Aspartate Carbamoyltransferase
Ornithine Carbamoyltransferase
Dihydroorotase
Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
Carbamyl Phosphate
Cytidine Triphosphate
Phosphonoacetic Acid
Moritella
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
Allosteric Regulation
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
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).
Aspartate Aminotransferases
Phosphotransferases (Carboxyl Group Acceptor)
Ornithine-Oxo-Acid Transaminase
Carbamoyl-Phosphate Synthase (Ammonia)
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
Arginase
Sodium Benzoate
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.
Transaminases
Amino Acid Sequence
Pyrococcus furiosus
Argininosuccinate Synthase
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)
Molecular-structure of bacillus-subtilis aspartate transcarbamoylase at 3.0-a resolution
regulation of purine and pyrimidine biosynthesis
Phylogenetic Analysis and Protein Modeling of Plasmodium falciparum Aspartate Transcarbamoylase (ATCase)<...
Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain superfamily
Studies on the heterotropic interaction of hemoglobin. II. Role of beta-146 and beta-2 histidines in the alkaline Bohr effect. ...
Toxicology and Cancer Biology
RCSB PDB - 1I5O: CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE
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RCSB PDB
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Relaxation Spectra of Aspartate Transcarbamylase. Interaction of the Native Enzyme with Carbamyl Phosphate - 指紋
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PROSITE
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Ornithine Carbamoyltransferase Antibody (NBP1-88121): Novus Biologicals
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CDH15 Gene - GeneCards | CAD15 Protein | CAD15 Antibody
Controlled proteolysis of the multifunctional protein that ini...
SA RS05760 - AureoWiki
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Human CAD Antibody
Human CAD Antibody
anti-CAD antibody | GeneTex
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Ornithine transcarbamylase
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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) Portal: Biology (CS1 ... Two catalytic trimers and two regulatory dimers assemble to form an intermediate of aspartate carbamoyltransferase consisting ...
William Lipscomb
Aspartate carbamoyltransferase performs a step in building the pyrimidine nucleotides (cytosine and thymidine). Aspartate ... as activator and inhibitor molecules attach to aspartate carbamoyltransferase to speed it up and to slow it down. Aspartate ... Aspartate carbamoyltransferase. (right) was the second protein structure from Lipscomb's group. For a copy of DNA to be made, a ... Aspartate carbamoyltransferase was a much larger molecule than anything solved previously. Leucine aminopeptidase, (left) a ...
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 ...
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 JP, Rubin MM (February 1968). "Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of ...
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 ...
Nucleotide
Next, aspartate carbamoyltransferase catalyzes a condensation reaction between aspartate and carbamoyl phosphate to form ... This new carbon is modified by the addition 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 ...
Pyrimidine metabolism
... aspartate carbamoyltransferase and dihydroorotase. Dihydroorotate dehydrogenase (DHODH) unlike CAD and UMPS is a mono- ... "Entrez Gene: CAD carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase". "Entrez Gene: DHODH ...
Amorphea
... 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 ...
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 ...
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 ... N-succinylornithine carbamoyltransferase EC 2.1.3.13: The enzyme has been replaced by EC 6.1.2.2 EC 2.1.3.14: The enzyme has ... 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: ...
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 - cholesterol ... 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 ligase ...
Opisthokont
... and aspartate carbamoyltransferase that is not present in plants, and plants have a fusion of thymidylate synthase and ...
Transferase
In ATCase such a transfer is written as carbamoyl phosphate + L-aspartate → {\displaystyle \rightarrow } L-carbamoyl aspartate ... "carbamoyltransferase". The Free Dictionary. Farlex, Inc. Retrieved 25 November 2013. "carbamoyl group (CHEBI:23004)". ChEBI: ... Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P (Apr 1984). "Mechanism of action of aspartate ... Reichard P, Hanshoff G (1956). "Aspartate Carbamyl Transferase from Escherichia coli" (PDF). Acta Chemica Scandinavica. 10: 548 ...
