Glutamate-Ammonia Ligase
Aspartate Ammonia-Lyase
Ammonia
Aspartate Aminotransferases
Aspartate Carbamoyltransferase
RNA Ligase (ATP)
Aspartic Acid
Ubiquitin-Protein Ligases
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.
DNA Ligases
Clostridium thermocellum
Renewable Energy
Biofuels
Clostridium
Cellulase
Gram-Positive Asporogenous Rods, Irregular
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)
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
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Aspartate-ammonia ligase
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 ...
Aspartate-ammonia ligase (ADP-forming)
... 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. ...
Asparagine synthetase
... (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 ...
List of MeSH codes (D08)
... 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 ...
D-aspartate ligase
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 ...
List of EC numbers (EC 6)
... aspartate-ammonia ligase (ADP-forming) EC 6.3.1.5: NAD+ synthase EC 6.3.1.6: glutamate-ethylamine ligase EC 6.3.1.7: 4- ... 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 ... aspartate-ammonia ligase EC 6.3.1.2: glutamine synthetase EC 6.3.1.3: Now EC 6.3.4.13, phosphoribosylamine-glycine ligase EC ... asparagine-tRNA ligase EC 6.1.1.23: aspartate-tRNAAsn ligase EC 6.1.1.24: glutamate-tRNAGln ligase EC 6.1.1.25: The tRNAPyl is ...
List of EC numbers (EC 2)
... aspartate kinase EC 2.7.2.5: Now EC 6.3.4.16, carbamoyl-phosphate synthase (ammonia) EC 2.7.2.6: formate kinase EC 2.7.2.7: ... glutamate-tRNA ligase, EC 1.2.1.70, glutamyl-tRNA reductase and EC 5.4.3.8 EC 2.7.2.14: branched-chain-fatty-acid kinase EC 2.7 ... 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 ...
Biosynthesis
... 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 ...
Amphetamine
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 ...
List of enzymes
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- ...
Mitochondrion
Reducing equivalents from the cytoplasm can be imported via the malate-aspartate shuttle system of antiporter proteins or fed ... 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 ...
Catalytic triad
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 ...
List of EC numbers (EC 4)
D-serine ammonia-lyase EC 4.3.1.19: threonine ammonia-lyase EC 4.3.1.20: erythro-3-hydroxy-L-aspartate ammonia-lyase EC 4.3. ... heme ligase EC 4.99.1.9:: coproporphyrin ferrochelatase * EC 4.99.1.10: magnesium dechelatase * EC 4.99.1.11: sirohydrochlorin ... diaminopropionate ammonia-lyase EC 4.3.1.16: threo-3-hydroxy-L-aspartate ammonia-lyase EC 4.3.1.17: L-serine ammonia-lyase EC ... aspartate ammonia-lyase EC 4.3.1.2: methylaspartate ammonia-lyase EC 4.3.1.3: histidine ammonia-lyase EC 4.3.1.4: ...
6.3.1.4: aspartate-ammonia ligase (ADP-forming) - BRENDA Enzyme Database
... aspartate-ammonia ligase (ADP-forming). This is an abbreviated version!. For detailed information about aspartate-ammonia ... L-aspartate. + NH3. = ADP. + phosphate. + L-asparagine. Synonyms. Asparagine synthetase, Asparagine synthetase (ADP-forming), ... ligase (ADP-forming), go to the full flat file.. Reaction. ATP. + ... 6.3.1 Acid ammonia (or amine) ligases (amide synthases). 6.3.1.4 aspartate-ammonia ligase (ADP-forming) ...
ASNS gene: MedlinePlus Genetics
Nicholas Rattray - Research output
- University of Strathclyde
DeCS
Aspartate-Ammonia Ligase Entry term(s). Asparagine Synthase Asparagine Synthetase Aspartate Ammonia Ligase Ligase, Aspartate- ... Aspartate Ammonia Ligase. Ligase, Aspartate-Ammonia. Synthase, Asparagine. Synthetase B, Asparagine. Synthetase, Asparagine. ... L-Aspartate:ammonia ligase (AMP-forming) Previous Indexing:. Ammonia (1973-1974). Aspartic Acid (1973-1974). Ligases (1973-1974 ... 95: was ASPARAGINE SYNTHETASE 1975-94 (see under LIGASES 1975-90). Online Note:. use ASPARTATE-AMMONIA LIGASE to search ...
