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.
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.
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.
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.
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 5'-(tetrahydrogen triphosphate). A cytosine nucleotide containing three phosphate groups esterified to the sugar moiety.
A simple organophosphorus compound that inhibits DNA polymerase, especially in viruses and is used as an antiviral agent.
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.
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.
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.
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.
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)
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.
A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.
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)
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).
An amino acid produced in the urea cycle by the splitting off of urea from arginine.
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.
A class of enzymes that transfers phosphate groups and has a carboxyl group as an acceptor. EC 2.7.2.
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.
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.
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.
An enzyme of the urea cycle which splits argininosuccinate to fumarate plus arginine. Its absence leads to the metabolic disease ARGININOSUCCINIC ACIDURIA in man. EC 4.3.2.1.
An essential amino acid that is physiologically active in the L-form.
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.
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.
Inorganic or organic salts and esters of arsenic acid.
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.
The rate dynamics in chemical or physical systems.
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.
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.
A species of strictly anaerobic, hyperthermophilic archaea which lives in geothermally-heated marine sediments. It exhibits heterotropic growth by fermentation or sulfur respiration.
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.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.
Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.
All of the divisions of the natural sciences dealing with the various aspects of the phenomena of life and vital processes. The concept includes anatomy and physiology, biochemistry and biophysics, and the biology of animals, plants, and microorganisms. It should be differentiated from BIOLOGY, one of its subdivisions, concerned specifically with the origin and life processes of living organisms.
A publication issued at stated, more or less regular, intervals.
A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.
A phylum of unicellular parasitic EUKARYOTES characterized by the presence of complex apical organelles generally consisting of a conoid that aids in penetrating host cells, rhoptries that possibly secrete a proteolytic enzyme, and subpellicular microtubules that may be related to motility.
Lists of persons or organizations, systematically arranged, usually in alphabetic or classed order, giving address, affiliations, etc., for individuals, and giving address, officers, functions, and similar data for organizations. (ALA Glossary of Library and Information Science, 1983)

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)

What are the characters Mendel selected for his experiments on pea plant? MTHFS is the first identified 10-formylTHF tight-binding protein. 2, the WT GBS strain, A909 is prototrophic for both purine and pyrimidine biosynthesis and reach an optical density at 600 nm (OD 600) of 0.8-0.9 (3-5 × 10 9 cfu ml −1) in dCDM, similar to growth in cCDM (Fig. Control by purines occurs through PurR-mediated repression ( 4 , 84 ), and nitrogen control involves the Ntr system acting through the nitrogen assimilation control protein NAC ( 4 , 119 ). Pyrimidine biosynthesis Unlike in purine biosynthesis, the pyrimidine ring is synthesized before it is conjugated to PRPP. Thus, the behavior of liver CTP synthetase activity is tightly linked with that of the CTP pool. the reaction catalysed by the enzyme aspartate transcarbamoylase. 2. iii. the reaction catalysed by the enzyme aspartate transcarbamoylase. CTP. Here we review progress in molecular aspects and recent studies on the regulation and manipulation of ...
Semantic Scholar extracted view of Studies on the heterotropic interaction of hemoglobin. II. Role of beta-146 and beta-2 histidines in the alkaline Bohr effect. by Masato Ohe et al.
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 ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
def: An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer. [EC:2.7.11.11, ISBN:0198506732 ...
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 ...
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.. ...
Dagiti unikonta ket addaan iti tallo a panagtitipon ti gene nga awan kadagiti bikonta. Dagiti tallo a genes a naitiptipon kadagiti unikonta ngem saan a ti bakteria wenno dagiti naikodigo nga ensima dagiti bikonta para iti sintesis dagiti pirimidina nukleotido: carbamoyl phosphate synthase, dihydroorotase, aspartate carbamoyltransferase. Daytoy ket mabalin a nakairamanan ti dua a panagtitipon, ti manmano a paris kadagiti pasamak, amangsupsuporat ti nakibinningayan a tinaudan ti Opisthokonta ken Amoebozoa. Ni Cavalier-Smith[4] ket kasisigud a nagisingasing a dagiti unikonta ket nagtaudda nga addaan iti agmaymaysa a flagelo ken agmaymaysa a basal a bagi. Daytoy ket saan a mabalin a kasta, nupay kasta, a kas dagiti adda ti flagelo nga opisthokonta, ken dagiti pay adda ti flagelo nga Amoebozoa, a mairaman ti Breviata, ket pudno nga adda ti dua a basal a bagbagi, a kas dagiti kadawyan a bikonta (urayno maymaysa laeng ti addaan iti flagelo iti kaaduan kadagiti unikonta). Daytoy naparisan a ...