Ornithine transcarbamylase
Rat ends with Ser, bovine with aspartate, and human with glycine. The human OTC gene is located on the short arm of chromosome ... Strautnieks S, Rutland P, Malcolm S (December 1991). "Arginine 109 to glutamine mutation in a girl with ornithine carbamoyl transferase ... Ornithine transcarbamylase (OTC) (also called ornithine carbamoyltransferase) is an enzyme (EC 2.1.3.3) that catalyzes the ... "The crystal structures of ornithine carbamoyltransferase from Mycobacterium tuberculosis and its ternary complex with carbamoyl ...
Postpartum psychosis
Cases have been described in carbamoyl phosphate synthetase 1, argino-succinate synthetase and ornithine carbamoyltransferase ... Postpartum anti-N-methyl-D-aspartate receptor encephalitis: a case report and literature review. Internal Medicine 56: 357-362 ...
2014 Ju-Jitsu World Championships
The 2014 Ju-Jitsu World Championship were the 12th edition of the Ju-Jitsu World Championships, and were held in Paris, France from November 28 to November 30, 2014. 28.11.2014 - Men's and Women's Fighting System, Men's and Women's Jiu-Jitsu (ne-waza), Men's Duo System - Classic 29.11.2014 - Men's and Women's Fighting System, Men's and Women's Jiu-Jitsu (ne-waza), Women's Duo System - Classic 30.11.2014 - Men's Jiu-Jitsu (ne-waza), Mixed Duo System - Classic, Team event Vincent MATCZAK (2014-09-30). "4TH INVITAION TO WORLD CHAMPIONSHIP 2014" (PDF). Retrieved 2019-11-28.[dead link] Online results Official results (PDF) Mixed team event results (PDF) (All articles with dead external links, Articles with dead external links from April 2022, Ju-Jitsu World Championships, 2014 in French sport ...
Bolley Johnson
Bolley L. "Bo" Johnson (born November 15, 1951) is an American politician from the state of Florida. A member of the Democratic Party, Johnson was a member of the Florida House of Representatives, and served as the Speaker of the Florida House of Representatives. Johnson is from Milton, Florida. His father and grandfather served as county commissioners for Santa Rosa County, Florida. Johnson graduated from Milton High School, and became the first member of his family to attend college. He received his bachelor's degree from Florida State University. Johnson volunteered for Mallory Horne when Horne served as the president of the Florida Senate. At the age of 22, Johnson met Lawton Chiles, then a member of the United States Senate, who hired him as a legislative aide in 1973. Johnson was elected to the Florida House of Representatives, representing the 4th district from November 7, 1978 to November 3, 1992. He also served the 1st district from November 3, 1992 to November 8, 1994. He became the ...
Don't Say No
... may refer to: Don't Say No (Billy Squier album), a 1981 album by American rock singer Billy Squier, and its title track Don't Say No (Seohyun EP), a 2016 extended play by South Korean pop singer Seohyun, and its title track "Don't Say No" (Tom Tom Club song), from the 1988 album Boom Boom Chi Boom Boom "Don't Say No", by Robbie Williams from the 2005 album Intensive Care "Don't Say No Tonight", a 1985 single by Eugene Wilde This disambiguation page lists articles associated with the title Don't Say No. If an internal link led you here, you may wish to change the link to point directly to the intended article. (Disambiguation pages with short descriptions, Short description is different from Wikidata, All article disambiguation pages, All disambiguation pages, Disambiguation pages ...
Dewoitine D.371
The Dewoitine 37 was the first of a family of 1930s French-built monoplane fighter aircraft. The D.37 was a single-seat aircraft of conventional configuration. Its fixed landing gear used a tailskid. The open cockpit was located slightly aft of the parasol wing. The radial engine allowed for a comparatively wide fuselage and cockpit. Design of this machine was by SAF-Avions Dewoitine but owing to over work at that companies plant at the time, manufacture of the D.37/01 was transferred to Lioré et Olivier. They were high-wing monoplanes of all-metal construction with valve head blisters on their engine cowlings. The first prototype flew in October 1931. Flight testing resulted in the need for multiple revisions in both engine and airframe, so it was February 1934 before the second prototype flew. Its performance prompted the French government to order for 28 for the Armée de l'Air and Aéronavale. The Lithuanian government ordered 14 that remained in service with their Air Force until 1936, ...
