ATP Phosphoribosyltransferase: An enzyme that catalyzes the first step of the pathway for histidine biosynthesis in Salmonella typhimurium. ATP reacts reversibly with 5-phosphoribosyl-1-pyrophosphate to yield N-1-(5'-phosphoribosyl)-ATP and pyrophosphate. EC 2.4.2.17.Hypoxanthine Phosphoribosyltransferase: An enzyme that catalyzes the conversion of 5-phosphoribosyl-1-pyrophosphate and hypoxanthine, guanine, or 6-mercaptopurine to the corresponding 5'-mononucleotides and pyrophosphate. The enzyme is important in purine biosynthesis as well as central nervous system functions. Complete lack of enzyme activity is associated with the LESCH-NYHAN SYNDROME, while partial deficiency results in overproduction of uric acid. EC 2.4.2.8.Adenine Phosphoribosyltransferase: An enzyme catalyzing the formation of AMP from adenine and phosphoribosylpyrophosphate. It can act as a salvage enzyme for recycling of adenine into nucleic acids. EC 2.4.2.7.Pentosyltransferases: Enzymes of the transferase class that catalyze the transfer of a pentose group from one compound to another.Fructose-Bisphosphatase: An enzyme that catalyzes the conversion of D-fructose 1,6-bisphosphate and water to D-fructose 6-phosphate and orthophosphate. EC 3.1.3.11.Adenosine Monophosphate: Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.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.Kinetics: The rate dynamics in chemical or physical systems.Allosteric Regulation: The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.Mycobacterium tuberculosis: A species of gram-positive, aerobic bacteria that produces TUBERCULOSIS in humans, other primates, CATTLE; DOGS; and some other animals which have contact with humans. Growth tends to be in serpentine, cordlike masses in which the bacilli show a parallel orientation.Pentoses: A class of carbohydrates that contains five carbon atoms.Tuberculosis: Any of the infectious diseases of man and other animals caused by species of MYCOBACTERIUM.Tuberculosis, Pulmonary: MYCOBACTERIUM infections of the lung.Antitubercular Agents: Drugs used in the treatment of tuberculosis. They are divided into two main classes: "first-line" agents, those with the greatest efficacy and acceptable degrees of toxicity used successfully in the great majority of cases; and "second-line" drugs used in drug-resistant cases or those in which some other patient-related condition has compromised the effectiveness of primary therapy.Histidine: An essential amino acid that is required for the production of HISTAMINE.Pyruvate Dehydrogenase (Lipoamide): The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Pyruvate Dehydrogenase Complex: A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)Pyruvate Dehydrogenase Complex Deficiency Disease: An inherited metabolic disorder caused by deficient enzyme activity in the PYRUVATE DEHYDROGENASE COMPLEX, resulting in deficiency of acetyl CoA and reduced synthesis of acetylcholine. Two clinical forms are recognized: neonatal and juvenile. The neonatal form is a relatively common cause of lactic acidosis in the first weeks of life and may also feature an erythematous rash. The juvenile form presents with lactic acidosis, alopecia, intermittent ATAXIA; SEIZURES; and an erythematous rash. (From J Inherit Metab Dis 1996;19(4):452-62) Autosomal recessive and X-linked forms are caused by mutations in the genes for the three different enzyme components of this multisubunit pyruvate dehydrogenase complex. One of the mutations at Xp22.2-p22.1 in the gene for the E1 alpha component of the complex leads to LEIGH DISEASE.Acetyl-CoA Carboxylase: A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.Acetate-CoA Ligase: An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.Carbon-Nitrogen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.Methylmannosides: Mannosides formed by the reaction of the hydroxyl group on the anomeric carbon atom of mannose with methyl alcohol. They include both alpha- and beta-methylmannosides.MethylglycosidesMycobacterium smegmatis: A rapid-growing, nonphotochromogenic species of MYCOBACTERIUM originally isolated from human smegma and found also in soil and water. (From Dorland, 28th ed)Mycobacterium: A genus of gram-positive, aerobic bacteria. Most species are free-living in soil and water, but the major habitat for some is the diseased tissue of warm-blooded hosts.3-O-Methylglucose: A non-metabolizable glucose analogue that is not phosphorylated by hexokinase. 3-O-Methylglucose is used as a marker to assess glucose transport by evaluating its uptake within various cells and organ systems. (J Neurochem 1993;60(4):1498-504)MethylglucosidesEnterohemorrhagic Escherichia coli: Strains of ESCHERICHIA COLI that are a subgroup of SHIGA-TOXIGENIC ESCHERICHIA COLI. They cause non-bloody and bloody DIARRHEA; HEMOLYTIC UREMIC SYNDROME; and hemorrhagic COLITIS. An important member of this subgroup is ESCHERICHIA COLI O157-H7.Escherichia coli O157: A verocytotoxin-producing serogroup belonging to the O subfamily of Escherichia coli which has been shown to cause severe food-borne disease. A strain from this serogroup, serotype H7, which produces SHIGA TOXINS, has been linked to human disease outbreaks resulting from contamination of foods by E. coli O157 from bovine origin.Escherichia coli Infections: Infections with bacteria of the species ESCHERICHIA COLI.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Shiga Toxin 2: A toxin produced by certain pathogenic strains of ESCHERICHIA COLI such as ESCHERICHIA COLI O157. It shares 50-60% homology with SHIGA TOXIN and SHIGA TOXIN 1.Galaxies: Large aggregates of CELESTIAL STARS; COSMIC DUST; and gas. (From McGraw Hill Dictionary of Scientific and Technical Terms, 6th ed)ArchivesBiological Science Disciplines: 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.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.PubMed: 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.Polyphosphates: Linear polymers in which orthophosphate residues are linked with energy-rich phosphoanhydride bonds. They are found in plants, animals, and microorganisms.Directories as Topic: 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)Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.EthylenediaminesMethanosarcina barkeri: A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Chelating Agents: Chemicals that bind to and remove ions from solutions. Many chelating agents function through the formation of COORDINATION COMPLEXES with METALS.Information Storage and Retrieval: Organized activities related to the storage, location, search, and retrieval of information.Semiconductors: Materials that have a limited and usually variable electrical conductivity. They are particularly useful for the production of solid-state electronic devices.Zinc: A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.Otolaryngology: A surgical specialty concerned with the study and treatment of disorders of the ear, nose, and throat.Otorhinolaryngologic Diseases: Pathological processes of the ear, the nose, and the throat, also known as the ENT diseases.Professional Practice Location: Geographic area in which a professional person practices; includes primarily physicians and dentists.Otorhinolaryngologic Surgical Procedures: Surgery performed on the ear and its parts, the nose and nasal cavity, or the throat, including surgery of the adenoids, tonsils, pharynx, and trachea.Voice Disorders: Pathological processes that affect voice production, usually involving VOCAL CORDS and the LARYNGEAL MUCOSA. Voice disorders can be caused by organic (anatomical), or functional (emotional or psychological) factors leading to DYSPHONIA; APHONIA; and defects in VOICE QUALITY, loudness, and pitch.Ear: The hearing and equilibrium system of the body. It consists of three parts: the EXTERNAL EAR, the MIDDLE EAR, and the INNER EAR. Sound waves are transmitted through this organ where vibration is transduced to nerve signals that pass through the ACOUSTIC NERVE to the CENTRAL NERVOUS SYSTEM. The inner ear also contains the vestibular organ that maintains equilibrium by transducing signals to the VESTIBULAR NERVE.Eye: The organ of sight constituting a pair of globular organs made up of a three-layered roughly spherical structure specialized for receiving and responding to light.

