamin and 4-thiouridine, but the reaction catalyzed by ThiI remains undetermined. Based upon sequence alignments, ThiI shares a unique "P-loop" motif with the PPi synthetase family, four enzymes that catalyze adenylation and subsequent substitution of carbonyl oxygens. To test whether or not this motif is critical for ThiI function, the Asp in the motif was converted to Ala (D189A), and a screen for in vivo 4-thiouridine production revealed the altered enzyme to be inactive. Further scrutiny of sequence data and the crystal structures of two members of the PPi synthetase family implicated Lys321 in the proposed adenylation function of ThiI, and the critical nature of Lys321 has been demonstrated by site-directed mutagenesis and genetic screening. Our results, then, indicate that ThiI catalyzes the adenylation of a substrate at the expense of ATP, a narrowing of possible reactions that provides a strong new basis for deducing the early steps in the transfer of sulfur from cysteine to both thiamin and 4-thiouridine. (+info)

A mutation in the Corynebacterium glutamicum ltsA gene causes susceptibility to lysozyme, temperature-sensitive growth, and L-glutamate production. (6/128)

The Corynebacterium glutamicum mutant KY9714, originally isolated as a lysozyme-sensitive mutant, does not grow at 37 degrees C. Complementation tests and DNA sequencing analysis revealed that a mutation in a single gene of 1,920 bp, ltsA (lysozyme and temperature sensitive), was responsible for its lysozyme sensitivity and temperature sensitivity. The ltsA gene encodes a protein homologous to the glutamine-dependent asparagine synthetases of various organisms, but it could not rescue the asparagine auxotrophy of an Escherichia coli asnA asnB double mutant. Replacement of the N-terminal Cys residue (which is conserved in glutamine-dependent amidotransferases and is essential for enzyme activity) by an Ala residue resulted in the loss of complementation in C. glutamicum. The mutant ltsA gene has an amber mutation, and the disruption of the ltsA gene caused lysozyme and temperature sensitivity similar to that in the KY9714 mutant. L-Glutamate production was induced by elevating growth temperature in the disruptant. These results indicate that the ltsA gene encodes a novel glutamine-dependent amidotransferase that is involved in the mechanisms of formation of rigid cell wall structure and in the L-glutamate production of C. glutamicum. (+info)

Evidence for multiple signaling pathways in the regulation of gene expression by amino acids in human cell lines. (7/128)

In mammals, plasma concentrations of amino acids (AA) are affected by nutritional or pathologic conditions. Alterations in AA profiles have been reported as a result of a deficiency of any one of the essential AA, a dietary imbalance of AA or an insufficient intake of protein. In recent years, evidence has accumulated that AA availability regulates the expression of several genes involved in the regulation of a number of cellular functions or AA metabolism. Nevertheless, the molecular mechanisms involved in the AA regulation of mammalian gene expression are limited, particularly the signaling pathways mediating the AA response. This work provides a better understanding of the signaling pathways involved in the AA control of gene expression. We studied the expression of C/EBP homologous protein (CHOP) and asparagine synthetase (AS) in response to deprivation of a single AA and investigated the possible link between protein synthesis inhibition due to amino acid limitation and gene expression. We have shown the following: 1) several mechanisms are involved in the AA control of gene expression. When omitted from the culture medium, each AA can activate one (or several) specific signaling pathways leading to the regulation of one specific pattern of genes. 2) AA limitation by itself can induce gene expression independently of a cellular stress due to protein synthesis inhibition. Together, these results suggest that AA control of gene expression involves several specific mechanisms by which one AA (or one group of AA) can activate one signaling pathway and thus alter one specific pattern of gene expression. (+info)

Activation of the human asparagine synthetase gene by the amino acid response and the endoplasmic reticulum stress response pathways occurs by common genomic elements. (8/128)

The human asparagine synthetase (AS) gene is transcriptionally regulated by amino acid deprivation (amino acid response, AAR) and the endoplasmic reticulum stress response (ERSR), also known as the unfolded protein response pathway. The results reported here document the novel observation that induction of the AS gene by the AAR and ERSR pathways occurs via the same set of genomic elements. Data supporting this conclusion include transient transfection of AS promoter/reporter gene constructs that illustrate that the transcriptional control elements used by both pathways are contained with nucleotides -111 to -34 of the AS promoter. In vivo footprinting analysis of this region identified six specific protein-binding sites. Within two of these sites, altered footprinting was observed following amino acid or glucose deprivation, but the patterns were identical for both the AAR and the ERSR pathway. Site-directed mutation of individual nucleotides within these two binding sites confirmed their importance for regulated transcription, and none of the mutations resulted in loss of response of only one pathway. Neither of these two sites corresponds to a recently identified ERSR cis-element, nor do they contain consensus sequences for known transcription factors. Collectively, the data document that there are at least two independent transcriptional mechanisms for gene activation by the ERSR pathway, one of which terminates at the same genomic elements used by the AAR pathway. (+info)

... (or aspartate-ammonia ligase) is a chiefly cytoplasmic enzyme that generates asparagine from aspartate. ... This domain is responsible for the binding of both Mg2+ATP and aspartate. These two active sites are connected by a tunnel ... The human glutamine-dependent AS is encoded by a single gene located in region q21.3 on chromosome 7. The lack of ammonia- ... Thus, after being released in, and channeled from, the glutaminase site, the ammonia molecule attacks the bound βAspAMP 1 to ...