Noor-ul-Ain
The Noor-ul-Ain (Persian: نور العين, lit. 'the light of the eye') is one of the largest pink diamonds in the world, and the centre piece of the tiara of the same name. The diamond is believed to have been recovered from the mines of Golconda, Hyderabad in India. It was first in possession with the nizam Abul Hasan Qutb Shah, later it was given as a peace offering to the Mughal emperor Aurangazeb when he defeated him in a siege. It was brought into the Iranian Imperial collection after the Persian king Nader Shah Afshar looted Delhi in the 18th century.[citation needed] The Noor-ul-Ain is believed to have once formed part of an even larger gem called the Great Table diamond. That larger diamond is thought to have been cut in two, with one section becoming the Noor-ul-Ain and the other the Daria-i-Noor diamond. Both of these pieces are currently part of the Iranian Crown Jewels. The Noor-ul-Ain is the principal diamond mounted in a tiara of the same name made for Iranian Empress Farah ...
Benoist Land Tractor Type XII
The Benoist Land Tractor Type XII was one of the first enclosed cockpit, tractor configuration aircraft built. Benoist used "Model XII" to several aircraft that shared the same basic engine and wing design, but differed in fuselage and control surfaces. The Type XII was a tractor-engined conversion of the model XII headless pusher aircraft that resembled the Curtiss pusher aircraft. Demonstration pilots used Benoist aircraft to demonstrate the first parachute jumps, and the tractor configuration was considered much more suitable for the task. The first example named the "Military Plane" had a small box frame covered fuselage that left the occupants mostly exposed to the wind. The later model XII "Cross Country Plane" had a full fuselage that occupants sat inside of. The first tractor biplane used a wooden fuselage with a small seat on top. The wings were covered with a Goodyear rubberized cloth. The first model XII was built in the spring of 1912. On 1 March 1912, Albert Berry used a headless ...
Santa Cruz Barillas
... (also known as Yalmotx in Qʼanjobʼal) is a town, with a population of 17,166 (2018 census), and a municipality in the Guatemalan department of Huehuetenango. It is situated at 1450 metres above sea level. It covers a terrain of 1,174 km². The annual festival is April 29-May 4. Barillas has a tropical rainforest climate (Af) with heavy to very heavy rainfall year-round and extremely heavy rainfall from June to August. Citypopulation.de Population of departments and municipalities in Guatemala Citypopulation.de Population of cities & towns in Guatemala "Climate: Barillas". Climate-Data.org. Retrieved July 26, 2020. Muni in Spanish Website of Santa Cruz Barillas Coordinates: 15°48′05″N 91°18′45″W / 15.8014°N 91.3125°W / 15.8014; -91.3125 v t e (Articles with short description, Short description is different from Wikidata, Pages using infobox settlement with no coordinates, Articles containing Q'anjob'al-language text, Coordinates on Wikidata, ...
Maria Margaret Pollen
Maria Margaret La Primaudaye Pollen (10 April 1838 - c. 1919), known as Minnie, was a decorative arts collector. As Mrs John Hungerford Pollen, she became known during the early-twentieth century as an authority on the history of textiles, publishing Seven Centuries of Lace in 1908. Maria Margaret La Primaudaye was born into a Huguenot family on 10 April 1838, the third child of the Revd Charles John La Primaudaye, a descendant of Pierre de La Primaudaye. She was educated in Italy. Her family converted to Catholicism in 1851, and it was in Rome that her father met another recent English convert, John Hungerford Pollen, previously an Anglican priest and a decorative artist. She became engaged to Pollen, who was then seventeen years her senior, in the summer of 1854, and was married in the church of Woodchester monastery, near Stroud, Gloucester, on 18 September 1855. The Pollens initially settled in Dublin, where John Hungerford Pollen had been offered the professorship of fine arts at the ...