Code System Concept
HOMD :: SEQF3493
CCL17371 details
Chromosomal localization of human genes required for G|sub|1|/sub| progression in mammalian cells - Fingerprint
- Albert...
HOMD :: SEQF2940
Aspartate--tRNA(Asp/Asn) ligase. 186. SEQF2940,KI515728.1. SEQF2940_00189 jb [NA] [AA] 933/310. 191067-191999. hypothetical ... Aspartate ammonia-lyase. 79. SEQF2940,KI515728.1. SEQF2940_00081 jb [NA] [AA] 846/281. 81359-80514. ATP ... Pup--protein ligase. 70. SEQF2940,KI515728.1. SEQF2940_00072 jb [NA] [AA] 192/63. 69135-68944. Prokaryotic ubiquitin-like ... Alanine--tRNA ligase. 183. SEQF2940,KI515728.1. SEQF2940_00186 jb [NA] [AA] 1386/461. 187677-186292. putative AAA domain- ...
Domain IPR003439:ABC transporter-like
Aspartate--ammonia ligase 10 Domain IPR025895:Lysine-2,3-aminomutase, C-terminal domain 10 Active_site IPR019756:Peptidase S26A ... Aspartate ammonia-lyase 5 Domain IPR021029:DNA polymerase III, tau subunit, domain V 5 Domain IPR025832:GxGYxYP putative ... Asparagine-tRNA ligase 16 Family IPR005921:Histidine ammonia-lyase 16 Domain IPR032712:AsmA-like, C-terminal 16 Family ... Ethanolamine ammonia-lyase light chain 3 Family IPR011957:Benzoate-CoA ligase family 3 Family IPR022448:Quinoprotein ...
"sequence id","alias","species","description",...
"Glutamate-ammonia-ligase adenylyltransferase [Ensembl]. GlnD PII-uridylyltransferase, Glutamate-ammonia ligase ... ","aspartate kinase, monofunctional class [Ensembl]. CASTOR, Aspartate/glutamate/uridylate kinase [Interproscan].","protein_ ... ","UDP-N-acetylmuramate--L-alanine ligase [Ensembl]. Mur ligase family, Mur ligase middle domain [Interproscan].","protein_ ... ","UDP-N-acetylmuramoylalanine--D-glutamate ligase [Ensembl]. Mur ligase family, Mur ligase middle domain [Interproscan]."," ...
Pesquisa | Biblioteca Virtual em Saúde - BRASIL
Glutamate-ammonia ligase (GLUL) is important for acid-base homeostasis, ammonia detoxification, cell signaling, and ... We observed increased labeling of malate and aspartate in A549 GLUL KO cells, whereas the non-resistant GLUL KO H1299 cells ... The malate and aspartate shuttle supported cellular NADH production and was associated with cellular metabolic fitness. ... We proposed a novel metabolic mechanism in cancer drug resistance where the increased capacity of the malate-aspartate shuttle ...
Ligase - Wikipédia
ARNt ligase EC 6.1.1.22 asparagine ARNt ligase EC 6.1.1.23 aspartate ARNt Asn ligase EC 6.1.1.24 glutamate ARNtGln ligase EC ... ligase EC 6.3.4.16 carbamoyl-phosphate synthase (ammonia) EC 6.3.4.17 formate-dihydrofolate ligase EC 6.3.4.18 5-(carboxyamino) ... 6.1.1.9 valine ARNt ligase EC 6.1.1.10 methionine ARNt ligase EC 6.1.1.11 serine ARNt ligase EC 6.1.1.12 aspartate ARNt ligase ... 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 acide-CoA ligase ( ...
UMLS. CSP-HL7-ICD9CM-NCI-NDFRT-RXNORM - Terms starting with 'U' - MEDINDEX.AM
49. glutamate ammonia ligase [An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and ... N methyl D aspartate receptor 7. Glucocorticoid Receptor [Widely expressed by human NR3C1 Gene (NR3 Family) as 6 isoforms, ... carbon nitrogen ligase; 3. glucan [group of polysaccharides composed of repeating glucose units; they can consist of branched ... The brain enzyme also acts on L-cysteate, L-cysteine sulfinate, and L-aspartate. EC 4.1.1.15. ( MSH )] (UMLS (CSP) C0017785) = ...