Many transmembrane receptors are oligomeric proteins. Binding of a ligand may alter the oligomeric state of the receptor, induce structural changes within the oligomer, or both. The bacterial aspartate chemoreceptor Tar forms a homodimer in the presence or absence of ligands. Tar mediates attractant and repellent responses by modulating the activity of the cytoplasmic kinase CheA. In vivo intersubunit suppression was used to show that certain combinations of full-length and truncated mutant Tar proteins complemented each other to restore attractant responses to aspartate. These results suggest that heterodimers with only one intact cytoplasmic domain are functional. The signaling mechanism may require interactions between dimers or conformational changes within a single cytoplasmic domain.. ...
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 ...
Motilin is a 22-amino-acid peptide secreted by endocrinocytes in the mucosa of the proximal small intestine. Motilin is a gastrointestinal regulatory polypeptide produced by motilin cells in the duodenal epithelium. Motilin is an intestinal peptide that stimulates contraction of gut smooth musc...
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 ...
Complete information for CDH10 gene (Protein Coding), Cadherin 10, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for CDH15 gene (Protein Coding), Cadherin 15, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Controlled proteolysis of the multifunctional protein that initiates pyrimidine biosynthesis in mammalian cells: evidence for discrete structural domains.: The
MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPyrimidine ribonucleotide biosynthesisaspartate carbamoyltransferase (TIGR00670; EC 2.1.3.2; HMM-score: 120.5) ...
Easy-to-read patient leaflet for Dasatinib. Includes indications, proper use, special instructions, precautions, and possible side effects.
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.
Pathway:Mouse:Alanine and aspartate metabolism KEGG]] moved to [[Pathway:Mus musculus:Alanine and aspartate metabolism KEGG]]: Renaming ...
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 ...
Ornithine transcarbamylase Ornithine carbamoyltransferase Human OTC trimer. From PDB 1OTH. Available structures: 1c9y, 1ep9, 1fb5, 1fvo, 1oth Identifiers
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.
DI-fusion, le Dépôt institutionnel numérique de lULB, est loutil de référencementde la production scientifique de lULB.Linterface de recherche DI-fusion permet de consulter les publications des chercheurs de lULB et les thèses qui y ont été défendues.
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
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 ...
Information on the environment for those involved in developing, adopting, implementing and evaluating environmental policy, and also the general public
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 ...
In a previous study (G. M. Wahl, B. Robert de Saint Vincent, and M. L. De Rose, Nature (London) 307:516-520, 1984), we used gene transfer of a CAD cosmid to demonstrate that gene position profoundly affects amplification frequency. One transformant, T5, amplified the donated CAD genes at a frequency at least 100-fold higher than did the other transformants analyzed. The CAD genes in T5 and two drug-resistant derivatives were chromosomally located. In this report, we show that a subclone of T5 gives rise to an extrachromosomal molecule (CAD episome) containing the donated CAD genes. Gel electrophoresis indicated that the CAD episome is approximately 250 to 300 kilobase pairs, and a variety of methods showed that it is a covalently closed circle. We show that the CAD episome replicates semiconservatively and approximately once per cell cycle. Since the CAD cosmid, which comprises most of the CAD episome, does not replicate autonomously when transfected into cells, our results indicate that either ...
We use cookies to ensure that we give you the best experience on our website. If you click Continue well assume that you are happy to receive all cookies and you wont see this message again. Click Find out more for information on how to change your cookie settings ...
Hangzhou Longshine Bio-Tech Co.,LTD is a professional l-ornithine l-aspartate salt/3230-94-2 manufacturer with productive factory, which is able to produce API and l-ornithine l-aspartate salt/3230-94-2 intermediate with reliable quality and good price.