An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis. (1/30)

In addition to their essential catalytic role in protein biosynthesis, aminoacyl-tRNA synthetases participate in numerous other functions, including regulation of gene expression and amino acid biosynthesis via transamidation pathways. Herein, we describe a class of aminoacyl-tRNA synthetase-like (HisZ) proteins based on the catalytic core of the contemporary class II histidyl-tRNA synthetase whose members lack aminoacylation activity but are instead essential components of the first enzyme in histidine biosynthesis ATP phosphoribosyltransferase (HisG). Prediction of the function of HisZ in Lactococcus lactis was assisted by comparative genomics, a technique that revealed a link between the presence or the absence of HisZ and a systematic variation in the length of the HisG polypeptide. HisZ is required for histidine prototrophy, and three other lines of evidence support the direct involvement of HisZ in the transferase function. (i) Genetic experiments demonstrate that complementation of an in-frame deletion of HisG from Escherichia coli (which does not possess HisZ) requires both HisG and HisZ from L. lactis. (ii) Coelution of HisG and HisZ during affinity chromatography provides evidence of direct physical interaction. (iii) Both HisG and HisZ are required for catalysis of the ATP phosphoribosyltransferase reaction. This observation of a common protein domain linking amino acid biosynthesis and protein synthesis implies an early connection between the biosynthesis of amino acids and proteins.  (+info)

Specific binding of the first enzyme for histidine biosynthesis to the DNA of histidine operon. (2/30)

Studies were done to examine direct binding of the first enzyme of the histidine biosynthetic pathway (phosphoribosyltransferase) to 32P-labeled phi80dhis DNA and competition of this binding by unlabeled homologous DNA and by various preparations of unlabeled heterologous DNA, including that from a defective phi80 bacteriophage carrying the histidine operon with a deletion of part of its operator region. Our findings show that phosphoribosyltransferase binds specifically to site in or near the regulatory region of the histidine operon. The stability of the complex formed by interaction of the enzyme with the DNA was markedly decreased by the substrates of the enzyme and was slightly increased by the allosteric inhibitor, histidine. These findings are consistent with previous data that indicate that phosphoribosyltransferase plays a role in regulating expression of the histidine operon.  (+info)