Overall Nitrogen Metabolism - Amino Acids: Disposal of Nitrogen | Biochemistry
Nitrogen leaves the body as urea, ammonia, and other products derived from amino acid metabolism. The role of body proteins in ... Note: Enzyme 1 (E1, or activating enzyme) activates Ub, which is then transferred to E2 (conjugating enzyme). E3 (a ligase) ... whereas those with aspartate at their N-terminus have a half-life of only 3 minutes. Additionally, proteins rich in sequences ...
HOMD :: SEQF3500
type I glutamate--ammonia ligase. 315. SEQF3500,VSEA01000013.1. TYB19786.1 jb [NA] [AA] 1284/427. 57934-56651. adhesin. ... bifunctional aspartate kinase/homoserine dehydrogenase I. 304. SEQF3500,VSEA01000013.1. TYB19775.1 jb [NA] [AA] 1389/462. 49039 ... tryptophan--tRNA ligase. 344. SEQF3500,VSEA01000012.1. TYB19815.1 jb [NA] [AA] 645/214. 32950-32306. 3%2C4-dihydroxy-2-butanone ...
SMPDB
Aspartate. aminotransferase,. cytoplasmic. Nitric oxide. synthase, brain. Bifunctional. glutamate/proline-. -tRNA ligase. ... ammonia],. mitochondrial. Glutamate. dehydrogenase. 1,. mitochondrial. Ornithine. aminotransferase,. mitochondrial. Delta-1-. ... ligase,. mitochondrial. Glycine. amidinotransferase,. mitochondrial. Guanidinoacetate. N-. methyltransferase. Creatine kinase. ...
Intestinal Metabolic Bromhidrosis Syndrome Alliance
Low potassium (ammonia impairs potassium uptake indirectly by binding to the potassium receptors) ... A possible unknown gene encoding an isovalerate CoA ligase Important is the aspect that e.g. the ACSM2B is also involved in ... Reducing the dietary amount of glutamine, glutamate, aspartate, lysine and ornithine *. Reducing the uptake of calcium ... Elevations in various amino acids related to the ammonia degradation have been found with transitive hyperammonemia. This ...
MIR4653 3P
Amino acids in rat neostriatum: Alteration by kainic acid lesion<...
Glutamate-Ammonia Ligase Medicine & Life Sciences 48% * Glutamine Medicine & Life Sciences 37% ... The large decrease in glutamate and aspartate is consistent with hypotheses concerning the intraneuronal localization of a ... The large decrease in glutamate and aspartate is consistent with hypotheses concerning the intraneuronal localization of a ... The large decrease in glutamate and aspartate is consistent with hypotheses concerning the intraneuronal localization of a ...
Metabolites | Free Full-Text | Modelling hCDKL5 Heterologous Expression in Bacteria
... l-aspartate. rxn00285. Citrate cycle (TCA cycle). Succinate-CoA ligase (ADP forming). ATP + CoA + succinate =, ADP + phosphate ... The 11 gene-encoded reactions included the reactions involved in histidine biosynthesis and an ammonia transporter. The ... ATPL-aspartate 4-phosphotransferase. ATP + l-aspartate =, ADP + 4-phospho-l-aspartate. ... and its subsequent conversion to 4-phospho-L-aspartate and l-aspartate-4-semialdehyde (Figure 4B), catalysed by ATPL-aspartate- ...
List of EC numbers (EC 2)
glutamate-ammonia-ligase) adenylyltransferase. *: N-acylneuraminate cytidylyltransferase. *: glucuronate-1-phosphate ... aspartate kinase. *: now EC 6.3.4.16. *: formate kinase. *: butyrate kinase. *: acetylglutamate kinase. *: now EC 6.3.5.5. *: ... ammonia kinase. *: phosphoenolpyruvate-protein phosphotransferase. *: agmatine kinase. *: now EC 2.7.13.1. *: now EC 2.7.13.2. ... List of EC numbers (EC 6) - This list contains a list of EC numbers for the sixth group, EC 6, ligases, placed in numerical ...
Lenalidomide (Teva Pharmaceuticals, Inc.): FDA Package Insert, Page 6
Time-resolved multi-omics analysis reveals the role of nutrient stress-induced resource reallocation for TAG accumulation in...
Glucose and ammonia in the medium, mycelial dry weigh and fatty acid methyl esters (FAME) were determined as described ... 4c). These proteins are mainly involved in glycine, serine and threonine, alanine, aspartate and glutamate, arginine and ... Zheng N, Shabek N. Ubiquitin ligases: structure, function, and regulation. Annu Rev Biochem. 2017;86:129-57. ... Nitrogen stress studies proceeded in 7.5 L-fermentation tanks containing 4.0 L Kendrick broth with ammonia as the nitrogen ...