As one of the most professional l-arginine l-aspartate cas 7675-83-4 manufacturers and suppliers in China, were featured by quality products and low price. Please rest assured to buy l-arginine l-aspartate cas 7675-83-4 in stock here from our factory. Contact us for more information about API and food ingredients for food, medical and cleaning.
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!
N-(N-((S)-1,3-Dicarboxypropyl)carbamoyl)-4-(18F)fluorobenzyl-L-cysteine: an imaging probe for prostate cancer; structure in first source
Aspartate carbamoyltransferase has a α6β6 subunit composition. The six αβ-protomers are arranged in D3 symmetry. Viral capsid ...
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 ...
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 ...
"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 ...
CTP acts as an inhibitor of the enzyme aspartate carbamoyltransferase, which is used in pyrimidine biosynthesis. CTP synthase ...
... coli enzyme aspartate carbamoyltransferase (ATCase) has become another good example of allosteric regulation. The kinetic ...
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 ...
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 ...
... aspartate carbamoyltransferase. This must have involved a double fusion, a rare pair of events, supporting the shared ancestry ...
"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 ...
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 ...
... 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 ...
... 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 ...
... and aspartate carbamoyltransferase that is not present in plants, and plants have a fusion of thymidylate synthase and ...
... (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 ...
Aspartate carbamoyltransferase. *Dihydroorotase. *P450-containing systems. *Cytochrome b6f complex. *Electron transport chain ...
Aspartate carbamoyltransferase. *Ornithine carbamoyltransferase. *Oxamate carbamoyltransferase. *Putrescine ...
Aspartate carbamoyltransferase. *Ornithine carbamoyltransferase. *Oxamate carbamoyltransferase. *Putrescine ...
Aspartate carbamoyltransferase. *Dihydroorotase. *Cholesterol side-chain cleavage enzyme. *Cytochrome b6f complex. *Electron ...
Aspartate carbamoyltransferase. *Dihydroorotase. *Cholesterol side-chain cleavage enzyme. *Cytochrome b6f complex. *Electron ...
Aspartate carbamoyltransferase. *Dihydroorotase. *Dihydroorotate dehydrogenase. *Orotidine 5'-phosphate decarboxylase/Uridine ...
Production of IMP from PRPP requires glutamine, glycine, aspartate, and 6 ATP, among other things.[1] IMP is then converted to ... This reaction requires aspartate, glutamine, bicarbonate, and 2 ATP molecules (to provide energy), as well as PRPP which ... AMP (adenosine monophosphate) using GTP and aspartate, which is converted into fumarate. While IMP can be directly converted to ... Aspartate carbamoyltransferase. *Dihydroorotase. *Dihydroorotate dehydrogenase. *Orotidine 5'-phosphate decarboxylase/Uridine ...
Aspartate carbamoyltransferase. *Ornithine carbamoyltransferase. *Oxamate carbamoyltransferase. *Putrescine ...
Aspartate carbamoyltransferase. *Dihydroorotase. *P450-containing systems. *Cytochrome b6f complex. *Electron transport chain ...
Aspartate carbamoyltransferase. *Dihydroorotase. *Cholesterol side-chain cleavage enzyme. *Cytochrome b6f complex. *Electron ...
Aspartate carbamoyltransferase. *Aspartate-semialdehyde dehydrogenase. *Asprosin. *Ataxin 7. *ATCase/OTCase family. *Atg1 ...
Aspartate carbamoyltransferase. *Dihydroorotase. *Dihydroorotate dehydrogenase. *Orotidine 5'-phosphate decarboxylase/Uridine ...
Reichard, P. and Hanshoff, G. (1956). "Aspartate carbamyl transferase from Escherichia coli". Acta Chem. Scand. 10: 548-566. ... Shepherson, M. and Pardee, A.B. (1960). "Production and crystallization of aspartate transcarbamylase". J. Biol. Chem. 235: ...
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 ...
... aspartate carbamoyltransferase. Daytoy ket mabalin a nakairamanan ti dua a panagtitipon, ti manmano a paris kadagiti pasamak, ...
... aspartate carbamoyltransferase. This must have involved a double fusion, a rare pair of events, supporting the shared ancestry ...
Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate ... carbamoyltransferase at 2.8-A resolution and neutral pH. ... AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE ... ASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN A, C 310 Escherichia coli EC#: 2.1.3.2 IUBMB Mutation: E60Q, E147Q, Q149E, ... ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN B, D 153 Escherichia coli Mutation: Q8G Gene Name(s): pyrI b4244 JW4203 ...
... aspartate carbamoyltransferase and dihydroorotase. Orotidylate is then decaroxylated to form uridylate. Cram.com makes it easy ... Carbamoyl phosphate combines with aspartate to form carbamoyl aspartate aided by the enzyme aspartate transcarbamoylase. II. ... the reaction catalysed by the enzyme aspartate transcarbamoylase. 2. iii. the reaction catalysed by the enzyme aspartate ... carbamoyl-phosphate synthetase II and aspartate carbamoyltransferase which decreased to 14 to 28% of the activity of normal rat ...
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 ...
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 ...
Catalysis of the reaction: L-aspartate + carbamoyl phosphate = N-carbamoyl-L-aspartate + H(+) + phosphate.. Synonyms. aspartate ... Gene Ontology Term: aspartate carbamoyltransferase activity. GO ID. GO:0004070 Aspect. Molecular Function. Description. ... L-aspartate transcarbamoylase activity, L-aspartate transcarbamylase activity View GO Annotations in other species in AmiGO ... L-aspartate carbamoyltransferase activity, carbamoylaspartotranskinase activity, carbamylaspartotranskinase activity, ...
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. ...
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 ...
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.UniRule annotation. Manual assertion ... sp,Q31EK2,PYRB_HYDCU Aspartate carbamoyltransferase OS=Hydrogenovibrio crunogenus (strain XCL-2) OX=317025 GN=pyrB PE=3 SV=1 ... 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. ...
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- ...
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 ...
... 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; ...
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 ...
Involved in allosteric regulation of aspartate carbamoyltransferase. Contains catalytic and regulatory chains. ... Aspartate carbamoyltransferase regulatory chain - Also known as PYRI_ECO8A, pyrI. ... Involved in allosteric regulation of aspartate carbamoyltransferase. Contains catalytic and regulatory chains. ... Involved in allosteric regulation of aspartate carbamoyltransferase. Contains catalytic and regulatory chains. ...
Order Recombinant Bacteroides thetaiotaomicron Aspartate carbamoyltransferase pyrB 01015982797 at Gentaur Bacteroides ... Aspartate carbamoyltransferase pyrB 01015982797 at Gentaur Bacteroides thetaiotaomicron Aspartate carbamoyltransferase (pyrB) ...
CRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ... Aspartate carbamoyltransferase: ACEGIK. Aspartate carbamoyltransferase regulatory chain: BDFHJL. SMTL:PDB. SMTL Chain Id:. PDB ... De Vos, D. et al., Crystal Structure of T State Aspartate Carbamoyltransferase of the Hyperthermophilic Archaeon Sulfolobus ... CRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ...
Aspartate/ornithine carbamoyltransferase. The name of this superfamily has been modified since the most recent official CATH+ ...
... 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 ...
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. ...
Aspartate carbamoyltransferase; PyrI subunit. 36.8. pyrB b4245. Aspartate carbamoyltransferase; PyrB subunit. 34.3. ...
Aspartate carbamoyltransferase has a α6β6 subunit composition. The six αβ-protomers are arranged in D3 symmetry. Viral capsid ...
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 ...
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. { ...
... on Shapeways. Learn more before you buy, or discover other cool products in Mathematical Art.
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: ...
Compound: aspartate carbamoyltransferase, catalytic chain. Database cross-references and differences (RAF-indexed): *Uniprot ... Compound: Aspartate carbamoyltransferase regulatory chain. Database cross-references and differences (RAF-indexed): *Uniprot ... Compound: aspartate carbamoyltransferase, catalytic chain. Database cross-references and differences (RAF-indexed): *Uniprot ... Compound: Aspartate carbamoyltransferase regulatory chain. Database cross-references and differences (RAF-indexed): *Uniprot ...
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. ...