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

... aspartate-ammonia ligase MeSH D08.811.464.259.200.600 - glutamate-ammonia ligase MeSH D08.811.464.259.300 - argininosuccinate ... alanine-tRNA ligase MeSH D08.811.464.263.200.100 - arginine-tRNA ligase MeSH D08.811.464.263.200.150 - aspartate-tRNA ligase ... ammonia-lyases MeSH D08.811.520.232.400.200 - aspartate ammonia-lyase MeSH D08.811.520.232.400.350 - ethanolamine ammonia-lyase ... valine-tRNA ligase MeSH D08.811.464.267.500 - coenzyme a ligases MeSH D08.811.464.267.500.200 - acetate-coa ligase MeSH D08.811 ...

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

In enzymology, an aspartate-ammonia ligase (EC 6.3.1.1) is an enzyme that catalyzes the chemical reaction ATP + L-aspartate + ... ligases (amide synthases). The systematic name of this enzyme class is L-aspartate:ammonia ligase (AMP-forming). Other names in ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... Webster GC, Varner JE (1955). "Aspartate metabolism and asparagine synthesis in plant systems". J. Biol. Chem. 215: 91-99. PMID ...

https://en.wikipedia.org/wiki/Aspartate—ammonia_ligase

... an aspartate-ammonia ligase (ADP-forming) (EC 6.3.1.4) is an enzyme that catalyzes the chemical reaction ATP + L-aspartate + ... ligases (amide synthases). The systematic name of this enzyme class is L-aspartate:ammonia ligase (ADP-forming). Other names in ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... L-aspartate, and NH3, whereas its 3 products are ADP, phosphate, and L-asparagine. ...

https://en.wikipedia.org/wiki/Aspartate—ammonia_ligase_(ADP-forming)

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... In enzymology, a D-aspartate ligase (EC 6.3.1.12) is an enzyme that catalyzes the chemical reaction ATP + D-aspartate + [beta- ... n ligase (ADP-forming). Other names in common use include Aslfm, UDP-MurNAc-pentapeptide:D-aspartate ligase, and D-aspartic ... Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL (2006). "Aslfm, the D-aspartate ligase responsible for the addition of ...

https://en.wikipedia.org/wiki/D-aspartate_ligase

... aspartate-ammonia ligase EC 6.3.1.2: glutamate-ammonia ligase EC 6.3.1.3: Now EC 6.3.4.13 EC 6.3.1.4: aspartate-ammonia ligase ... valine-tRNA ligase EC 6.1.1.10: methionine-tRNA ligase EC 6.1.1.11: serine-tRNA ligase EC 6.1.1.12: aspartate-tRNA ligase EC ... histidine-tRNA ligase EC 6.1.1.22: asparagine-tRNA ligase EC 6.1.1.23: aspartate-tRNAAsn ligase EC 6.1.1.24: glutamate-tRNAGln ... diphthine-ammonia ligase EC 6.3.2.1: pantoate-b-alanine ligase EC 6.3.2.2: glutamate-cysteine ligase EC 6.3.2.3: glutathione ...

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

... asparagine synthetase catalyzes the addition of nitrogen from glutamine or soluble ammonia to aspartate to yield asparagine. ... Okazaki fragments are covalently joined by DNA ligase to form a continuous strand. Then, to complete DNA replication, RNA ... The biosynthesis of aspartate is a one step reaction that is catalyzed by a single enzyme. The enzyme aspartate ... The aspartate family of amino acids includes: threonine, lysine, methionine, isoleucine, and aspartate. Lysine and isoleucine ...

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

... aspartate ammonia-lyase EC 4.3.1.2: methylaspartate ammonia-lyase EC 4.3.1.3: histidine ammonia-lyase EC 4.3.1.4: ... heme ligase "Enzyme: 4.1.2.8". Kyoto Encyclopedia of Genes and Genomes. Retrieved 2017-04-07. European Bioinformatics Institute ... b-alanyl-CoA ammonia-lyase EC 4.3.1.7: ethanolamine ammonia-lyase EC 4.3.1.8: now EC 2.5.1.61 EC 4.3.1.9: glucosaminate ammonia ... threo-3-hydroxyaspartate ammonia-lyase EC 4.3.1.17: L-serine ammonia-lyase EC 4.3.1.18: D-serine ammonia-lyase EC 4.3.1.19: ...

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

... glutamate-ammonia-ligase) adenylyltransferase EC 2.7.7.43: N-acylneuraminate cytidylyltransferase EC 2.7.7.44: glucuronate-1- ... aspartate kinase EC 2.7.2.5: now EC 6.3.4.16 EC 2.7.2.6: formate kinase EC 2.7.2.7: butyrate kinase EC 2.7.2.8: acetylglutamate ... ammonia kinase EC 2.7.3.9: Phosphoenolpyruvate-protein phosphotransferase EC 2.7.3.10: agmatine kinase EC 2.7.3.11: now EC 2.7. ... aspartate transaminase EC 2.6.1.2: alanine transaminase EC 2.6.1.3: cysteine transaminase EC 2.6.1.4: glycine transaminase EC ...