Ronald Fogleman
Ronald Robert Fogleman (born January 27, 1942) is a retired United States Air Force general who served as the 15th Chief of Staff of the Air Force from 1994 to 1997 and as Commanding General of the United States Transportation Command from 1992 to 1994. A 1963 graduate from the United States Air Force Academy, he holds a master's degree in military history and political science from Duke University. A command pilot and a parachutist, he amassed more than 6,800 flying hours in fighter, transport, tanker and rotary wing aircraft. He flew 315 combat missions and logged 806 hours of combat flying in fighter aircraft. Eighty of his missions during the Vietnam War were as a "Misty FAC" in the F-100F Super Sabre at Phù Cát Air Base, South Vietnam between 25 December 1968 and 23 April 1969. Fogleman was shot down in Vietnam in 1968, while piloting an F-100. He was rescued by clinging to an AH-1 Cobra attack helicopter that landed at the crash site. In early assignments he instructed student pilots, ...
Peachtree Street (song)
Peachtree Street" is a 1950 song co-written and recorded by Frank Sinatra in a duet with Rosemary Clooney. The song was released as a Columbia Records single. Frank Sinatra co-wrote the song with Leni Mason and Jimmy Saunders. Mason composed the music while Sinatra and Saunders wrote the lyrics. The song was arranged by George Siravo The song was released as an A side Columbia 10" 78 single, Catalog Number 38853, Matrix Number CO-43100-1 and as a 7" 33, 1-669. The B side was the re-issued "This Is the Night." Neither of the songs charted. The subject of the song is a stroll down the street in Atlanta, Georgia of the same name. Sinatra originally intended Dinah Shore to sing the duet with him. When Shore declined, Clooney was asked. The song was recorded on April 8, 1950. The song features spoken asides by Sinatra and Clooney. Rosemary Clooney asks: "Say, Frank, you wanna take a walk?" Frank Sinatra replies: "Sure, sweetie, just pick a street." He noted how there were no peach trees on the ...
We, Too, Have a Job to Do
... is a painting by American illustrator Norman Rockwell that depicts a Boy Scout in full uniform standing in front of a waving American flag. It was originally created by Rockwell in 1942 for the 1944 Brown & Bigelow Boy Scout Calendar. The model, Bob Hamilton, won a contest to be in the painting and personally delivered a print to the Vice President of the United States at the time, Henry A. Wallace. The painting was created to encourage Scouts to participate in the war effort during World War II. The name of the painting, We, Too, Have a Job to Do, comes from a slogan that the Boy Scouts of America used in 1942 to rally scouts to support the troops by collecting metal and planting victory gardens. The model, Bob Hamilton, won a contest with his local council in Albany, New York, to be depicted in the painting. He traveled to Rockwell's studio in Arlington, Vermont, to model for Rockwell. Since Hamilton was a scout, the uniform shown in the painting was his, unlike some ...
CATH Superfamily 3.30.70.140
SWISS-MODEL Template Library | 2yfk
Sol Genomics Network
HOMD :: SEQF2940
Aspartate carbamoyltransferase. 155. SEQF2940,KI515728.1. SEQF2940_00158 jb [NA] [AA] 609/202. 164974-164366. Bifunctional ... 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 ...
HOMD :: SEQF2888
aspartate carbamoyltransferase. 170. SEQF2888,AENP01000030.1. EFR32309.1 jb [NA] [AA] 186/61. 4120-3935. conserved hypothetical ... aspartate carbamoyltransferase regulatory chain%2C allosteric domain protein. 95. SEQF2888,AENP01000030.1. EFR32234.1 jb [NA] [ ... putative aspartate transaminase. 119. SEQF2888,AENP01000030.1. EFR32258.1 jb [NA] [AA] 1398/465. 12295-10898. ABC transporter% ...
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
DeCS
Aspartate carbamoyltransferase Entry term(s):. Aspartate Transcarbamylase. Carbamoyltransferase, Aspartate. Co(II)-Aspartate ... Aspartate Carbamoyltransferase Entry term(s). Aspartate Transcarbamylase Carbamoyltransferase, Aspartate Transcarbamylase, ... Aspartate Carbamoyltransferase - Preferred Concept UI. M0001827. Scope note. An enzyme that catalyzes the conversion of ... An enzyme that catalyzes the conversion of carbamoyl phosphate and L-aspartate to yield orthophosphate and N-carbamoyl-L- ...