... aspartate carbamoyltransferase / dihydroorotase [EC:6.3.5.5 2.1.3.2 3.5.2.3] K00764 purF; amidophosphoribosyltransferase [EC: ...
aspartate carbamoyltransferase activity carbamoyl-phosphate synthase (ammonia) activity carbamoyl-phosphate synthase (glutamine ... Protein Aliases: Aspartate carbamoyltransferase; CAD protein; CAD trifunctional protein; Dihydroorotase; Glutamine-dependent ... aspartate binding nucleotide binding UTP binding catalytic activity amino acid binding transferase activity carboxyl- or ... aspartate transcarbamoylase, and dihydroorotase. This protein is regulated by the mitogen-activated protein kinase (MAPK) ...
Aspartate carbamoyltransferase. 1380. 1424. Pyrimidine operon protein. 1379. 1423. Transport and binding proteins (n = 7). ...
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 ...
Aspartate Carbamoyltransferase (PYRB) * Phosphoglucosamine Mutase (GLMM) * Porphobilinogen Deaminase (HEMC) * Phenylalanyl-tRNA ...
  • Aspartate carbamoyltransferase (also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine biosynthetic pathway (EC 2.1.3.2). (wikipedia.org)
  • Protein differentiation: a comparison of aspartate transcarbamoylase and ornithine transcarbamoylase from Escherichia coli K-12. (ebi.ac.uk)
  • Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit. (ebi.ac.uk)
  • The first high pH structure of Escherichia coli aspartate transcarbamoylase. (ebi.ac.uk)
  • Crystal structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase. (ebi.ac.uk)
  • Structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form. (ebi.ac.uk)
  • 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. (pnas.org)
  • 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. (thermofisher.com)
  • In animals, the de novo pathway is initiated and controlled by CAD, a ∼240‐kDa multifunctional protein with four different enzymatic domains: glutaminase (GLN), carbamoyl phosphate synthetase (CPS), dihydroorotase (DHO) and aspartate transcarbamoylase (ATC). (els.net)
  • CAD is a 243‐kDa polypeptide with four enzymatic domains [glutaminase (GLN), carbamoyl phosphate synthetase (CPS), dihydroorotase (DHO) and aspartate transcarbamoylase (ATC)] that oligomerises into 1.5‐megaDa hexamers. (els.net)
  • The binding of CTP to the regulatory subunit of aspartate transcarbamoylase stabilizes the T state. (sugokuii.info)
  • Aspartate transcarbamoylase genes of Pseudomonas putida: requirement for an inactive dihydroorotase for assembly into the dodecameric holoenzyme. (pseudomonas.com)
  • CAD dihydroorotase and aspartate transcarbamoylase domains self-assembles into dimers and trimers. (anticorps-enligne.fr)
  • Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes. (anticorps-enligne.fr)
  • Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB). (ebi.ac.uk)
  • ATCase is a highly regulated enzyme that catalyses the first committed step in pyrimidine biosynthesis, the condensation of l-aspartate and carbamoyl phosphate to form N-carbamyl-L-aspartate and inorganic phosphate. (wikipedia.org)
  • Insight into the mode of binding of substrates to the catalytic center of ATCase was first made possible by the binding of a bisubstrate analogue, N-(phosphonoacetyl)-L-aspartate (PALA). (wikipedia.org)
  • Aspartate carbamoyltransferase ( EC:2.1.3.2 ) (ATCase) catalyses the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novo biosynthesis of pyrimidine nucleotides [ PMID: 3015959 ]. (ebi.ac.uk)
  • Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain. (antibody-antibodies.com)
  • The pyrBI operon of Escherichia coli K-12 encodes the two nonidentical subunits of the pyrimidine biosynthetic enzyme aspartate transcarbamylase (ATCase). (uab.edu)
  • The biochemical and functional evidence presented here demonstrates that an origin of bidirectional replication (OBR) resides within the constitutively expressed housekeeping gene CAD, which encodes the first three reactions of de novo uridine biosynthesis (carbamoyl-phosphate synthetase, aspartate carbamoyltransferase, and dihydroorotase). (asm.org)