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

CYP2D6, dopamine β-hydroxylase (DBH), flavin-containing monooxygenase 3 (FMO3), butyrate-CoA ligase (XM-ligase), and glycine N- ... The review indicated that magnesium L-aspartate and magnesium chloride produce significant changes in addictive behavior; other ... Another method is the reaction of phenylacetone with ammonia, producing an imine intermediate that is reduced to the primary ... This reaction is catalyzed by the HXM-A and HXM-B medium-chain acid:CoA ligases and requires energy in the form of ATP. ... The ...

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

Glutarate-CoA ligase EC 6.2.1.7: Cholate-CoA ligase EC 6.2.1.8: Oxalate-CoA ligase EC 6.2.1.9: Malate-CoA ligase EC 6.2.1.10: ... 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. ... EC 4.3.1 Phenylalanine ammonia-lyase (EC 4.3.1.24) Category:EC 4.4.1 Cystathionine gamma-lyase Cystathionine beta-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: o- ...

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

Reducing equivalents from the cytoplasm can be imported via the malate-aspartate shuttle system of antiporter proteins or feed ... For example, mitochondria in liver cells contain enzymes that allow them to detoxify ammonia, a waste product of protein ... kynurenine hydroxylase and fatty acid Co-A ligase. Disruption of the outer membrane permits proteins in the intermembrane space ...

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

Carboxy phosphate reacts with ammonia to give carbamic acid. In turn, carbamic acid reacts with a second ATP to give carbamoyl ... Aspartate. *Cysteine. *D-alanine-poly(phosphoribitol) ligase. *Glutamate. *Glutamine. *Glycine. *Histidine. *Isoleucine ... The small subunit contains the glutamine binding site and catalyses the hydrolysis of glutamine to glutamate and ammonia, which ... The carboxylphosphate then reacts with ammonia to form carbamic acid, releasing inorganic phosphate. ...

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

In the first active site, a cysteine triad hydrolyses a glutamine substrate to release free ammonia. The ammonia then diffuses ... The aspartate is hydrogen bonded to the histidine, increasing the pKa of its imidazole nitrogen from 7 to around 12. This ... 1994). "A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues". Science. 266 (5183 ... Two amino acids have acidic side chains at physiological pH (aspartate or glutamate) and so are the most commonly used for this ...

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

... glutamate-ammonia ligase) hydrolase EC 3.1.4.16: 2',3'-cyclic-nucleotide 2'-phosphodiesterase EC 3.1.4.17: 3',5'-cyclic- ... The enzyme is not a serine protease, as thought previously, but an aspartate protease EC 3.4.21.88: Repressor LexA EC 3.4.21.89 ... N-acyl-D-aspartate deacylase EC 3.5.1.84: biuret amidohydrolase EC 3.5.1.85: (S)-N-acetyl-1-phenylethylamine hydrolase EC 3.5. ... aspartate carboxypeptidase EC 3.4.17.6: alanine carboxypeptidase EC 3.4.17.7: Transferred entry: acylmuramoyl-alanine ...

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

... belongs to the class V group of aspartate aminotransferase superfamily of structurally homologous pyridoxal 5'- ...

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

... is an oxidase that is the rate-limiting enzyme for controlling the production of melanin. The enzyme is mainly involved in two distinct reactions of melanin synthesis otherwise known as the Raper Mason pathway. Firstly, the hydroxylation of a monophenol and secondly, the conversion of an o-diphenol to the corresponding o-quinone. o-Quinone undergoes several reactions to eventually form melanin.[5] Tyrosinase is a copper-containing enzyme present in plant and animal tissues that catalyzes the production of melanin and other pigments from tyrosine by oxidation. It is found inside melanosomes which are synthesized in the skin melanocytes. In humans, the tyrosinase enzyme is encoded by the TYR gene.[6] ...

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

... a cysteine triad hydrolyses a glutamine substrate to release free ammonia. The ammonia then diffuses though an internal tunnel ... The aspartate is hydrogen bonded to the histidine, increasing the pKa of its imidazole nitrogen from 7 to around 12. This ... 1994). "A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues". Science. 266 (5183 ... The triad consists of an aspartate (acid), histidine (base) and serine (nucleophile). The substrate (black) is bound by the ...

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

Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ...

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

glutamate-ammonia ligase. Active site between two monomers of glutamine synthetase from Salmonella typhimurium. Cation binding ... Aspartic acid (aspartate). *DIDS. *Direct blue 71. *Erythro-4-methyl-L-glutamic acid ... which reacts with ammonia, forming glutamine and inorganic phosphate. ADP and Pi do not dissociate until ammonia binds and ... Ammonium, rather than ammonia, binds to GS because the binding site is polar and exposed to solvent.[7] In the second step, ...

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

Category:Ligases (EC 6) (Ligase)Edit. Category:EC 6.1 (form carbon-oxygen bonds)Edit. 6-carboxytetrahydropterin synthase ... Phenylalanine ammonia-lyase (EC 4.3.1.24). Category:EC 4.4 (carbon-sulfur lyases)Edit. *Category:EC 4.4.1 *Cystathionine gamma- ... Aspartate transaminase EC 2.6.1.1. Category:EC 2.7 (transfer phosphorus-containing groups)Edit. *Category:EC 2.7.2 *Butyrate ... 6 Category:Ligases (EC 6) (Ligase) *6.1 Category:EC 6.1 (form carbon-oxygen bonds) ...

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

https://en.wikipedia.org/wiki/Aspartate%E2%80%94ammonia_ligase

https://en.wikipedia.org/wiki/Aspartate%E2%80%94ammonia_ligase_(ADP-forming)

Information on EC 6.3.1.1 - aspartate-ammonia ligase. for references in articles please use BRENDA:EC6.3.1.1 ... ammonia-dependent ASNS, ammonia-dependent asparagine synthetase, AS-A, AS-AR, AsnA, ASNS, Asparagine synthetase, Asparagine ... and EC 6.3.5.4: The gene asnA codes for ammonia-dependent asparagine synthetases, EC 6.3.1.1, and the gene asnB codes for Gln- ... Alanine, aspartate and glutamate metabolism, Biosynthesis of secondary metabolites, Cyanoamino acid metabolism ...

https://brenda-enzymes.org/enzyme.php?ecno=6.3.1.1

aspartate ammonia ligase. *glutamine-dependent asparagine synthetase. *TS11. *TS11 cell cycle control protein ... Asparagine helps to break down toxic ammonia within cells, is important for protein modification, and is needed for making a ...

https://medlineplus.gov/genetics/gene/asns/

Aspartate-Ammonia Ligase / deficiency * Aspartate-Ammonia Ligase / genetics * Aspartate-Ammonia Ligase / metabolism ...

https://pubmed.ncbi.nlm.nih.gov/28842428/?dopt=Abstract

In addition, the aspartate ammonia ligase gene is expressed, as evidenced by an EST. In another case, copies of a 1,4-α-glucan ... The trpB gene and the gene for aspartate ammonia ligase are located 4,881 base-pairs (bp) apart on the same strand of a contig ... The origin of aspartate ammonia ligase is eubacterial, but not definitively of any particular lineage. In the absence of genome ... Three genes - aspartate ammonia ligase, BT-1 and lactate dehydrogenase - are expressed, as confirmed by the presence of an EST ...

https://genomebiology.biomedcentral.com/articles/10.1186/gb-2004-5-11-r88

Aspartate-Ammonia Ligase / antagonists & inhibitors * Aspartate-Ammonia Ligase / biosynthesis* * Aspartate-Ammonia Ligase / ...

https://pubmed.ncbi.nlm.nih.gov/17514734/?dopt=Abstract

Aspartate-ammonia ligase (EC 6.3.1.1). Incomplete. Asn or Asp. asnB Asparagine synthase (EC 6.3.5.4). ... Enzymes involved in these conversions include citrate lyase (1), aspartate aminotransferase (2), phosphoenolpyruvate ...

https://aem.asm.org/content/74/2/416/figures-only

... an asparate ammonia ligase subunit; the CTP synthase PyrG; PrfC, a peptide chain release factor; and SP_0095, a protein with ...

https://bmcmicrobiol.biomedcentral.com/articles/10.1186/1471-2180-11-245

... aspartate-ammonia ligase/asparagine synthetase (asnA[36] or asnB[37]), asparaginase (ansA or ansZ[38, 39]); and the transport ... encoding aspartate-ammonia ligase).. We also found a clear GlnR-binding site upstream of several genes involved in regulation, ... who argue that transport of ammonia (NH4+) should be tightly regulated to limit futile cycling by diffusion of ammonia out of ... In the case of the amtB-glnK operon (import of ammonia) it was formerly concluded that it is not repressed by GlnR on the basis ...

https://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-13-191

... ammonia ligase (asparagine synthetase) catalyses the conversion of L-aspartate to L-asparagine in the presence of ATP and ... The crystal structure of E.coli asparagine synthetase also showed the presence of this small subdomain[16]. Aspartate-- ... ammonia. AsnA structure revealed that AsnA structure is similar to that of the catalytic domain of yeast aspartyl-tRNA ...

http://pubmedcentralcanada.ca/pmcc/articles/PMC2865477/

... by asparagine synthase or aspartate-ammonia ligase.. Genes for fatty acid biosynthesis, such as fabG, fabA, fabZ, fabI, fabK, ... The l-asparagine pathway is absent in all the S. aureus genomes, along with the capability to convert l-aspartate to asparagine ...

https://jb.asm.org/content/191/12/4015

... aspartate-ammonia ligase (K01914), glutamine synthetase (K01915), asparagine synthase (K01953), diaminopimelate epimerase ( ... On the other hand, signals for gene expression attenuation seem to affect predominantly the alanine, aspartate and glutamate ( ... alanine-aspartate-glutamate (ko:00250), phenyalanine (ko:00360), tryptophan (ko:00380), and arginine (ko:00220) metabolism. ...

https://www.frontiersin.org/articles/10.3389/fcimb.2017.00383/full

glutamate-ammonia ligase. 2805. 2805. GOT1. glutamic-oxaloacetic transaminase 1, solubl.... 2806. 2806. GOT2. glutamic- ... Gene Set: KEGG_ALANINE_ASPARTATE_AND_GLUTAMATE_METABOLISM. Standard name. KEGG_ALANINE_ASPARTATE_AND_GLUTAMATE_METABOLISM. ...

http://software.broadinstitute.org/gsea/msigdb/cards/KEGG_ALANINE_ASPARTATE_AND_GLUTAMATE_METABOLISM.html

Aspartate-Ammonia Ligase / metabolism. Fatal Outcome. Female. Humans. Remission Induction. *Genetic Alliance. consumer health ... Aspartate-Ammonia Ligase ...

http://www.bmlsearch.com/?kwr=m0+acute+myelogenous+leukemia+drug+therapy+2000:2010%5Bpubdate%5D&cxts=100&stmp=b1

MeSH-minor] Aspartate-Ammonia Ligase / biosynthesis. Aspartate-Ammonia Ligase / genetics. Cell Line, Tumor. Doxorubicin / ... Chemical-registry-number] 7006-34-0 / Asparagine; EC 6.3.1.1 / Aspartate-Ammonia Ligase ... Aspartate-Ammonia Ligase ...

http://www.bmlsearch.com/?kwr=nk+cell+lymphoblastic+lymphoma+drug+therapy+2000:2010%5Bpubdate%5D&cxts=100&stmp=b1

6.3.1.1 Aspartate--ammonia ligase 6.3.1.2 Glutamine synthetase 6.3.1.3 Transferred entry: 6.3.4.13 6.3.1.4 Aspartate--ammonia ... ligase (ADP-forming) 6.3.1.5 NAD(+) synthase 6.3.1.6 Glutamate--ethylamine ligase 6.3.1.7 4-methyleneglutamate--ammonia ligase ... Ligases. Forming carbon-nitrogen bonds. Acid--ammonia (or amine) ligases (amide synthases). ... ligase 6.3.1.14 Diphthine--ammonia ligase 6.3.1.15 8-demethylnovobiocic acid synthase 6.3.1.16 Transferred entry: 6.3.3.6 6.3. ...

https://enzyme.expasy.org/EC/6.3.1.-

Aspartate-Ammonia Ligase * Neutral Amino Acid Transport Systems * Activating Transcription Factor 3 ...

https://experts.illinois.edu/en/publications/?descending=false&showAdvanced=false&allConcepts=true&inferConcepts=true&publicationYear=2010&publicationYear=2011&publicationYear=2012&publicationYear=2013&publicationYear=2014&publicationYear=2015&publicationYear=2017&publicationYear=2019&format=&nofollow=true&page=6

Aspartate-Ammonia Ligase aspartate-ammonia ligase Transcription Initiation Site Hep G2 Cells ...

https://experts.illinois.edu/en/persons/hong-chen/publications/?ordering=type&descending=false

aspartate-ammonia ligase Carrier Proteins Aspartate-Ammonia Ligase life events Genes gluconeogenesis ...

https://moh-it.pure.elsevier.com/en/publications/the-exposure-to-uteroplacental-insufficiency-is-associated-with-a

Wyrobek, A. J., Mulvihill, J. J., Wassom, J. S., Malling, H. V., Shelby, M. D., Lewis, S. E., Witt, K. L., Preston, R. J., Perreault, S. D., Allen, J. W., DeMarini, D. M., Woychik, R. P., Bishop, J. B., Anderson, D., Arnheim, N., Boice, J. D., Bridges, B. A., Crow, J. F., Dubrova, Y. E., Eichenlaub-Ritter, U. & 16 others, Erickson, R. P., Fridlyand, J., Gray, J., Hanawalt, P. C., Handel, M. A., Marchetti, F., Mohrenweiser, H. W., Moyzis, R. K., Primig, M., Russell, L. B., Sankaranarayanan, K., Skinner, M. K., Shoubridge, E. A., Taylor, J. A., Trasler, J. M. & Vasicek, T. J., Feb 2007, In : Environmental and Molecular Mutagenesis. 48, 2, p. 71-95 25 p.. Research output: Contribution to journal › Article ...

https://ohsu.pure.elsevier.com/en/persons/joe-gray/publications/?page=1&ordering=type&descending=false

Aspartate-ammonia ligase (substance). Code System Preferred Concept Name. Aspartate-ammonia ligase (substance). ... Enzyme (substance) {90668006 , SNOMED-CT } Substance with ligase mechanism of action (substance) {1672007 , SNOMED-CT } ... Aspartate-ammonia ligase Current Synonym true false 6200014 Asparagine synthetase Current Synonym true false ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=3070009

Aspartate-Ammonia Ligase aspartate-ammonia ligase Bombyx Polycomb-Group Proteins transcriptional activation ...

https://kyushu-u.pure.elsevier.com/ja/persons/takahiro-kusakabe/publications/?ordering=publicationYearThenTitle&descending=false&page=2

Aspartate-Ammonia Ligase Chemical Compounds * Starvation Medicine & Life Sciences * Aspartic Acid Chemical Compounds ... and disrupting their malate-aspartate shuttle. Supplementation of aspartate, depletion of mitochondria, and knockdown of ASNS ... and disrupting their malate-aspartate shuttle. Supplementation of aspartate, depletion of mitochondria, and knockdown of ASNS ... and disrupting their malate-aspartate shuttle. Supplementation of aspartate, depletion of mitochondria, and knockdown of ASNS ...

https://ucdavis.pure.elsevier.com/en/publications/arginine-starvation-kills-tumor-cells-through-aspartate-exhaustio

Aspartate-ammonia ligase (adenosine diphosphate-forming) Current Synonym true false 58222010 Aspartate-ammonia ligase (ADP- ... Aspartate-ammonia ligase (adenosine diphosphate-forming) (substance). Code System Preferred Concept Name. Aspartate-ammonia ... Enzyme (substance) {90668006 , SNOMED-CT } Substance with ligase mechanism of action (substance) {1672007 , SNOMED-CT } ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=34888001

Alanine, aspartate and glutamate metabolism; Arginine and proline metabolism; Metabolic pathways; Nitrogen metabolism. ... GLUL glutamate-ammonia ligase [ Homo sapiens ]. Synonyms:. GLUL; glutamate-ammonia ligase; GS; GLNS; PIG43; PIG59; glutamine ... ATP binding; glutamate decarboxylase activity; glutamate-ammonia ligase activity; identical protein binding; ligase activity; ... Recombinant Human Glutamate-ammonia Ligase, His-tagged. Download Datasheet See All GLUL Products. Bring this labeled protein ...

https://www.creativebiomart.net/description_631_14.htm

Fingerprint Dive into the research topics where RCCTM - Precision medicine is active. These topic labels come from the works of this organisations members. Together they form a unique fingerprint. ...

https://tmu.pure.elsevier.com/en/organisations/rcctm-precision-medicine/fingerprints/

In vitro SUMOylation assay to study SUMO E3 ligase activity. Yang, W. S., Campbell, M., Kung, H. J. & Chang, P. C., 一月 29 2018 ... Arginine starvation kills tumor cells through aspartate exhaustion and mitochondrial dysfunction. Cheng, C. T., Qi, Y., Wang, Y ... Kaposis Sarcoma-Associated Herpesvirus K-Rta Exhibits SUMO-Targeting Ubiquitin Ligase (STUbL) Like Activity and Is Essential ...

https://tmu.pure.elsevier.com/zh/publications/?ordering=lastNameFirstName&descending=true&showAdvanced=false&allConcepts=true&inferConcepts=true&publicationYear=2011&publicationYear=2012&publicationYear=2013&publicationYear=2014&publicationYear=2015&publicationYear=2016&publicationYear=2017&publicationYear=2018&publicationYear=2019&publicationYear=2020&author=f25f5146-ff7c-4173-bf7e-828ca4e032a7

Aspartate-Ammonia Ligase/genetics. *Aspartate-Ammonia Ligase/metabolism*. *Basic-Leucine Zipper Transcription Factors/genetics ...

https://www.ncbi.nlm.nih.gov/pubmed/18088315?dopt=Abstract

Aspartate-Ammonia Ligase. Asparagine. Prognosis. Reproducibility of Results. RNA Interference. Biological Availability ...

https://repository.icr.ac.uk/handle/internal/1289

See Aspartame , Aspartate aminotransferase . (thefreedictionary.com)
Aspartate aminotransferase-immunoglobulin complexes in patients with chronic liver disease. (thefreedictionary.com)
An immunological procedure for determination of mitochondrial aspartate aminotransferase in human serum. (thefreedictionary.com)
Immunoglobulin-complexed aspartate aminotransferase. (thefreedictionary.com)

The enzyme that divide the l-asparagine to aspartic acid and ammonia components. (ukessays.com)

An important gene associated with Citrullinemia, Classic is ASS1 (Argininosuccinate Synthase 1), and among its related pathways/superpathways are Arginine biosynthesis and Alanine, aspartate and glutamate metabolism . (malacards.org)

This enzyme participates in 3 metabolic pathways: alanine and aspartate metabolism, cyanoamino acid metabolism, and nitrogen metabolism. (wikipedia.org)

In enzymology, an aspartate-ammonia ligase (EC 6.3.1.1) is an enzyme that catalyzes the chemical reaction ATP + L-aspartate + NH3 ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-asparagine The 3 substrates of this enzyme are ATP, L-aspartate, and NH3, whereas its 3 products are AMP, diphosphate, and L-asparagine. (wikipedia.org)
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). (wikipedia.org)
The systematic name of this enzyme class is L-aspartate:ammonia ligase (AMP-forming). (wikipedia.org)
In enzymology, an aspartate-ammonia ligase (ADP-forming) (EC 6.3.1.4) is an enzyme that catalyzes the chemical reaction ATP + L-aspartate + NH3 ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate + L-asparagine The 3 substrates of this enzyme are ATP, L-aspartate, and NH3, whereas its 3 products are ADP, phosphate, and L-asparagine. (wikipedia.org)
These genetic changes likely alter the structure of the enzyme, impairing its ability to attach to molecules such as citrulline and aspartate. (medlineplus.gov)
The dependence of the enzyme on pyridoxal 5′-phosphate and the production of 3H4P with the release of ammonia indicate that it is a carbon-nitrogen lyase. (plantphysiol.org)
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. (wikibooks.org)
The systematic name of this enzyme class is xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming). (wikibooks.org)
Oxaloacetate is converted to aspartate using a transaminase enzyme. (hmdb.ca)
The enzyme transfers the amino group from glutamate to oxaloacetate producing alpha-ketoglutarate and aspartate. (hmdb.ca)

GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. (creativebiomart.net)
GLUL is essential for proliferation of fetal skin fibroblasts and plays an important role in controlling body pH by removing ammonia from circulation. (creativebiomart.net)
Homo sapiens glutamate-ammonia ligase (glutamine synthetase) (GLUL), transcript variant 2, mRNA. (abnova.com)
Glutamine synthetase (EC 6.3.1.2), also called glutamate-ammonia ligase (GLUL), is expressed throughout the body and plays an important role in controlling body pH and in removing ammonia from the circulation. (abnova.com)
Background: Glutamate-ammonia ligase (GLUL), also known as glutamine synthetase (GS), catalyzes the de novo synthesis of glutamine from glutamate and ammonia. (cellsignal.com)

Asparagine helps to break down toxic ammonia within cells, is important for protein modification, and is needed for making a certain molecule that transmits signals in the brain (a neurotransmitter). (medlineplus.gov)
A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. (leibniz-fli.de)
Below are the list of possible Aspartate, glycine, lysine and serine-rich protein products. (mybiosource.com)
This step combines two protein building blocks (amino acids), citrulline and aspartate, to form a molecule called argininosuccinic acid. (medlineplus.gov)
Using sensitive sequence analysis methods we show that PafA, the protein required for pupylation, belongs to the glutamine synthetase fold and predict that it is likely to catalyze an ATP-dependent peptide ligase reaction. (biomedcentral.com)

Background: Glutamate oxaloacetate transaminase 1 (GOT1) catalyzes the interconversion of aspartate and oxaloacetate (1). (cellsignal.com)
Among those patients who have AMA antibodies and alkaline phosphatase levels that are less than 1.5 times normal values, primary biliary cirrhosis may be diagnosed with 55% accuracy if patients have aspartate transaminase levels that are more than 5 times the upper limit of normal. (thefreedictionary.com)

Supplementation of aspartate, depletion of mitochondria, and knockdown of ASNS all protect the arginine-starved cells, establishing the causal effects of aspartate depletion and mitochondrial dysfunction on the arginine starvation-induced cell death. (elsevier.com)
Ann, David K. / Arginine starvation kills tumor cells through aspartate exhaustion and mitochondrial dysfunction . (elsevier.com)

carbamoyl-phosphate synthetase 2, aspartate. (broadinstitute.org)

Mechanistically, arginine starvation induces asparagine synthetase (ASNS), depleting these cancer cells of aspartate, and disrupting their malate-aspartate shuttle. (elsevier.com)

Our analyses imply GlnR-mediated regulation in constraining the import of ammonia/amino-containing compounds and the production of intracellular ammonia under conditions of high nitrogen availability. (biomedcentral.com)
As a result, nitrogen (in the form of ammonia) and other byproducts of the urea cycle (such as citrulline) build up in the bloodstream. (medlineplus.gov)

Hence, we predict that PafA is the Pup ligase, which catalyzes the ATP-dependent ligation of the terminal γ-carboxylate of glutamate to lysines, similar to the above enzymes. (biomedcentral.com)

This property describes a single polypeptide chain tRNA ligase responsible for direct aminoacylation with Asn. (jcvi.org)

In the asparagine synthetase reaction, ATP is used to activate aspartate, forming beta-aspartyl-AMP. (hmdb.ca)

Aspartate ammonia-lyase is an example of this class. (scienceaid.net)

An accumulation of ammonia during the first few days of life leads to poor feeding, vomiting, seizures, and the other signs and symptoms of type I citrullinemia. (medlineplus.gov)
12 An urea cycle disorder that involves the accumulation of ammonia in the blood. (malacards.org)

Tumor cells lack aspartate-ammonia ligase activity which restricts its ability to synthesize L-aspargine. (sanfoundry.com)

In addition less-conserved associations were found with, for instance, glutamate dehydrogenase in Streptococcaceae, purine catabolism and the reduction of nitrite in Bacillaceae, and aspartate/asparagine deamination in Lactobacillaceae. (biomedcentral.com)

A ubiquitin ligase complex found in the nucleus. (leibniz-fli.de)
A ubiquitin ligase complex found in the ER. (leibniz-fli.de)
In S. cerevisiae, this complex contains the ubiquitin ligase Hrd1p. (leibniz-fli.de)
In mammals, this complex contains the ubiquitin ligase HRD1 (Synoviolin) or AMFR (gp78). (leibniz-fli.de)
In S. cerevisiae, this complex contains the ubiquitin ligase Ssm4p/Doa10p. (leibniz-fli.de)

in proteins, aspartate takes the form of its amide, asparagine. (thefreedictionary.com)

Catalysis of the reaction: ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine. (leibniz-fli.de)

Our data challenge the view that ASNS promotes homeostasis, arguing instead that ASNS-induced aspartate depletion promotes cytotoxicity, which can be exploited for anti-cancer therapies. (elsevier.com)

In addition, GOT1 is critical to the survival of cells with electron transport chain inhibition by generating aspartate, a metabolite determining the proliferation of these cells (3-4). (cellsignal.com)

The first clinical trial to report successful treatment of erectile dysfunction with Pycnogenol[R] and L-arginine aspartate involved 40 men between 25 and 45 years of age suffering from mild ED. (thefreedictionary.com)