Code System Concept
Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue<...
L-aspartate carbamoyltransferase, EC 2.1.3.2); such modification eliminates cooperativity, feedback inhibition, and enzymatic ... L-aspartate carbamoyltransferase, EC 2.1.3.2); such modification eliminates cooperativity, feedback inhibition, and enzymatic ... L-aspartate carbamoyltransferase, EC 2.1.3.2); such modification eliminates cooperativity, feedback inhibition, and enzymatic ... L-aspartate carbamoyltransferase, EC 2.1.3.2); such modification eliminates cooperativity, feedback inhibition, and enzymatic ...
IMSEAR at SEARO: Search
HOMD :: SEQF1950
List of EC numbers (EC 2)
aspartate carbamoyltransferase. *: ornithine carbamoyltransferase. *: deleted. *: oxamate carbamoyltransferase. *: putrescine ... 3-hydroxymethylcephem carbamoyltransferase. *: lysine carbamoyltransferase. *: N-acetylornithine carbamoyltransferase. EC 2.1.4 ... aspartate kinase. *: now EC 6.3.4.16. *: formate kinase. *: butyrate kinase. *: acetylglutamate kinase. *: now EC 6.3.5.5. *: ... aspartate transaminase. *: alanine transaminase. *: cysteine transaminase. *: glycine transaminase. *: tyrosine transaminase. ...
"sequence id","alias","species","description",...
"Probable aspartate carbamoyltransferase PyrB (ATCase) (aspartate transcarbamylase) [Ensembl]. Aspartate/ornithine ... ","ornithine carbamoyltransferase 2, chain F; CP4-6 prophage [Ensembl]. Aspartate/ornithine carbamoyltransferase [Interproscan ... ","aspartate 1-decarboxylase [Ensembl]. Aspartate decarboxylase [Interproscan].","protein_coding" "CPC67168","asp3"," ... ","Probable L-aspartate oxidase NadB [Ensembl]. FAD binding domain, Fumarate reductase flavoprotein C-term [Interproscan]."," ...
nadB protein (Pseudomonas aeruginosa) - STRING interaction network
Aspartate carbamoyltransferase catalytic subunit; Asp_carb_tr: aspartate carbamoyltransferase; Belongs to the ATCase/OTCase ... Aspartate carbamoyltransferase catalytic subunit; Asp_carb_tr: aspartate carbamoyltransferase; Belongs to the ATCase/OTCase ... Aspartate carbamoyltransferase catalytic subunit; Asp_carb_tr: aspartate carbamoyltransferase; Belongs to the ATCase/OTCase ... L-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate (538 aa). ...
Network Portal - Gene VNG2302G
RCSB PDB - 6PNZ: The structure of the Aspartate Transcarbamoylase trimer from Staphylococcus aureus complexed with PALA at 2.27...
The structure of the Aspartate Transcarbamoylase trimer from Staphylococcus aureus complexed with PALA at 2.27 Resolution. ... Aspartate carbamoyltransferase. A, B, C. 293. Staphylococcus aureus subsp. aureus COL. Mutation(s): 0 Gene Names: pyrB, ... The structure of the Aspartate Transcarbamoylase trimer from Staphylococcus aureus complexed with PALA at 2.27 Resolution.. * ... The structure of the Aspartate Transcarbamoylase trimer from Staphylococcus aureus complexed with PALA at 2.27 Resolution.. ...