  • Chez www.anticorps-enligne.fr sont 119 Carbamoyl-Phosphate Synthetase 2, Aspartate Transcarbamylase, and Dihydroorotase (CAD) Anticorps de 23 de différents fournisseurs disponibles. (anticorps-enligne.fr)
  • De plus, nous expédions Carbamoyl-Phosphate Synthetase 2, Aspartate Transcarbamylase, and Dihydroorotase Kits (6) et beaucoup plus de produits pour cette protéine. (anticorps-enligne.fr)
  • Un total de 138 Carbamoyl-Phosphate Synthetase 2, Aspartate Transcarbamylase, and Dihydroorotase produits sont actuellement listés. (anticorps-enligne.fr)
  • In a subsequent cyclization reaction, the enzyme Aspartate carbamoyltransferase forms N-carbamoyl-aspartate which is converted into dihydroorotic acid by dihydroorotase. (meddic.jp)
  • 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)
  • enzyme catalyzing the condensation of carbamoyl phosphate and l-aspartate to N -carbamoyl-l-aspartate. (thefreedictionary.com)
  • The enzyme takes the end methyl residue from the methionine side chain and adds it to the side chain carboxyl group of L-isoaspartate or D-aspartate to create a methyl ester. (xfam.org)
  • The multifunctional protein that initiates de novo pyrimidine biosynthesis in mammalian cells carries carbamoylphosphate synthetase, aspartate transcarbamylase (aspartate carbamoyltransferase), and dihydro-orotase activities on a single 215,000-dalton polypeptide chain. (mysciencework.com)
  • 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)
  • Results from x-ray diffraction have contributed immensely to the understanding of hemoglobins, of allosteric enzymes such as aspartate carbamoyltransferase, of DNA, and of viral agents such as the influenza virus. (iastate.edu)
  • No repression of five enzymes of the pyrimidine biosynthetic pathway (aspartate carbamoyltransferase, dihydro-orotase, dihydro-orotate dehydrogenase, orotidine-5′-phosphate pyrophosphorylase and orotidine-5′-phosphate decarboxylase) could be detected on addition of pyrimidines to minimal asparagine cultures of P. putida A90, but a 1.5-to 2-fold degree of derepression was found following pyrimidine starvation of pyrimidine auxotrophic mutants of P. putida A90. (microbiologyresearch.org)
  • Next, aspartate undergoes a condensation reaction with carbamoyl-phosphate to form orotic acid. (meddic.jp)
  • Pyrimidines are synthesized first from aspartate and carbamoyl-phosphate in the cytoplasm to the common precursor ring structure orotic acid, onto which a phosphorylated ribosyl unit is covalently linked. (meddic.jp)
  • Construction of a cDNA to the hamster CAD gene and its application toward defining the domain for aspartate transcarbamylase. (antibody-antibodies.com)
  • DNA replication initiates within this region in the single-copy CAD gene in Syrian baby hamster kidney cells and in the large chromosomal amplicons that were generated after selection with N-phosphonacetyl-L-aspartate, a specific inhibitor of CAD. (asm.org)
  • Crystal structure of Sulfolobus acidocaldarius aspartate carbamoyltransferase in complex with its allosteric activator CTP. (ebi.ac.uk)
  • Crystal Structure of T State Aspartate Carbamoyltransferase of the Hyperthermophilic Archaeon Sulfolobus acidocaldarius. (expasy.org)
  • Catalysis of the reaction: L-aspartate + carbamoyl phosphate = N-carbamoyl-L-aspartate + H(+) + phosphate. (yeastgenome.org)
  • 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)
  • Characterization of the aspartate carbamoyltransferase subunit obtained from a generic viagra multienzyme aggregate in the pyrimidine pathway of yeast. (beginstyle.top)
  • The catalytic subunits catalyze the carbamylation of the amino group of aspartate but do not have regulatory properties, while the regulatory subunits do not have any catalytic activity but contain the regulatory sites for effector binding. (wikipedia.org)
  • CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate CC + N-carbamoyl-L-aspartate. (univ-lyon1.fr)
  • Each of the catalytic domains is composed of two structural domains, the aspartate domain, which contains most of the residues responsible for binding aspartate, and the carbamoyl phosphate domain, which contains most of the residues that bind to carbamoyl phosphate. (wikipedia.org)