YOR184W 2167.216480 INESSENTIAL SER1 phosphoserine transaminase,phosphoserine aminotransferase
... aspartate--tRNA ligase, mitochondrion YER182W -0.456649 INESSENTIAL biological_process unknown, molecular_function unknown, ... 2.448005 INESSENTIAL MEP2 Ammonia transport protein, transport, YDR183W 2.431624 INESSENTIAL PLP1 Phosducin-Like Protein, ... YER052C 510.712176 INESSENTIAL HOM3 Aspartate kinase (L-aspartate 4-P-transferase) (EC 2.7.2.4),aspartate kinase, YNL046W ... component unknown YLR027C 61.250510 INESSENTIAL AAT2 aspartate aminotransferase, cytosolic, aspartate catabolism*, aspartate ...
Genome-scale metabolic analysis of Clostridium thermocellum for bioethanol production | BMC Systems Biology | Full Text
We did, however, add a reaction for succinate:CoA ligase, based on the fact that succinate has been reported as a metabolic ... In addition to the carbon source, the in silico minimal medium used for simulations contained water (h2o), ammonia (nh4), ... excess carbon is relieved by an increase in the production of aspartate to 8.48 mmol gDW-1 hr-1 (see Additional file 1). With ... CoA ligase. There was no clear genetic evidence for these genes, although similarity searches produced some probable reciprocal ...
SMPDB
Ammonia Recycling. *Arbekacin Action Pathway. *Aspartate Metabolism. *Azithromycin Action Pathway. *Canavan Disease ... and ubiquitin ligase (Fbs). They are thought to recognize high-mannose-type glycans with subtly different structures. Mannose- ... Aspartic acid (Asp, D), also known as aspartate, the name of its anion, is one of the 20 natural proteinogenic amino acids ... Interestingly, methylamine and ammonia levels are reciprocally controlled by a semicarbazide-sensitive amine oxidase activity ...
Asparagine3
- 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)
- An enzyme that catalyzes the formation of asparagine from ammonia and aspartic acid, in the presence of ATP . (bvsalud.org)
- In the asparagine synthetase reaction, ATP is used to activate aspartate, forming beta-aspartyl-AMP. (smpdb.ca)
Glutamate6
- glutamate-ammonia ligase [Source:HGN. (gsea-msigdb.org)
- The high affinity uptake of choline by synaptosomal preparations of lesioned striatum was decreased by 70% compared to controls whereas that of glutamate/aspartate was either unchanged or somewhat increased on a per mg protein basis. (mssm.edu)
- The unchanging glutamine levels and increase in glutamine synthetase activity are consistent with the widespread gliosis and the lack of change in glutamate/aspartate high affinity uptake is consistent with a sparing of afferent terminals. (mssm.edu)
- The large decrease in glutamate and aspartate is consistent with hypotheses concerning the intraneuronal localization of a major pool of these amino acids, especially in GABAergic neurons. (mssm.edu)
- The enzyme transfers the amino group from glutamate to oxaloacetate producing alpha-ketoglutarate and aspartate. (smpdb.ca)
- Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. (lookformedical.com)
Enzymes3
- Le nom courant des enzymes de type ligase inclut souvent le terme « ligase » comme l' ADN ligase du phage T4 utilisée pour structurer des fragments d' ADN . (wikipedia.org)
- Attention cependant à ne pas confondre les enzymes synthétases avec les enzymes synthases (qui sont toutes deux des enzymes du groupe des ligases). (wikipedia.org)
- Les ligases sont classées EC 6 dans la nomenclature EC des enzymes. (wikipedia.org)
Synthase1
- En fait la synthase forme et défait les doubles liaisons d'une protéine. (wikipedia.org)
Enzyme that catalyzes1
- An enzyme that catalyzes the conversion of L-tryptophan and water to indole, pyruvate, and ammonia. (lookformedical.com)
Glutamine1
- EC 6.3.5 Carbone-Azote Ligases avec Glutamine comme Amido-N-Donneur. (wikipedia.org)
Protein1
- E3 (a ligase) identifies the protein to be degraded and interacts with E2-Ub. (pharmacy180.com)
Methyl1
- There are well known further players such as carboxylates (e.g. butyrate, isovalerate), amines, sulfuric compounds, ammonia, methyl mercaptan and indole to name some of them. (imbs-alliance.org)
Oxaloacetate1
- Oxaloacetate is converted to aspartate using a transaminase enzyme. (smpdb.ca)
Threonine1