SPRINT==| Query Results
ASPARTATE TRANSCARBAMYLASE) (ATCASE) - ESCHERICHIA COLI. PYRB_LACLE ASPARTATE CARBAMOYLTRANSFERASE (EC 2.1.3.2) (ASPARTATE ... ASPARTATE TRANSCARBAMYLASE) (ATCASE) - PSEUDOMONAS PUTIDA. PYRB_PYRAB ASPARTATE CARBAMOYLTRANSFERASE (EC 2.1.3.2) (ASPARTATE ... ASPARTATE TRANSCARBAMYLASE) (ATCASE) - SERRATIA MARCESCENS. PYRB_SULSO ASPARTATE CARBAMOYLTRANSFERASE (EC 2.1.3.2) (ASPARTATE ... ASPARTATE TRANSCARBAMYLASE) (ATCASE) - BACILLUS CALDOLYTICUS. PYRB_BACSU ASPARTATE CARBAMOYLTRANSFERASE (EC 2.1.3.2) (ASPARTATE ...
Faculty Publications Archive | Page 56 | Lewis-Sigler Institute
Aspartate Carbamoyltransferase. J. D. Rabinowitz, Hsiao, J. J., Gryncel, K. R., Kantrowitz, E. R., Feng, X. - J., Li, G., and ... nucleotide regulation of aspartate transcarbamoylase.", Biochemistry, vol. 47, no. 21, pp. 5881-8, 2008.*Google Scholar ... nucleotide regulation of aspartate transcarbamoylase.", Biochemistry, vol. 47, no. 21, pp. 5881-8, 2008.*Google Scholar ... nucleotide regulation of aspartate transcarbamoylase.", Biochemistry, vol. 47, no. 21, pp. 5881-8, 2008.*Google Scholar ...
YJR139C 267.488705 INESSENTIAL HOM6 "Homoserine dehydrogenase (L-homoserine:NADP oxidoreductase),5-amino-6-(5...
... aspartate transcarbamylase, and glutamine amidotransferase,aspartate carbamoyltransferase, " YOL163W 0.836745 INESSENTIAL " ... "aspartate aminotransferase, mitochondrial, aspartate catabolism, aspartate aminotransferase, mitochondrion" YJR128W 9.031074 ... "Ornithine carbamoyltransferase, arginine biosynthesis*, ornithine carbamoyltransferase, cytosol" YLR040C -4.104693 INESSENTIAL ... aspartate--tRNA ligase, mitochondrion" YFL019C -5.080596 INESSENTIAL "biological_process unknown, molecular_function unknown ...
metabolism
Studies of aspartate carbamoyltransferase have revealed that the affinity of this enzyme for its substrate (aspartate) is ... If a cell contains sufficient pyrimidine nucleotides (e.g., UTP), aspartate carbamoyltransferase, the first enzyme of ... the interaction of aspartate carbamoyltransferase with the different nucleotides provides an explanation for the control of the ... The first step in the synthesis of pyrimidine nucleotides is that catalyzed by aspartate carbamoyltransferase [70a]. This step ...
PathBank
In a subsequent cyclization reaction, the enzyme Aspartate carbamoyltransferase forms N-carbamoyl-aspartate which is converted ... Next, aspartate undergoes a condensation reaction with carbamoyl-phosphate to form orotic acid. ... The key regulatory enzymes directly associated with citrate production in the prostate cells are mitochondrial aspartate ...