N(omega)-L-arginino)succinate from L-aspartate and L-citrulline: step 1/1. (abcam.com)

Ammonia is toxic, particularly to the nervous system. (medlineplus.gov)
25 Citrullinemia is an inherited disorder that causes ammonia and other toxic substances to accumulate in the blood. (malacards.org)

Anatomy1

Organisms9

Diseases1

Chemicals and Drugs22

Analytical, Diagnostic and Therapeutic Techniques and Equipment3

Phenomena and Processes4

Disciplines and Occupations4

Anthropology, Education, Sociology and Social Phenomena3

Humanities1

Information Science9

Health Care3

Geographicals2

L-Asparagine synthetase in serum as a marker for neoplasia. (1/128)

Transcriptional regulation of the human asparagine synthetase gene by carbohydrate availability. (2/128)

RT-PCR cloning, characterization and mRNA expression analysis of a cDNA encoding a type II asparagine synthetase in common bean. (3/128)

Activation of the unfolded protein response pathway induces human asparagine synthetase gene expression. (4/128)

Using genomic information to investigate the function of ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis. (5/128)

A mutation in the Corynebacterium glutamicum ltsA gene causes susceptibility to lysozyme, temperature-sensitive growth, and L-glutamate production. (6/128)

Evidence for multiple signaling pathways in the regulation of gene expression by amino acids in human cell lines. (7/128)

Activation of the human asparagine synthetase gene by the amino acid response and the endoplasmic reticulum stress response pathways occurs by common genomic elements. (8/128)

Glutamate-Ammonia Ligase

Aspartate Ammonia-Lyase

Ammonia

Aspartate Aminotransferases

Aspartate Carbamoyltransferase

RNA Ligase (ATP)

Aspartic Acid

Ubiquitin-Protein Ligases

DNA Ligases

Leuconostocaceae

Lactobacillales

Glutamate Dehydrogenase

Genomics

Sodium-Hydrogen Antiporter

Molecular Sequence Data

Genome, Bacterial

Mycoplasma gallisepticum

Archives

Mycoplasma

Biological Science Disciplines

Periodicals as Topic

PubMed

Directories as Topic

Bacteroides

Bacteroides fragilis

Bacteroides Infections

Prevotella

Tetracycline Resistance

Conjugation, Genetic

R Factors

Receptors, Lipoprotein

Lipoproteins, HDL

ADP-ribosyl Cyclase

Search Engine

Lipoproteins, LDL

Lipoproteins

Receptors, LDL

Oregon

Crows

Bibliometrics

Publications

State Health Plans

Publishing

Argininosuccinate Synthase

Arginine

Argininosuccinate Lyase

Citrulline

Arginase

Cell Line, Tumor

Equidae

Individualized Medicine

Health Maintenance Organizations

Dermatoglyphics

DNA Fingerprinting

Taiwan

Research

Diving

L-Asparagine synthetase in serum as a marker for neoplasia. (1/128)

Transcriptional regulation of the human asparagine synthetase gene by carbohydrate availability. (2/128)

RT-PCR cloning, characterization and mRNA expression analysis of a cDNA encoding a type II asparagine synthetase in common bean. (3/128)

Activation of the unfolded protein response pathway induces human asparagine synthetase gene expression. (4/128)

Using genomic information to investigate the function of ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis. (5/128)

A mutation in the Corynebacterium glutamicum ltsA gene causes susceptibility to lysozyme, temperature-sensitive growth, and L-glutamate production. (6/128)

Evidence for multiple signaling pathways in the regulation of gene expression by amino acids in human cell lines. (7/128)

Activation of the human asparagine synthetase gene by the amino acid response and the endoplasmic reticulum stress response pathways occurs by common genomic elements. (8/128)

Asparagine synthase (glutamine-hydrolysing) - Wikipedia

OriGene - ASNS (NM 001178076) Human ORF cDNA Clone

asnB - Asparagine synthetase B - Mycobacterium tuberculosis variant pinnipedii - asnB gene & protein

Aspartate-Ammonia Ligase - Asparagine Synthetase Summary Report | CureHunter

ASNS Gene - GeneCards | ASNS Protein | ASNS Antibody

Plus it

Asparagine synthetase Overexpression Lysate (Adult Normal), Novus Biologicals (NBL1-07768) | VWR

WikiGenes - ASNSD1 - asparagine synthetase domain containing 1

Limiting Dietary Asparagine Could Reduce Cancer Spread

Anti-Asparagine synthetase antibody [EP282Y] (ab40850)

INRA - NitroScape

Root parasite induced nitrogen transfer between plants is density dependent - Citation formats | Research Explorer | The...

anti-Asparagine synthetase antibody | GeneTex

ASNS Antibody (monoclonal) (M01) - Mouse monoclonal antibody raised against a partial recombinant ASNS. E - Buy Now! |Abgent

The Yang Research Group - Members - Hee Sun Chung

$Gentaur Molecular :Sceti K.K. \ L Asparagine \ 2703$ Gentaur Molecular :Sceti K.K. \ L Asparagine \ 2703

$Gentaur Molecular :Biosera \ L Asparagine Monohydrate 100g \ PM-P1404/100$ Gentaur Molecular :Biosera \ L Asparagine Monohydrate 100g \ PM-P1404/100