- Threonine catabolism in mammals appears to be due primarily (70-80%) to the activity of threonine dehydrogenase (EC 1.1.1.103) that oxidizes threonine to 2-amino-3-oxobutyrate, which forms glycine and acetyl CoA, whereas threonine dehydratase (EC 4.2.1.16) that catabolizes threonine into 2-oxobutyrate and ammonia, is significantly less active. (smpdb.ca)
Nitrogen1
- Nitrogen leaves the body as urea, ammonia, and other products derived from amino acid metabolism. (pharmacy180.com)
Levels1
- Interestingly, methylamine and ammonia levels are reciprocally controlled by a semicarbazide-sensitive amine oxidase activity that deaminates methylamine to formaldehyde with the production of ammonia and hydrogen peroxide. (smpdb.ca)
Diphthine-ammoni1
- EC 6.3.2.22: Now EC 6.3.1.14 , diphthine-ammonia ligase. (wikibedia.ru)
Alanine1
- This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism . (wikipedia.org)
Fumarate2
- Hence, this enzyme has one substrate , L-aspartate , and two products , fumarate and NH 3 . (wikipedia.org)
- The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming) . (wikipedia.org)
Toxic ammonia2
- 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)
- Legal Disclaimer Glutamic acid is also important for energy production, protecting the immune system, removing toxic ammonia from the body and supporting muscle growth and function. (landcert.com)
Glutamine3
- In pathways I or II, aspartate is amidated directly, with glutamine or ammonia as the nitrogen source. (lbl.gov)
- Individuals with HHH syndrome should be maintained on an age-appropriate protein-restricted diet, citrulline supplementation, and sodium phenylbutyrate to maintain plasma concentrations of ammonia, glutamine, arginine, and essential amino acids within normal range. (nih.gov)
- Attention to subtle changes in mood, behavior, and eating and/or the onset of vomiting, which may suggest that plasma concentrations of glutamine and ammonia are increasing. (nih.gov)
Carbon-nitrogen bonds1
- This enzyme belongs to the family of lyases , specifically ammonia lyases, which cleave carbon-nitrogen bonds. (wikipedia.org)
Enzyme2
- An enzyme that catalyzes the formation of asparagine from ammonia and aspartic acid, in the presence of ATP. (nih.gov)
- Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. (nih.gov)
TRNA2
- In pathway III, aspartate is ligated to tRNA(Asn) and then amidated to Asn-tRNA(Asn). (lbl.gov)
- EC 6.1.1.28: proline/cysteine-tRNA ligase. (wikibedia.ru)
Arginine1
- Of primary importance is the use of established protocols to rapidly control hyperammonemic episodes by discontinuation of protein intake, intravenous infusion of glucose and, as needed, infusion of supplemental arginine and the ammonia removal drugs sodium benzoate and sodium phenylacetate. (nih.gov)
Acid1
- Routine assessment of plasma ammonia concentration, plasma and urine amino acid concentrations, urine organic acids, and urine orotic acid based on age and history of compliance and metabolic control. (nih.gov)
Substrate1
- An important step in the proteolytic cascade is specific recognition of the substrate by one of many ubiquitin ligases, E3s, which is followed by generation of the polyubiquitin degradation signal. (pharmaceuticalintelligence.com)
Compounds1
- A group of compounds derived from ammonia by substituting organic radicals for the hydrogens. (lookformedical.com)
Sodium1
- Fluorescence characters from the powdered seed The drug natural powder was used and treated with different chemical reagents such as for example sulphuric acidity, hydrochloric acidity, 5% iodine option, 50% ferric chloride, 10% sodium hydroxide and ammonia option, business lead Acetate and the color attained was visualized under brief UV light (254 nm) and longer UV light (366 nm) within an UV chamber. (dactolisib.info)
Activity1
- Regulates E3 ubiquitin-protein ligase activity of RNF19A (By similarity). (nih.gov)
Reaction1
- The reaction is the basis of the industrial synthesis of aspartate. (wikipedia.org)
Names1
- Other names in common use include aspartase , fumaric aminase , L-aspartase , and L-aspartate ammonia-lyase . (wikipedia.org)
Group1
- This list contains a list of EC numbers for the sixth group, EC 6 , ligases , placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology . (wikibedia.ru)