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
Búsqueda | Portal Regional de la BVS
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
MESH TREE NUMBER CHANGES - 2014 MeSH. July 29, 2013
Ornithine8
- 3. HUYGEN, R., CRABEEL, M. AND GLANSDORFF, N. Nucleotide sequence of the ARG3 gene of the yeast Saccharomyces cerevisiae encoding ornithine carbamoyltransferase. (130.88.97)
- AOTCASE is a 4-element fingerprint that provides a signature for the ornithine/aspartate carbamoyltransferase superfamily. (130.88.97)
- O87319 ORNITHINE CARBAMOYLTRANSFERASE - NOSTOC PCC73102. (130.88.97)
- These enzymes catalyze the transfer of a particular group from one substrate to another e.g., aspartate amino transferase (AST), alanine aminotransferase (ALT), hexokinase, phosphoglucomutase, hexose- 1-phosphate uridyltransferase, ornithine carbamoyl transferase etc. (amano-enzyme.com)
- The urea cycle enzymes ornithine carbamoyltransferase and arginase are also found in the mitochondria, whereas the cytoplasm contains argininosuccinate synthetase and argininosuccinate lyase. (vedantu.com)
- In vivo, it forms 2 active metabolites: aspartate and ornithine, which have a short T1 / 2 of 0.3 0.4 h, are excreted by the kidneys through the urea cycle. (drdoping.com)
- Another nitrogen is added from aspartate, producing the denitrogenated fumarate, and the resulting arginine (a guanidinium compound) is hydrolysed back to ornithine, producing urea. (selfdecode.com)
- The nitrogens of urea come from the ammonia and aspartate, and the nitrogen in ornithine remains intact. (selfdecode.com)
Transcarbamylase1
- Landfear, SM , Evans, DR & Lipscomb, WN 1978, ' Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue ', Proceedings of the National Academy of Sciences of the United States of America , vol. 75, no. 6, pp. 2654-2658. (elsevier.com)
Transcarbamoylase1
- 6PNZ: The structure of the Aspartate Transcarbamoylase trimer from Staphylococcus aureus complexed with PALA at 2.27 Resolution. (rcsb.org)
Carbamoyl phosphate2
- An enzyme that catalyzes the conversion of carbamoyl phosphate and L-aspartate to yield orthophosphate and N-carbamoyl-L-aspartate. (bvsalud.org)
- Next, aspartate undergoes a condensation reaction with carbamoyl-phosphate to form orotic acid. (pathbank.org)
Aminotransferase1
- The key regulatory enzymes directly associated with citrate production in the prostate cells are mitochondrial aspartate aminotransferase, pyruvate dehydrogenase, and mitochondrial aconitase. (pathbank.org)
Citrulline1
- Argininosuccinate synthase combines with citrulline and aspartate to generate argininosuccinate. (vedantu.com)
Enzyme2
- In a subsequent cyclization reaction, the enzyme Aspartate carbamoyltransferase forms N-carbamoyl-aspartate which is converted into dihydroorotic acid by Dihydroorotase. (pathbank.org)
- In fact, the origins of the word "Enzyme" derive from Greek: "en" (in) and "zyme" (ferment). (amano-enzyme.com)
Form1
- A small part of aspartate is excreted by the kidneys in unchanged form. (drdoping.com)
Formation1
- aspartate carbamoyltransferase catalyses the formation of carbamoyl-aspartate, the commitment step in the pyrimidine biosynthetic pathway. (130.88.97)
Ornithine carbamoyltransferase2
- Serum levels of total bilirubin and one or more cytoplasmic enzymes including alanine aminotransferase, aspartate aminotransferase, ornithine carbamoyltransferase, and/or sorbitol dehydrogenase in males and females receiving 300 mg/kg were higher than those of controls. (nih.gov)
- Aspartate carbamoyltransferase, dihydroorotase, and the arginine pathway enzyme, ornithine carbamoyltransferase, remained constant during the growth cycle but showed a sharp decrease in activity after entering the stationary phase. (microbiologyresearch.org)
Pyrimidine2
- PYRB is an aspartate carbamoyltransferase catalyzing the second step in the de novo pyrimidine ribonucleotide biosynthesis. (phytoab.com)
- Derepression studies carried out by starving individual pyrimidine (Pyr − ) deletion mutants for uracil showed that the extent of derepression obtained for aspartate carbamoyltransferase, dihydroorotase and dihydroorotate dehydrogenase depended on the location of the pyr gene mutation. (microbiologyresearch.org)
Pathway1
- Aspartate carbamoyltransferase showed the greatest degree of derepression of the six enzymes studied, with pyrA strains (blocked in the first step of the pathway) showing about twice as much derepression as pyrF strains (blocked in the sixth step of the pathway). (microbiologyresearch.org)
Type1
- Vmax of the proteolytically cleaved trimer (CPC) is 75% that of the wild-type C trimer, whereas Km for aspartate and Kd for the bisubstrate analog, N-(phosphonacetyl)-L-aspartate, are increased about 7- and 15-fold, respectively. (nih.gov)