Molecular dissection of the role of histidine in nickel hyperaccumulation in Thlaspi goesingense (Halacsy). (3/30)

To understand the role of free histidine (His) in Ni hyperaccumulation in Thlaspi goesingense, we investigated the regulation of His biosynthesis at both the molecular and biochemical levels. Three T. goesingense cDNAs encoding the following His biosynthetic enzymes, ATP phosphoribosyltransferase (THG1, GenBank accession no. AF003347), imidazoleglycerol phosphate dehydratase (THB1, GenBank accession no. AF023140), and histidinol dehydrogenase (THD1, GenBank accession no. AF023141) were isolated by functional complementation of Escherichia coli His auxotrophs. Northern analysis of THG1, THD1, and THB1 gene expression revealed that each gene is expressed in both roots and shoots, but at the concentrations and dosage times of Ni treatment used in this study, these genes failed to show any regulation by Ni. We were also unable to observe any increases in the concentration of free His in root, shoot, or xylem sap of T. goesingense in response to Ni exposure. X-ray absorption spectroscopy of root and shoot tissue from T. goesingense and the non-accumulator species Thlaspi arvense revealed no major differences in the coordination of Ni by His in these tissues. We therefore conclude that the Ni hyperaccumulation phenotype in T. goesingense is not determined by the overproduction of His in response to Ni.  (+info)

Molecular cloning and characterization of ATP-phosphoribosyl transferase from Arabidopsis, a key enzyme in the histidine biosynthetic pathway. (4/30)

We have characterized two isoforms of ATP-phosphoribosyl transferase (ATP-PRT) from Arabidopsis (AtATP-PRT1 [accession no. AB025251] and AtATP-PRT2), catalyzing the first step of the pathway of hisidine (His) biosynthesis. The primary structures deduced from AtATP-PRT1 and AtATP-PRT2 cDNAs share an overall amino acid identity of 74.6% and contain N-terminal chloroplast transit peptide sequences. DNA-blot analyses indicated that the ATP-PRTs in Arabidopsis are encoded by two separate genes with a closely similar gene structural organization. Both gene transcripts were detected throughout development, and protein-blot analysis revealed predominant accumulation of the AtATP-PRT proteins in Arabidopsis leaves. The His auxotrophy of a his1 mutant of Saccharomyces cerevisiae was suppressed by the transformation with AtATP-PRT1 and AtATP-PRT2 cDNAs, indicating that both isoforms are functionally active ATP-PRT enzymes. The K(m) values for ATP and phosphoribosyl pyrophosphate of the recombinant AtATP-PRT proteins were comparable to those of the native ATP-PRTs from higher plants and bacteria. It was demonstrated that the recombinant AtATP-PRTs were inhibited by L-His (50% inhibition of initial activity = 40-320 microM), suggesting that His biosynthesis was regulated in plants through feedback inhibition by L-His.  (+info)

Evidence against a covalent intermediate in the adenosine triphosphate phosphoribosyltransferase reaction of histidine biosynthesis. (5/30)

14C-Labeled 5-phospho-alpha-D-ribose-1-diphosphate (PRibPP) was synthesized and its interaction with adenosine triphosphate phosphoribosyltransferase was examined by gel filtration in a search for a form of this substrate covalently bound to the enzyme. Wide variation in solvent conditions gave little labeling of the enzyme. Heavy labeling was found only in the presence of the second substrate, ATP, and this was shown to arise from tightly but noncovalently bound product. Previous reports of a covalent intermediate in this enzymatic reaction probably were due to contaminating ATP in 5-phospho-alpha-D-ribose-1-diphosphate. Feedback inhibition of the enzyme by histidine was shown to occur at the step giving product or at some earlier step in the mechanism.  (+info)

trans-Recessive mutation in the first structural gene of the histidine operon that results in constitutive expression of the operon. (6/30)

The first enzyme for histidine biosynthesis, encoded in the hisG gene, is involved in regulation of expression of the histidine operon in Salmonella typhimurium. The studies reported here concern the question of how expression of the histidine operon is affected by a mutation in the hisG gene that alters the allosteric site of the first enzyme for histidine biosynthesis, rendering the enzyme completely resistant to inhibition by histidine. The intracellular concentrations of the enzymes encoded in the histidine operon in a strain carrying such a mutation on an episome and missing the chromosomal hisG gene are three- to fourfold higher than in a strain carrying a wild-type hisG gene on the episome. The histidine operon on such a strain fails to derepress in response to histidine limitation and fails to repress in response to excess histidine. Furthermore, utilizing other merodiploid strains, we demonstrate that the wild-type hisG gene is trans dominant to the mutant allele with respect to this regulatory phenomenon. