Aspartate Carbamoyltransferase: 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.Ornithine Carbamoyltransferase: A urea cycle enzyme that catalyzes the formation of orthophosphate and L-citrulline (CITRULLINE) from CARBAMOYL PHOSPHATE and L-ornithine (ORNITHINE). Deficiency of this enzyme may be transmitted as an X-linked trait. EC 2.1.3.3.Dihydroorotase: An enzyme that, in the course of pyrimidine biosynthesis, catalyzes ring closure by removal of water from N-carbamoylaspartate to yield dihydro-orotic acid. EC 3.5.2.3.Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing): An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and glutamine. This enzyme is important in the de novo biosynthesis of pyrimidines. EC 6.3.5.5.Carbamyl Phosphate: The monoanhydride of carbamic acid with PHOSPHORIC ACID. It is an important intermediate metabolite and is synthesized enzymatically by CARBAMYL-PHOSPHATE SYNTHASE (AMMONIA) and CARBAMOYL-PHOSPHATE SYNTHASE (GLUTAMINE-HYDROLYZING).Cytidine Triphosphate: Cytidine 5'-(tetrahydrogen triphosphate). A cytosine nucleotide containing three phosphate groups esterified to the sugar moiety.Phosphonoacetic Acid: A simple organophosphorus compound that inhibits DNA polymerase, especially in viruses and is used as an antiviral agent.Moritella: A genus of gram-negative, curved or straight rod-shaped bacteria, in the family ALTEROMONADACEAE. They are chemo-organotrophic, halophilic, and associated with cold marine habitats.Dihydroorotate Oxidase: An enzyme that in the course of pyrimidine biosynthesis, catalyzes the oxidation of dihydro-orotic acid to orotic acid utilizing oxygen as the electron acceptor. This enzyme is a flavoprotein which contains both FLAVIN-ADENINE DINUCLEOTIDE and FLAVIN MONONUCLEOTIDE as well as iron-sulfur centers. EC 1.3.3.1.Aspartic Acid: 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.Allosteric Regulation: The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.X-Ray Diffraction: The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Carboxyl and Carbamoyl Transferases: A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.Ornithine Carbamoyltransferase Deficiency Disease: An inherited urea cycle disorder associated with deficiency of the enzyme ORNITHINE CARBAMOYLTRANSFERASE, transmitted as an X-linked trait and featuring elevations of amino acids and ammonia in the serum. Clinical features, which are more prominent in males, include seizures, behavioral alterations, episodic vomiting, lethargy, and coma. (Menkes, Textbook of Child Neurology, 5th ed, pp49-50)Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Ornithine: An amino acid produced in the urea cycle by the splitting off of urea from arginine.Aspartate Aminotransferases: 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.CitrullinePhosphotransferases (Carboxyl Group Acceptor): A class of enzymes that transfers phosphate groups and has a carboxyl group as an acceptor. EC 2.7.2.Orotic AcidOrnithine-Oxo-Acid Transaminase: A pyridoxal phosphate enzyme that catalyzes the formation of glutamate gamma-semialdehyde and an L-amino acid from L-ornithine and a 2-keto-acid. EC 2.6.1.13.Carbamoyl-Phosphate Synthase (Ammonia): An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and ammonia. This enzyme is specific for arginine biosynthesis or the urea cycle. Absence or lack of this enzyme may cause CARBAMOYL-PHOSPHATE SYNTHASE I DEFICIENCY DISEASE. EC 6.3.4.16.Hydrolases: Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.Argininosuccinate Lyase: 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.Arginine: An essential amino acid that is physiologically active in the L-form.Arginase: 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.Sodium Benzoate: The sodium salt of BENZOIC ACID. It is used as an antifungal preservative in pharmaceutical preparations and foods. It may also be used as a test for liver function.Arsenates: Inorganic or organic salts and esters of arsenic acid.Transferases: Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.Kinetics: The rate dynamics in chemical or physical systems.Transaminases: A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Pyrococcus furiosus: A species of strictly anaerobic, hyperthermophilic archaea which lives in geothermally-heated marine sediments. It exhibits heterotropic growth by fermentation or sulfur respiration.Argininosuccinate Synthase: 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.Molecular Sequence Data: 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.

Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit. (1/437)

The lack of knowledge of the three-dimensional structure of the trimeric, catalytic (C) subunit of aspartate transcarbamoylase (ATCase) has impeded understanding of the allosteric regulation of this enzyme and left unresolved the mechanism by which the active, unregulated C trimers are inactivated on incorporation into the unliganded (taut or T state) holoenzyme. Surprisingly, the isolated C trimer, based on the 1.9-A crystal structure reported here, resembles more closely the trimers in the T state enzyme than in the holoenzyme:bisubstrate-analog complex, which has been considered as the active, relaxed (R) state enzyme. Unlike the C trimer in either the T state or bisubstrate-analog-bound holoenzyme, the isolated C trimer lacks 3-fold symmetry, and the active sites are partially disordered. The flexibility of the C trimer, contrasted to the highly constrained T state ATCase, suggests that regulation of the holoenzyme involves modulating the potential for conformational changes essential for catalysis. Large differences in structure between the active C trimer and the holoenzyme:bisubstrate-analog complex call into question the view that this complex represents the activated R state of ATCase.  (+info)

Simulations of the T <--> R conformational transition in aspartate transcarbamylase. (2/437)

Aspartate transcarbamylase (ATCase) from Escherichia coli is one of the best known allosteric enzymes. In spite of numerous experiments performed by biochemists, no consensus model for the cooperative transition between the tensed (T) and the relaxed (R) forms exists. It is hypothesized, however, that changes in the quaternary structure play a key role in the allosteric properties of oligomeric proteins such as ATCase. Previous normal mode calculations of the two states of ATCase illustrated the type of motions that could be important in initiating the transition. In this work four pathways for the transition were calculated using the targeted molecular dynamics (TMD) method without constraint on the symmetry of the system. The most important quaternary structure changes are the relative rotation and translation of the catalytic trimers and the rotations of the regulatory dimers. The simulations show that these quaternary changes start immediately and finish when about 70% of the transition is completed whereas there are tertiary changes throughout the transition. In agreement with the work of Lipscomb et al., it was found that the relative translation between the catalytic trimers appears to play a central role in allowing the transition to occur. In all the simulations differences are observed in the opening and closing behaviours of the domains in the catalytic and regulatory chains that could provide a structural interpretation for the results of certain site-directed mutagenesis experiments. Overall the motions of the subunits are concerted even though the constraint imposed on the TMD method does not explicitly require that this be so.  (+info)

Micronuclei formation with chromosome breaks and gene amplification caused by Vpr, an accessory gene of human immunodeficiency virus. (3/437)

Vpr, an accessory gene of human immunodeficiency virus, induces cell cycle abnormality by accumulating cells at the G2-M phase. We reported recently that Vpr caused both micronuclei formation and aneuploidy. Here, we show that Vpr also induced chromosome breaks and gene amplification. Expression of Vpr induced more than 10-fold increase of colonies resistant to N-(phosphonacetyl)-L-aspartate, an inhibitor of pyrimidine de novo synthesis. Fluorescence in situ hybridization analysis detected that 4 of 10 N-(phosphonacetyl)-L-aspartate resistant clones studied had intrachromosomal amplification of carbamyl-phosphate synthetase/aspartate transcarbamoylase/dihydroorotase gene. Another single clone had dicentrics. Data suggested that the Vpr-induced chromosome breaks leading to gene amplification, followed by bridge-breakage-fusion cycle, were one of the possible mechanisms of Vpr-induced genomic instability.  (+info)

The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity. (4/437)

The X-ray structure of the Escherichia coli aspartate transcarbamoylase with the bisubstrate analog phosphonacetyl-L-aspartate (PALA) bound shows that PALA interacts with Lys84 from an adjacent catalytic chain. To probe the function of Lys84, site-specific mutagenesis was used to convert Lys84 to alanine, threonine, and asparagine. The K84N and K84T enzymes exhibited 0.08 and 0.29% of the activity of the wild-type enzyme, respectively. However, the K84A enzyme retained 12% of the activity of the wild-type enzyme. For each of these enzymes, the affinity for aspartate was reduced 5- to 10-fold, and the affinity for carbamoyl phosphate was reduced 10- to 30-fold. The enzymes K84N and K84T exhibited no appreciable cooperativity, whereas the K84A enzyme exhibited a Hill coefficient of 1.8. The residual cooperativity and enhanced activity of the K84A enzyme suggest that in this enzyme another mechanism functions to restore catalytic activity. Modeling studies as well as molecular dynamics simulations suggest that in the case of only the K84A enzyme, the lysine residue at position 83 can reorient into the active site and complement for the loss of Lys84. This hypothesis was tested by the creation and analysis of the K83A enzyme and a double mutant enzyme (DM) that has both Lys83 and Lys84 replaced by alanine. The DM enzyme has no cooperativity and exhibited 0.18% of wild-type activity, while the K83A enzyme exhibited 61% of wild-type activity. These data suggest that Lys84 is not only catalytically important, but is also essential for binding both substrates and creation of the high-activity, high-affinity active site. Since low-angle X-ray scattering demonstrated that the mutant enzymes can be converted to the R-structural state, the loss of cooperativity must be related to the inability of these mutant enzymes to form the high-activity, high-affinity active site characteristic of the R-functional state of the enzyme.  (+info)

Half of Saccharomyces cerevisiae carbamoyl phosphate synthetase produces and channels carbamoyl phosphate to the fused aspartate transcarbamoylase domain. (5/437)

The first two steps of the de novo pyrimidine biosynthetic pathway in Saccharomyces cerevisiae are catalyzed by a 240-kDa bifunctional protein encoded by the ura2 locus. Although the constituent enzymes, carbamoyl phosphate synthetase (CPSase) and aspartate transcarbamoylase (ATCase) function independently, there are interdomain interactions uniquely associated with the multifunctional protein. Both CPSase and ATCase are feedback inhibited by UTP. Moreover, the intermediate carbamoyl phosphate is channeled from the CPSase domain where it is synthesized to the ATCase domain where it is used in the synthesis of carbamoyl aspartate. To better understand these processes, a recombinant plasmid was constructed that encoded a protein lacking the amidotransferase domain and the amino half of the CPSase domain, a 100-kDa chain segment. The truncated complex consisted of the carboxyl half of the CPSase domain fused to the ATCase domain via the pDHO domain, an inactive dihydroorotase homologue that bridges the two functional domains in the native molecule. Not only was the "half CPSase" catalytically active, but it was regulated by UTP to the same extent as the parent molecule. In contrast, the ATCase domain was no longer sensitive to the nucleotide, suggesting that the two catalytic activities are controlled by distinct mechanisms. Most remarkably, isotope dilution and transient time measurements showed that the truncated complex channels carbamoyl phosphate. The overall CPSase-ATCase reaction is much less sensitive than the parent molecule to the ATCase bisubstrate analogue, N-phosphonacetyl-L-aspartate (PALA), providing evidence that the endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site.  (+info)

Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius. Cloning, sequence analysis, enzyme purification and characterization. (6/437)

The genes coding for aspartate carbamoyltransferase (ATCase) in the extremely thermophilic archaeon Sulfolobus acidocaldarius have been cloned by complementation of a pyrBI deletion mutant of Escherichia coli. Sequencing revealed the existence of an enterobacterial-like pyrBI operon encoding a catalytic chain of 299 amino acids (34 kDa) and a regulatory chain of 170 amino acids (17.9 kDa). The deduced amino acid sequences of the pyrB and pyrI genes showed 27.6-50% identity with archaeal and enterobacterial ATCases. The recombinant S. acidocaldarius ATCase was purified to homogeneity, allowing the first detailed studies of an ATCase isolated from a thermophilic organism. The recombinant enzyme displayed the same properties as the ATCase synthesized in the native host. It is highly thermostable and exhibits Michaelian saturation kinetics for carbamoylphosphate (CP) and positive homotropic cooperative interactions for the binding of L-aspartate. Moreover, it is activated by nucleoside triphosphates whereas the catalytic subunits alone are inhibited. The holoenzyme purified from recombinant E. coli cells or present in crude extract of the native host have an Mr of 340 000 as estimated by gel filtration, suggesting that it has a quaternary structure similar to that of E. coli ATCase. Only monomers could be found in extracts of recombinant E. coli or Saccharomyces cerevisiae cells expressing the pyrB gene alone. In the presence of CP these monomers assembled into trimers. The stability of S. acidocaldarius ATCase and the allosteric properties of the enzyme are discussed in function of a modeling study.  (+info)

Functional linkage between the glutaminase and synthetase domains of carbamoyl-phosphate synthetase. Role of serine 44 in carbamoyl-phosphate synthetase-aspartate carbamoyltransferase-dihydroorotase (cad). (7/437)

Mammalian carbamoyl-phosphate synthetase is part of carbamoyl-phosphate synthetase-aspartate carbamoyltransferase-dihydroorotase (CAD), a multifunctional protein that also catalyzes the second and third steps of pyrimidine biosynthesis. Carbamoyl phosphate synthesis requires the concerted action of the glutaminase (GLN) and carbamoyl-phosphate synthetase domains of CAD. There is a functional linkage between these domains such that glutamine hydrolysis on the GLN domain does not occur at a significant rate unless ATP and HCO(3)(-), the other substrates needed for carbamoyl phosphate synthesis, bind to the synthetase domain. The GLN domain consists of catalytic and attenuation subdomains. In the separately cloned GLN domain, the catalytic subdomain is down-regulated by interactions with the attenuation domain, a process thought to be part of the functional linkage. Replacement of Ser(44) in the GLN attenuation domain with alanine increases the k(cat)/K(m) for glutamine hydrolysis 680-fold. The formation of a functional hybrid between the mammalian Ser(44) GLN domain and the Escherichia coli carbamoyl-phosphate synthetase large subunit had little effect on glutamine hydrolysis. In contrast, ATP and HCO(3)(-) did not stimulate the glutaminase activity, indicating that the interdomain linkage had been disrupted. In accord with this interpretation, the rate of glutamine hydrolysis and carbamoyl phosphate synthesis were no longer coordinated. Approximately 3 times more glutamine was hydrolyzed by the Ser(44) --> Ala mutant than that needed for carbamoyl phosphate synthesis. Ser(44), the only attenuation subdomain residue that extends into the GLN active site, appears to be an integral component of the regulatory circuit that phases glutamine hydrolysis and carbamoyl phosphate synthesis.  (+info)

Substitutions in the aspartate transcarbamoylase domain of hamster CAD disrupt oligomeric structure. (8/437)

Aspartate transcarbamoylase (ATCase; EC 2.1.3.2) is one of three enzymatic domains of CAD, a protein whose native structure is usually a hexamer of identical subunits. Alanine substitutions for the ATCase residues Asp-90 and Arg-269 were generated in a bicistronic vector that encodes a 6-histidine-tagged hamster CAD. Stably transfected mammalian cells expressing high levels of CAD were easily isolated and CAD purification was simplified over previous procedures. The substitutions reduce the ATCase V(max) of the altered CADs by 11-fold and 46-fold, respectively, as well as affect the enzyme's affinity for aspartate. At 25 mM Mg(2+), these substitutions cause the oligomeric CAD to dissociate into monomers. Under the same dissociating conditions, incubating the altered CAD with the ATCase substrate carbamoyl phosphate or the bisubstrate analogue N-phosphonacetyl-L-aspartate unexpectedly leads to the reformation of hexamers. Incubation with the other ATCase substrate, aspartate, has no effect. These results demonstrate that the ATCase domain is central to hexamer formation in CAD and suggest that the ATCase reaction mechanism is ordered in the same manner as the Escherichia coli ATCase. Finally, the data indicate that the binding of carbamoyl phosphate induces conformational changes that enhance the interaction of CAD subunits.  (+info)

*Aspartate carbamoyltransferase

... (also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine ... "2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate". ... Aspartate carbamoyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Two catalytic trimers and two regulatory dimers assemble to form an intermediate of aspartate carbamoyltransferase consisting ...

*Protomer

Aspartate carbamoyltransferase has a α6β6 subunit composition. The six αβ-protomers are arranged in D3 symmetry. Viral capsid ...

*Biosynthesis

Aspartate carbamoyltransferase condenses carbamoyl phosphate with aspartate to form uridosuccinate. Dihydroorotase performs ... 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 ... Aspartate semialdehyde dehydrogenase catalyzes the NADPH-dependent reduction of aspartyl phosphate to yield aspartate ...

*Don Craig Wiley

Noteworthy in this effort was that Wiley managed to grow crystals of aspartate carbamoyltransferase suitable for obtaining its ... There, Wiley did early work on the structure of aspartate carbamoyltransferase, the largest molecular structure determined at ... "Complex of aspartate carbamoyltransferase from Escherichia coli with its allosteric inhibitor, cytidine triphosphate: Electron ... "Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli". Journal of ...

*Cooperative binding

"Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli". Journal of ... Another enzyme that has been suggested early to bind ligands cooperatively is aspartate trans-carbamylase. Although initial ... Changeux, J. P.; Rubin, M. M. (1968). "Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental ...

*Cytidine triphosphate

CTP acts as an inhibitor of the enzyme aspartate carbamoyltransferase, which is used in pyrimidine biosynthesis. CTP synthase ...

*Allosteric enzyme

... coli enzyme aspartate carbamoyltransferase (ATCase) has become another good example of allosteric regulation. The kinetic ...

*ATCase/OTCase family

Aspartate carbamoyltransferase (ATCase) catalyses the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, ... aspartate carbamoyltransferase EC 2.1.3.2 and ornithine carbamoyltransferase EC 2.1.3.3. It has been shown that these enzymes ... Ke HM, Honzatko RB, Lipscomb WN (July 1984). "Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6- ... Ornithine carbamoyltransferase (OTCase) catalyses the conversion of ornithine and carbamoyl phosphate to citrulline. In mammals ...

*Nucleotide

Next, aspartate carbamoyltransferase catalyzes a condensation reaction between aspartate and carbamoyl phosphate to form ... This new carbon is modified by the additional of a third NH2 unit, this time transferred from an aspartate residue. Finally, a ... First, GTP hydrolysis fuels the addition of aspartate to IMP by adenylosuccinate synthase, substituting the carbonyl oxygen for ... Pyrimidines are synthesized first from aspartate and carbamoyl-phosphate in the cytoplasm to the common precursor ring ...

*Unikont

... aspartate carbamoyltransferase. This must have involved a double fusion, a rare pair of events, supporting the shared ancestry ...

*Raymond C. Stevens

"Crystal Structures of Aspartate Carbamoyltransferase Li gated with Phosphonoacetamide, Malonate and CTP or ATP at 2.8-A ... "Escherichia coli aspartate carbamoyltransferase: The probing of crystal structure analysis via site-specific mutagenesis," ... "Crystal structure of the Glu-239 to Gln mutant of aspartate carbamoyltransferase at 3.1 A resolution: An intermediate ... "Structural Consequences of Effector Binding to the T State of Aspartate Carbamoyltransferase Crystal Structures of the ...

*Thomas A. Steitz

Steitz made contributions to determining the atomic structures of carboxypeptidase A and aspartate carbamoyltransferase, each ... The structure of aspartate transcarbamylase, I. A molecular twofold axis in the complex with cytidine triphosphate. Proc Natl ...

*List of EC numbers (EC 2)

... aspartate carbamoyltransferase EC 2.1.3.3: ornithine carbamoyltransferase EC 2.1.3.4: deleted EC 2.1.3.5: oxamate ... putrescine carbamoyltransferase EC 2.1.3.7: 3-hydroxymethylcephem carbamoyltransferase EC 2.1.3.8: lysine carbamoyltransferase ... 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 ... aspartate transaminase EC 2.6.1.2: alanine transaminase EC 2.6.1.3: cysteine transaminase EC 2.6.1.4: glycine transaminase EC ...

*List of MeSH codes (D08)

... aspartate carbamoyltransferase MeSH D08.811.913.555.275.600 --- ornithine carbamoyltransferase MeSH D08.811.913.555.400 --- ... aspartate carbamoyltransferase MeSH D08.811.600.130 --- aspartokinase homoserine dehydrogenase MeSH D08.811.600.200 --- ... aspartate aminotransferases MeSH D08.811.913.477.700.225.249 --- aspartate aminotransferase, cytoplasmic MeSH D08.811.913.477. ... aspartate-tRNA ligase MeSH D08.811.464.263.200.250 --- glutamate-trna ligase MeSH D08.811.464.263.200.350 --- glycine-trna ...

*Opisthokont

... and aspartate carbamoyltransferase that is not present in plants, and plants have a fusion of thymidylate synthase and ...

*Transferase

Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P (Apr 1984). "Mechanism of action of aspartate ... "carbamoyltransferase". The Free Dictionary. Farlex, Inc. Retrieved 25 November 2013. "carbamoyl group (CHEBI:23004)". ChEBI: ... In ATCase such a transfer is written as Carbamyl phosphate + L-aspertate → {\displaystyle \rightarrow } L-carbamyl aspartate + ... Reichard P, Hanshoff G (1956). "Aspartate Carbamyl Transferase from Escherichia Coli" (PDF). Acta Chemica Scandinavica: 548-566 ...
A study of the sulfhydryl groups of the catalytic subunit of Escherichia coli aspartate transcarbamylase. The use of enzyme--5-thio-2-nitrobenzoate mixed disulfides as intermediates in modifying enzyme sulfhydryl groups ...
1AT1: Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-A resolution and neutral pH.
cAMP- and cGMP-dependent protein kinases (cAPK and cGPK). Both types of kinases contains two tandem copies of the cyclic nucleotide-binding domain. The cAPKs are composed of two different subunits: a catalytic chain and a regulatory chain which contains both copies of the domain. The cGPKs are single chain enzymes that include the two copies of the domain in their N- terminal section. The nucleotide specificity of cAPK and cGPK is due to an amino acid in the conserved region of β-barrel 7: a threonine that is invariant in cGPK is an alanine in most cAPK ...
A 20-year-old cow was presented due to chronic diarrhea and weight loss. The clinical examination revealed a markedly enlarged left ovary. However, a cause of the diarrhea could not observe. The examination of the feces was negative for a parasites or bacteria causing diarrhea. The results of hematological and biochemical analyses revealed a mild leucocytosis, bilirubinaemia, higher activities of the enzymes aspartate transaminase, gamma-glutamyltransferase and creatine kinase. The plasma concentrations of estrogen and testosterone were below the detection limits, progesterone concentration was 2.7 ng/ml. The postmortem examination revealed a bile ductule carcinoma with metastases in the lung and in lung and mestenterial lymph nodes. The cause of the tumor remained unclear. Diarrhea might have been the consequence of a portal hypertension due to the tumor. The pathological examination confirmed the clinical diagnosis of the ovarian tumor. The genesis of the ovarian tumor may be independent of ...
1B4X: The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.
p>An evidence describes the source of an annotation, e.g. an experiment that has been published in the scientific literature, an orthologous protein, a record from another database, etc.,/p> ,p>,a href="/manual/evidences">More…,/a>,/p> ...
PRKDC(protein kinase, DNA-activated, catalytic polypeptide),别名HYRC,p350,DNAPK, DNPK1, HYRC1, IMD26, XRCC7, DNA-PKcs,属于PI3/PI4-激酶家族,主要编码DNA依赖性蛋白激酶(DNA-PK)的催化亚基。PRKDC蛋白在结合两个小的调节亚基(Ku70和Ku80)后形成DNA-PK,而DNA-PK能够对断裂的双链DNA进行修复和损伤应答[1]。 PRKDC蛋白可维持端粒的稳定性,参与免疫蛋白质的位置特异性V(D)J重组反应[2]和逆转录病毒DNA的整合[3]。此外,PRKDC蛋白对c-myc蛋白稳定性起到调控作用,从而在一定程度上参与细胞的恶性转化过程[4]。 NBRI利用CRISPR/Cas9技术和囊胚注射技术,在PRKDC基因部分外显子上下游内含子上各设计一条gRNA,利用gRNA引导Cas9内切酶对DNA进行定点切割,从而删除-561bp,使该基因下游序列发生移码,同时保留了mouse ...
The massive, bizarre towers of the Pala group protrude from the stony alpine plateau. Climbing here in the southernmost mountain range of the Dolom...
The unikonts have a triple-gene fusion that is lacking in the bikonts. The three genes that are fused together in the unikonts, but not bacteria or bikonts, encode enzymes for synthesis of the pyrimidine nucleotides: carbamoyl phosphate synthase, dihydroorotase, aspartate carbamoyltransferase. This must have involved a double fusion, a rare pair of events, supporting the shared ancestry of Opisthokonta and Amoebozoa.. Cavalier-Smith[1] originally proposed that unikonts ancestrally had a single flagellum and single basal body. This is unlikely, however, as flagellated opisthokonts, as well as some flagellated Amoebozoa, including Breviata, actually have two basal bodies, as in typical bikonts (even though only one is flagellated in most unikonts). This paired arrangement can also be seen in the organization of centrioles in typical animal cells. In spite of the name of the group, the common ancestor of all unikonts was probably a cell with two basal bodies.. ...
I had a good summer studying Advanced Bacterial Genetics at Cold Spring Harbor Laboratory. The course was intense but very good. Research in the lab is centering around the thermodynamics of the transfer of iron from various chelators to bacterial siderophores, and learning more about bioinformatics and molecular modeling. Plans are also being made to get back to isolating and characterizing bacterial iron reductases.. Relevant Scholarly Activities. I am an active, ad hoc reviewer for the journal Archives of Biochemistry & Biophysics.. Attending STEM Conference for Educators, June 20 - 24, 2016, San Diego, CA.. ATP, Positive Heterotropic Interactions, and Allosteric Control of Fe3+ Release from Fe3+-Transferrin. Richard E. Cowart. Presented at the University of Iowa School of Medicine, Department of Biochemistry, June 6, 2015.. U.S. Patent No. 8,647,640, February 11, 2014. Vaccine Compositions and Methods of Use to Protect against Infectious Diseases. Richard E. Cowart, Inventor. A putative ...
Rabbit Polyclonal Anti-Ornithine Carbamoyltransferase Antibody. Validated: IHC, IHC-P. Tested Reactivity: Human, Mouse, Rat. 100% Guaranteed.
A Phase I clinical trial of N-(phosphonacetyl)-l-aspartate, an antimetabolite which inhibits a key enzyme in the de novo pathway of pyrimidine biosynthesis, was conducted. N-(Phosphonacetyl)-l-aspartate was given as an i.v. 15-min infusion once daily for five days; cycles of treatment were repeated every three weeks. Thirty-four patients received treatment. Dose-limiting toxicity was observed at 1500 to 2000 mg/sq m/day and was manifested by skin rash, diarrhea, and stomatitis. Rash and diarrhea usually began during the first week of treatment and persisted up to Day 17 of a cycle of therapy. No consistent hematopoietic, hepatic, or renal toxicity was observed. One partial response in a patient with colon carcinoma was seen and continues at more than eight months. Stable disease was observed in three patients with colon carcinoma, two patients with hypernephroma, one patient with pancreatic carcinoma, and one patient with melanoma. The predictability and reversibility of toxicity and the ...
MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPyrimidine ribonucleotide biosynthesisaspartate carbamoyltransferase (TIGR00670; EC 2.1.3.2; HMM-score: 120.5) ...
The tumor suppressor p53 is stabilized following the induction of deficiencies in nucleotide pool levels by antimetabolites. N-(phosphonacetyl)-L-aspartate (PALA) reversibly inhibits aspartate transcarbamylase, causing interruption of de novo pyrimidine synthesis; hydroxyurea (HU) reversibly inhibits ribonucleotide reductase, inhibiting the conversion of ribonucleotide triphosphates to deoxynucleotide triphosphates. When HCT116, a human colon carcinoma cell line, is treated with either HU or PALA, p53 accumulates and cells arrest in S-phase. Beyond these similarities, the cellular responses to PALA and HU are strikingly different. Chk1 is phosphorylated to a far greater extent in HU-treated HCT116 cells than following PALA treatment. The lack of Chk1 phosphorylation observed during PALA treatment was found to be due to the p53-dependent transcriptional activation of the Wip1 phosphatase, rather than the inactivity of ATR. Chromatin immunoprecipitation studies performed on PALA-treated cells ...
Ornithine Carbamoyltransferase Proteins available through Novus Biologicals. Browse our Ornithine Carbamoyltransferase Protein catalog backed by our Guarantee+.
CAD antibody (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) for ICC/IF, WB. Anti-CAD pAb (GTX28406) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
Curien G, Bastien O, Robert-Genthon M, Cornish-Bowden A, Cárdenas ML, Dumas R; Understanding the regulation of aspartate metabolism using a model based on measured kinetic parameters.; Mol Syst Biol, 2009 PubMed Europe PMC ...
In article ,03AA4458B49F028531 at MCOIARC.BITNET,, TAO%OPUS at MCOIARC.BITNET writes: , , , I am interested in getting hold of Genetic Technology Corportation, the maker , , of CAD GENE. The ads I had is old and the phone number is no longer in use. , , Could anyone in the netland offer some help? , , Tao , The address for CAD Gene is: CAD Gene Genetic Technology Corporation P.O. Box 1179 Kendall Square Cambridge, MA 02142 800-462-7179 508-879-0258 (This number is both a fax and an answering machine) Tomi M kel Dept. of Virology University of Helsinki tomakela at cc.helsinki.fi ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
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Potassium L-aspartate 14007-45-5 NMR spectrum, Potassium L-aspartate H-NMR spectral analysis, Potassium L-aspartate C-NMR spectral analysis ect.
ELKOS HEALTHCARE PRIVATE LIMITED - Manufacturer, Service Provider, Supplier, Trading Company of L-ornithine L-aspartate Injections based in Ambala Cantt, India
Maycardin K information about active ingredients, pharmaceutical forms and doses by Mayrhofer Pharmazeutika, Maycardin K indications, usages and related health products lists
Scientist John Northrop crystallized chymotrypsin in the early 1930s.. In the following years, other scientists contributed to the characterization ...
New treatments need to be developed for the significant human diseases of toxoplasmosis and malaria to circumvent problems with current treatments and drug resistance. Apicomplexan parasites causing these lethal diseases are deficient in pyrimidine salvage, suggesting that selective inhibition of de novo pyrimidine biosynthesis can lead to a severe loss of uridine 5-monophosphate (UMP) and thymidine 5-monophosphate (dTMP) pools, thereby inhibiting parasite RNA and DNA synthesis. Disruption of Toxoplasma gondii carbamoyl phosphate synthetase II (CPSII) induces a severe uracil auxotrophy with no detectable parasite replication in vitro and complete attenuation of virulence in mice. Here we show that a CPSII cDNA minigene efficiently complements the uracil auxotrophy of CPSII-deficient mutants, restoring parasite growth and virulence. Our complementation assays reveal that engineered mutations within, or proximal to, the catalytic triad of the N-terminal glutamine amidotransferase (GATase) domain ...
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Definition of heterotropic pregnancies. Provided by Stedmans medical dictionary and Drugs.com. Includes medical terms and definitions.
Plant based calcium aspartate anhydrous supplement absorbs at an unprescedented 92%. Helps to significantly improve bone joint and muscle health challenges. Absorption is Key!
From NCBI Gene:. The de novo synthesis of pyrimidine nucleotides is required for mammalian cells to proliferate. This gene encodes a trifunctional protein which is associated with the enzymatic activities of the first 3 enzymes in the 6-step pathway of pyrimidine biosynthesis: carbamoylphosphate synthetase (CPS II), aspartate transcarbamoylase, and dihydroorotase. This protein is regulated by the mitogen-activated protein kinase (MAPK) cascade, which indicates a direct link between activation of the MAPK cascade and de novo biosynthesis of pyrimidine nucleotides. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Apr 2015]. From UniProt: ...
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Looking for online definition of allosteric enzymes in the Medical Dictionary? allosteric enzymes explanation free. What is allosteric enzymes? Meaning of allosteric enzymes medical term. What does allosteric enzymes mean?
This chapter discusses the de novo pathway of pyrimidine nucleotide biosynthesis. Animals do not have a dietary requirement for pyrimidines, and many microorgan
Expression of the pyrC gene, which encodes the pyrimidine biosynthetic enzyme dihydroorotase, is negatively regulated by pyrimidine availability in Escherichia coli. To define the mechanism of this regulation, an essential regulatory region between the pyrC promoter and the initial codons of the pyrC structural gene was identified. Mutational analysis of this regulatory region showed that the formation of a hairpin at the 5 end of the pyrC transcript, which overlaps the pyrC ribosome binding site, is required for repression of pyrC expression. Formation of the hairpin appears to be controlled by nucleotide-sensitive selection of the site of pyrC transcriptional initiation. When the CTP level is high, the major pyrC transcript is initiated with this nucleotide at a position seven bases downstream of the pyrC -10 region. This transcript is capable of forming a stable hairpin at its 5 end. When the CTP level is low and the GTP level is high, conditions found in cells limited for pyrimidines, the ...
Carbamoylphosphate synthetase I deficiency (CPS1) Test Cost INR 30000.00 Surat Pune Jaipur Lucknow Kanpur Nagpur Visakhapatnam Indore Thane Bhopal Patna Vadodara Ghaziabad Ludhiana Coimbatore Madurai Meerut Ranchi Allahabad Trivandrum Pondicherry Mysore Aligarh best offer discount price
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Magnesium Potassium Aspartate 360 Capsules Magnesium and potassium aspartate is most readily absorbed by the body and are both key minerals that your body needs for muscles and nerve health.
Scarfolk is a town in North West England that did not progress beyond 1979. Instead, the entire decade of the 1970s loops ad infinitum. Here in Scarfolk, pagan rituals blend seamlessly with science; hauntology is a compulsory subject at school, and everyone must be in bed by 8pm because they are perpetually running a slight fever. "Visit Scarfolk today. Our number one priority is keeping rabies at bay." For more information please reread.. ...
InChI=1S/C10H18N4O6/c11-5(8(17)18)2-1-3-13-10(12)14-6(9(19)20)4-7(15)16/ h5-6H,1-4,11H2,(H,15,16)(H,17,18)(H,19,20)(H3,12,13,14)/t5-,6-/m0/s1 (InChI ...
Reissatessa on mukava maistella kaikkea jännää ja eksoottista, mitä kohdemaan keittiö tarjoaa. Ennakkoluulottomuus kannattaa, sillä niin voi löytää uusia suosikkeja. Välillä on kiva esitellä myös omaa ruokakulttuuria, mutta se ei ole aina niin helppoa.. Laskiaisen lähestyessä päätimmekin tehdä perinteisiä laskiaispullia. Matkaan tuli kuitenkin pari pikku muuttujaa. Hiiva ei kuulu vietnamilaiseen keittiöön, eikä sitä siis löytynyt mistään. Onneksi pomolla oli kotona iso purkki leivinjauhetta, jota laitettiin sekaan silmämääräisellä arviolla. Jauhojen kilohinta oli muuten noin 3 €, ihanan kallista. Kardemummaksi meille väietty mauste oli jotain aivan muuta, joten tällä kertaa pullat maustettiin suklaalla. Pullasudin virkaa toimitti pala leivinpaperia eikä raesokeriakaan ollut. Tämä ei innokasta apukokkiamme kuitenkaan lannistanut. Pieneen pöytämalliseen sähköuuniin mahtui kerrallaan viisi pullaa.. Onneksi mansikkahilloa ja kermavaahtoa löytyy ...
Rat liver ornithine carbamoyltransferase appears to be located exclusively in the mitochondria; the activity that is found in the soluble fraction is indistinguishable from mitochondrial ornithine carbamoyltransferase by simple kinetic criteria, and seems to result from breakage of mitochondria during homogenization. Of several rat tissues studied, only the liver and the mucosa of small intestine contain significant amounts of ornithine carbamoyltransferase; the activity in intestinal mucosa is less than one thousandth of that in liver. Qualitatively, this distribution coincides with that of carbamoyl phosphate synthetase I and its cofactor, acetylglutamate. The rat liver contents of carbamoyl phosphate and ornithine were 0.1 and 0.15μmol/g wet wt. of tissue respectively. On the basis of these values, it is proposed that in vivo the ornithine carbamoyltransferase activity of liver may be much lower than its maximal activity in vitro might suggest.. ...
Lysine biosynthesis is one of the unique metabolic capabilities of cyst forming Coccidia such as Toxoplasma gondii and Neospora caninum. Toxoplasma and Neospora genome analysis shows that they have the unique metabolic capability to synthesise lysine, an essential amino acid in humans. This capability is absent in other Apicomplexa. It has been suggested that Toxoplasma can convert aspartate into lysine via diaminopimelate pathway [1]. This pathway takes place via four different routes in different organisms (KEGG Lysine biosynthesis pathway). Of these, three variants belong to different groups of prokaryotes and the plant variant of the pathway was identified recently in Arabidopsis thaliana [2]. The first four enzymes (aspartate kinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase) and the last enzyme (diaminopimelate decarboxylase) is the same in all variants of the pathway and these five enzymes are present in T. gondii and N. caninum ...
The pyrimidine synthesis is a similar process than that of Purines(Purines Synthesis). In the de novo synthesis of Pyrimidines, the ring is synthesized first and then it is attached to a ribose-phosphate to for a pyrimidine nucleotide. Pyrimidine rings are assembled from bicarbonate, aspartate and Ammonia. The pyrimidine biosynthesis (de novo pyrimidine synthesis pathway) was […] ...
The mechanisms that regulate myosin II activity in SC and OL during myelination are not yet known. In SC, phosphorylation of the regulatory chain of myosin II (MLC2) is up-regulated at the onset of myelination and then down-regulated (Melendez-Vasquez et al., 2004), following the same pattern of Rho activation in peripheral nerve extracts (unpublished data). Our previous studies revealed an important role for ROCK during the initial events of PNS myelination, possibly by regulating the phosphorylation status of MLC (Melendez-Vasquez et al., 2004). However, inhibition of ROCK did not interfere with the wrapping of the axon, which suggests that another ROCK-independent mechanism controls the actual motor of SC adaxonal membrane progression around the axon. Our current study extends these initial observations and provides further evidence of the important role of polarized actomyosin contraction for SC myelin formation. Similar to our previous results with a ROCK-specific pharmacological inhibitor, ...
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.Allochthonous phosphate.(a) Beds of allochthonous.Figure 11.Hammer is 40 cm long.Unit 7Hammer is 45 cm long.Unit 9(a) Succession of phosphate cemented,allochthonous Figure 13.Pyri
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Magnesium Potassium Aspartate Reviews and other Reviews of Nutritional Supplements and Merchants Plus Related Resources Including a 2017 Buying Guide. Healthy Learning for Healthy Living.
Cevat K rma, Vecih Oduncu, Ali Cevat Tanalp, Ayhan Erkol, Cihan D ndar, Dicle S rma, K r at Tigen, Sel uk Pala, Ak n zgi, Muhsin T rkmen, Nihal zdemir, Hasan ...
The mechanism of release and the role of l-aspartate as a central neurotransmitter are controversial. A vesicular release mechanism for l-aspartate has been difficult to prove, as no vesicular l-aspartate transporter was identified until it was found that sialin could transport l-aspartate and l-glutamate when reconstituted into liposomes. We sought to clarify the release mechanism of l-aspartate and the role of sialin in this process by combining l-aspartate uptake studies in isolated synaptic vesicles with immunocyotchemical investigations of hippocampal slices. We found that radiolabeled l-aspartate was taken up into synaptic vesicles. The vesicular l-aspartate uptake, relative to the l-glutamate uptake, was twice as high in the hippocampus as in the whole brain, the striatum, and the entorhinal and frontal cortices and was not inhibited by l-glutamate. We further show that sialin is not essential for exocytosis of l-aspartate, as there was no difference in ATP-dependent l-aspartate uptake in ...
The mitochondrial enzyme encoded by this gene catalyzes synthesis of carbamoyl phosphate from ammonia and bicarbonate. This reaction is the first committed step of the urea cycle, which is important in the removal of excess urea from cells. The encoded protein may also represent a core mitochondrial nucleoid protein. Three transcript variants encoding different isoforms have been found for this gene. The shortest isoform may not be localized to the mitochondrion. Mutations in this gene have been associated with carbamoyl phosphate synthetase deficiency, susceptibility to persistent pulmonary hypertension, and susceptibility to venoocclusive disease after bone marrow transplantation.[provided by RefSeq, May 2010]
Ornithine transcarbamylase (OTC) Deficiency information including symptoms, diagnosis, misdiagnosis, treatment, causes, patient stories, videos, forums, prevention, and prognosis.
Potassium Magnesium (aspartate) Supports a number of physiologic functions, including cardiovascular health and muscle function Potassium and magnesium are essential for healthy nerve impulse function, muscle contraction, cardiovascular function, acid/alkaline balance and carbohydrate and nutrient metabolism. Magnesium also plays an important role in facilitating potassium utilization, helping to provide optimal support from this important combination. Potassium and magnesium provide key roles in heart, muscular, and nerve health. Supplement Facts: Amount Per Serving each vegetable capsule contains: potassium (aspartate) 99 mg. magnesium (aspartate) 70 mg. vitamin C (as ascorbyl palmitate) 8 mg. Directions: 1-4 capsules per day, in divided doses, with meals.
Orotic acid, first discovered in ruminant milk, is an intermediate in the pyrimidine biosynthesis pathway of animal cells. Its synthesis is initiated by the formation of carbamoyl phosphate (CP) in the cytoplasm, with ammonia derived from glutamine.
http://www.wisegeek.com/what-is-nucleotide-biosynthesis.htm Nucleotide biosynthesis is the process whereby nucleotides are created or synthesized. This process
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Drugs may be covered by multiple patents or regulatory protections. All trademarks and applicant names are the property of their respective owners or licensors. Although great care is taken in the proper and correct provision of this service, thinkBiotech LLC does not accept any responsibility for possible consequences of errors or omissions in the provided data. The data presented herein is for information purposes only. There is no warranty that the data contained herein is error free. thinkBiotech performs no independent verifification of facts as provided by public sources nor are attempts made to provide legal or investing advice. Any reliance on data provided herein is done solely at the discretion of the user. Users of this service are advised to seek professional advice and independent confirmation before considering acting on any of the provided information. thinkBiotech LLC reserves the right to amend, extend or withdraw any part or all of the offered service without notice. ...
Vecih Oduncu, Ayhan Erkol, Ali Cevat Tanalp, Cihan D ndar, brahim Halil Tanboga, Dicle S rma, Ali Karag z, Can Y cel Karabay, Ak n zgi, Sel uk Pala, K r at Tigen, Cevat K ...

Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase | PNASThree-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase | PNAS

Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase. J E Gouaux and W N ... The three-dimensional structure of the ternary complex of carbamoyl phosphate, succinate, and aspartate carbamoyltransferase ( ... L-Aspartate Association Contributes to Rate Limitation and Induction of the T -, R Transition in Escherichia coli Aspartate ... Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase ...
more infohttp://www.pnas.org/content/85/12/4205.long

Aspartate carbamoyltransferase - WikipediaAspartate carbamoyltransferase - Wikipedia

Aspartate carbamoyltransferase (also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine ... "2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate". ... Aspartate carbamoyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Two catalytic trimers and two regulatory dimers assemble to form an intermediate of aspartate carbamoyltransferase consisting ...
more infohttps://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase

pyrB - Aspartate carbamoyltransferase - Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) - pyrB gene & proteinpyrB - Aspartate carbamoyltransferase - Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) - pyrB gene & protein

Aspartate carbamoyltransferaseUniRule annotation. ,p>Manual validated information which has been generated by the UniProtKB ... sp,A5EKQ8,PYRB_BRASB Aspartate carbamoyltransferase OS=Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) OX=288000 GN=pyrB PE=3 ... Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.UniRule annotation. ,p>Manual validated information ... Aspartate transcarbamylaseUniRule annotation. ,p>Manual validated information which has been generated by the UniProtKB ...
more infohttp://www.uniprot.org/uniprot/A5EKQ8

pyrB - Aspartate carbamoyltransferase - Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637) - pyrB gene & proteinpyrB - Aspartate carbamoyltransferase - Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637) - pyrB gene & protein

sp,B8DRT6,PYRB_DESVM Aspartate carbamoyltransferase OS=Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637) OX=883 GN=pyrB PE ... N-carbamoyl-L-aspartate*Search proteins in UniProtKB for this molecule.. *Search chemical reactions in Rhea for this molecule. ... N-carbamoyl-L-aspartate*Search proteins in UniProtKB for this molecule.. *Search chemical reactions in Rhea for this molecule. ... Aspartate carbamoyltransferase. Desulfovibrio sp.. 325. UniRef90_B8DRT6. Aspartate carbamoyltransferase. Desulfovibrio sp. HK- ...
more infohttps://www.uniprot.org/uniprot/B8DRT6

aspartate carbamoyltransferase(EC 2.1.3.2) - Creative Enzymesaspartate carbamoyltransferase(EC 2.1.3.2) - Creative Enzymes

... also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine biosynthetic pathway. ATCase is ... Aspartate carbamoyltransferase (also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine ... L-aspartate transcarbamoylase; L-aspartate transcarbamylase; carbamoylaspartotranskinase; aspartate transcarbamylase; aspartate ... carbamylaspartotranskinase; aspartate transcarbamylase; aspartate carbamyltransferase; aspartic acid transcarbamoylase; ...
more infohttps://www.creative-enzymes.com/product/Aspartate-Carbamoyltransferase_12185.html

RCSB PDB - 3LXM: 2.00 Angstrom resolution crystal structure of a catalytic subunit of an aspartate carbamoyltransferase (pyrB)...RCSB PDB - 3LXM: 2.00 Angstrom resolution crystal structure of a catalytic subunit of an aspartate carbamoyltransferase (pyrB)...

2.00 Angstrom resolution crystal structure of a catalytic subunit of an aspartate carbamoyltransferase (pyrB) from Yersinia ... 2.00 Angstrom resolution crystal structure of a catalytic subunit of an aspartate carbamoyltransferase (pyrB) from Yersinia ... 2.00 Angstrom resolution crystal structure of a catalytic subunit of an aspartate carbamoyltransferase (pyrB) from Yersinia ...
more infohttps://www.rcsb.org/structure/3lxm

RCSB PDB 









- 8AT1: CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED WITH PHOSPHONOACETAMIDE, MALONATE, AND...RCSB PDB - 8AT1: CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED WITH PHOSPHONOACETAMIDE, MALONATE, AND...

Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A ... ASPARTATE CARBAMOYLTRANSFERASE (R STATE), CATALYTIC CHAIN A, C 310 Escherichia coli EC#: 2.1.3.2 IUBMB Mutation: E60Q, E147Q, ... ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN B, D 153 Escherichia coli Mutation: Q8G Gene Name(s): pyrI b4244 JW4203 ... CRYSTAL STRUCTURES OF ASPARTATE CARBAMOYLTRANSFERASE LIGATED WITH PHOSPHONOACETAMIDE, MALONATE, AND CTP OR ATP AT 2.8-ANGSTROMS ...
more infohttp://www.rcsb.org/pdb/explore/explore.do?structureId=8at1

Aspartate/ornithine carbamoyltransferase superfamily (IPR036901) | InterPro | EMBL-EBIAspartate/ornithine carbamoyltransferase superfamily (IPR036901) | InterPro | EMBL-EBI

Aspartate carbamoyltransferase (EC:2.1.3.2) (ATCase) catalyses the conversion of aspartate and carbamoyl phosphate to ... Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution.. Proc. Natl. Acad. Sci. U.S.A. ... Aspartate/ornithine carbamoyltransferase superfamily (IPR036901). Short name: Asp/Orn_carbamoylTrfase_sf Description. This ... Ornithine carbamoyltransferase (EC:2.1.3.3) (OTCase) catalyses the conversion of ornithine and carbamoyl phosphate to ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR036901

Aspartate carbamoyltransferase(pyrB) | Technique alternative | 01022855209 - Amoy TopeAspartate carbamoyltransferase(pyrB) | Technique alternative | 01022855209 - Amoy Tope

Baculovirus 01022855209 at Gentaur Acidiphilium cryptum Aspartate carbamoyltransferase (pyrB) Baculovirus ... aspartate carbamoyltransferase catalytic subunit; Aspartate carbamoyltransferase; aspartate carbamoyltransferase catalytic ... Aspartate carbamoyltransferase(pyrB) is a recombinant protein expressed in Baculovirus . The protein can be with or without a ... Order Acidiphilium cryptum Aspartate carbamoyltransferase pyrB -Baculovirus 01022855209 at Gentaur Acidiphilium cryptum ...
more infohttps://amoytope.com/catalog/9-mbs-recombinant/21374-acidiphilium-cryptum-aspartate-carbamoyltransferase-pyrb-baculovirus

Literature: Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain (IPR006131) | InterPro | EMBL-EBILiterature: Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain (IPR006131) | InterPro | EMBL-EBI

Literature: Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain (IPR006131). References used in this entry. The ... Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution.. Ke HM, Honzatko RB, Lipscomb WN ... Crystal structure of Sulfolobus acidocaldarius aspartate carbamoyltransferase in complex with its allosteric activator CTP.. De ... Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB).. Lerner CG, Switzer RL.. J. Biol. Chem. ...
more infohttps://www.ebi.ac.uk/interpro/entry/IPR006131/literature

SWISS-MODEL Repository | A0A5F1H3F9SWISS-MODEL Repository | A0A5F1H3F9

COMPLEX OF N-PHOSPHONACETYL-L-ASPARTATE WITH ASPARTATE CARBAMOYLTRANSFERASE. X-RAY REFINEMENT, AN.... Heteromer. P0A786; P0A7F3 ... Natural Source Aspartate Carbamoyltransferase in E.Coil (Ligand-free and Zinc-free). Heteromer. C3SF53; C3SF57; 4wto. 1-153. ... Aspartate carbamoyltransferase regulatory subunit UniProtKBInterProInteractive Modelling. 153 aa; Sequence (Fasta) 191 ... ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA). Heteromer. P0A786; P0A7F3; 6×ZN; 6×PAL;. 1d09. ...
more infohttps://swissmodel.expasy.org/repository/uniprot/A0A5F1H3F9

Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated...Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated...

... aspartate carbamoyltransferase, carbamoyl phosphate:l-aspartate carbamoyltransferase; EC 2.1.3.2), which catalyzes the first ... aspartate transcarbamoylase;. C trimer or subunit,. catalytic trimer or subunit;. PALA,. N-(phosphonacetyl)-l-aspartate;. T ... The lack of knowledge of the three-dimensional structure of the trimeric, catalytic (C) subunit of aspartate transcarbamoylase ... Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated ...
more infohttps://www.pnas.org/content/96/10/5388?ijkey=ee1ff39b4f00fda3733388d4060738a3107b542b&keytype2=tf_ipsecsha

SWISSPROT: PYRB PSEABSWISSPROT: PYRB PSEAB

DE RecName: Full=Aspartate carbamoyltransferase {ECO:0000255,HAMAP-Rule:MF_00001}; DE EC=2.1.3.2 {ECO:0000255,HAMAP-Rule:MF_ ... DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006207; P:de novo pyrimidine ... FT CHAIN 1 334 Aspartate carbamoyltransferase. FT /FTId=PRO_0000301607. SQ SEQUENCE 334 AA; 36629 MW; 2DC90450FA2E42E9 CRC64; ... 7:R90.1-R90.14(2006). CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate CC + N-carbamoyl-L-aspartate. { ...
more infohttp://pbil.univ-lyon1.fr/cgi-bin/acnuc-search-ac?query=ABJ15369&db=SWISSPROT&ident=ACNUC7421

Hemagglutinin (FXUY55TCP) by 3DBiologyHemagglutinin (FXUY55TCP) by 3DBiology

... on Shapeways. Learn more before you buy, or discover other cool products in Mathematical Art.
more infohttps://www.shapeways.com/product/FXUY55TCP/hemagglutinin?optionId=61399204

Principles of Biochemistry/Nucleic acid III: Sythesis of nucleotides - Wikibooks, open books for an open worldPrinciples of Biochemistry/Nucleic acid III: Sythesis of nucleotides - Wikibooks, open books for an open world

aspartic transcarbamolyase (aspartate carbamoyl transferase)[17]. carbamoyl aspartic acid. - dihhydroorotase[18]. ... As we have just seen, a six-step process links glycine, formate, bicarbonate, glutamine, and aspartate to lead to an ... the imidazoles carboxylate group phosphatises and adds aspartate. ... "Entrez Gene: CAD carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase". http://www.ncbi.nlm.nih.gov ...
more infohttps://en.wikibooks.org/wiki/Principles_of_Biochemistry/Nucleic_acid_III:_Sythesis_of_nucleotides

Targeting Purine and Pyrimidine Metabolism in Human Apicomplexan ParasitesTargeting Purine and Pyrimidine Metabolism in Human Apicomplexan Parasites

Aspartate carbamoyltransferase. cAMP. Cyclic AMP. CG. Cycloguanil. CoQ. Coenzyme Q. CPSII. Carbamoyl phosphate synthetase II. ... The other important enzymes in de novo UMP synthesis comprise aspartate carbamoyltransferase (ATCase; EC 2.1.3.2), which ...
more infohttp://pubmedcentralcanada.ca/pmcc/articles/PMC2720675/

KEGG BRITE: KEGG Orthology (KO) - Mycobacterium tuberculosis HaarlemKEGG BRITE: KEGG Orthology (KO) - Mycobacterium tuberculosis Haarlem

TBHG_01360 aspartate carbamoyltransferase PyrB TBHG_03365 glutamate decarboxylase GadB TBHG_02525 4-aminobutyrate ... 00250 Alanine, aspartate and glutamate metabolism [PATH:mtul00250] TBHG_01556 l-aspartate oxidase NadB TBHG_01519 L- ... aspartate carbamoyltransferase catalytic subunit [EC:2.1.3.2] K01580 E4.1.1.15; glutamate decarboxylase [EC:4.1.1.15] K07250 ... TBHG_00332 aspartate aminotransferase AspC TBHG_03646 2-isopropylmalate synthase K01754 E4.3.1.19; threonine dehydratase [EC: ...
more infohttp://www.genome.jp/kegg-bin/get_htext?mtul00001+TBHG_00332

Ghent University Academic BibliographyGhent University Academic Bibliography

Crystal structure of T state aspartate carbamoyltransferase of the hyperthermophilic archaeon Sulfolobus acidocaldarius. Dirk ...
more infohttps://biblio.ugent.be/publication?q=author%3D%22Remaut%2C+Han%22+or+

SCOPe 2.07: Structural Classification of Proteins - extendedSCOPe 2.07: Structural Classification of Proteins - extended

Compound: Aspartate carbamoyltransferase catalytic chain. Species: Escherichia coli [TaxId:83333]. Gene: pyrB, b4245, JW4204. ... Compound: Aspartate carbamoyltransferase regulatory chain. Species: Escherichia coli [TaxId:83333]. Gene: pyrI, b4244, JW4203. ... Compound: Aspartate carbamoyltransferase catalytic chain. Species: Escherichia coli [TaxId:83333]. Gene: pyrB, b4245, JW4204. ... Compound: Aspartate carbamoyltransferase regulatory chain. Species: Escherichia coli [TaxId:83333]. Gene: pyrI, b4244, JW4203. ...
more infohttp://scop.berkeley.edu/pdb/code=1rag

Protomer - WikipediaProtomer - Wikipedia

Aspartate carbamoyltransferase has a α6β6 subunit composition. The six αβ-protomers are arranged in D3 symmetry. ...
more infohttps://en.wikipedia.org/wiki/Protomer

KEGG BRITE: KEGG Orthology (KO) - Cricetulus griseus (Chinese hamster)KEGG BRITE: KEGG Orthology (KO) - Cricetulus griseus (Chinese hamster)

... aspartate carbamoyltransferase / dihydroorotase [EC:6.3.5.5 2.1.3.2 3.5.2.3] K01425 glsA; glutaminase [EC:3.5.1.2] K01425 glsA ... K14454 GOT1; aspartate aminotransferase, cytoplasmic [EC:2.6.1.1] K14455 GOT2; aspartate aminotransferase, mitochondrial [EC: ... aspartate aminotransferase, cytoplasmic [EC:2.6.1.1] K14455 GOT2; aspartate aminotransferase, mitochondrial [EC:2.6.1.1] K00814 ... 00250 Alanine, aspartate and glutamate metabolism [PATH:cge00250] 100762297 Got1; glutamic-oxaloacetic transaminase 1 100762838 ...
more infohttp://www.genome.jp/kegg-bin/get_htext?cge00001+100774486

Gentaur antibody-antibodies.com The Marketplace for AntibodiessGentaur antibody-antibodies.com The Marketplace for Antibodiess

Human Aspartate Carbamoyltransferase(ATCase)ELISA Kit. 96T. UB-E01250. Human Aspartate Carbamoyltransferase(ATCase)ELISA Kit. ... GO; GO:0070335; F:aspartate binding; IDA:BHF-UCL.. GO; GO:0004070; F:aspartate carbamoyltransferase activity; IDA:BHF-UCL.. GO ... Human Aspartate Carbamoyltransferase(ATCase)ELISA Kit. 96T. EIAAB11775. Dolichol-phosphate mannose synthase,Dolichol-phosphate ... RecName: Full=Aspartate carbamoyltransferase;. EC=2.1.3.2 {ECO:0000269,PubMed:9218000};. Includes:. RecName: Full= ...
more infohttps://www.antibody-antibodies.com/gene.php?title_uniprot=CAD+protein+%5BIncludes%3A+Glutamine-dependent+carbamoyl-phosphate+synthase+%28EC+6.3.5.5%29%3B+Aspartate+carbamoyltransferase+%28EC+2.1.3.2%29%3B+Dihydroorotase+%28EC+3.5.2.3%29%5D&uniprot_id=P08955

CAD: A Multifunctional Protein Leading De Novo Pyrimidine BiosynthesisCAD: A Multifunctional Protein Leading De Novo Pyrimidine Biosynthesis

Gouaux JE, Krause KL and Lipscomb WN (1987) The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a ... Role of serine 44 in carbamoyl‐phosphate synthetase‐aspartate carbamoyltransferase‐dihydroorotase (cad). Journal of Biological ... Qiu Y and Davidson JN (1998) Aspartate‐90 and arginine‐269 of hamster aspartate transcarbamylase affect the oligomeric state of ... aspartate carbamoyl transferase complex enzyme. Molecular & General Genetics 161 (3): 297-304.. Mally MI, Grayson DR and Evans ...
more infohttp://www.els.net/WileyCDA/ElsArticle/refId-a0027193.html

Fresh insights into the pyrimidine metabolism in the trypanosomatids | Parasites & Vectors | Full TextFresh insights into the pyrimidine metabolism in the trypanosomatids | Parasites & Vectors | Full Text

Nara T, Hirayama-Noguchi Y, Gao G, Murai E, Annoura T, Aoki T. Diversity of aspartate carbamoyltransferase genes of Trypanosoma ... Aspartate transcarbamoylase (ATCase). Aspartate transcarbamoylases (ATCases) in the trypanosomatids display a variety of ... Abbreviations: CPSII, carbamoyl-phosphate synthase; ATCase, aspartate carbamoyl transferase; DHOase, dihydroorotase; DHODH, ... ClATCase catalyzed reaction proceeded with a K m of 28.7 μM (for carbamoyl phosphate) and 2.6 μM (for aspartate), respectively ...
more infohttps://parasitesandvectors.biomedcentral.com/articles/10.1186/s13071-018-2660-8
  • In addition, physical chemical measurements of the change in quaternary structure and catalytic activation promoted by substoichiometric amounts of the bisubstrate analog ( 5 ), N -(phosphonacetyl)- L -aspartate (PALA), were interpreted readily in terms of the model ( 2 ). (pnas.org)
  • Publications] AOKI,Takashi: 'Purification and characterization of Leishmania mexicana aspartate carbamoyltransferase,the second enzyme of de novo pyrimidine biosynthesis' Bulletin de la Societe Francaise de Parasitologie. (nii.ac.jp)
  • Use of L-asparagine and N-phosphonacetyl-L-asparagine to investigate the linkage of catalysis and homotropic cooperativity in E. coli aspartate transcarbomoylase. (ebi.ac.uk)
  • Crystal structure of Sulfolobus acidocaldarius aspartate carbamoyltransferase in complex with its allosteric activator CTP. (ebi.ac.uk)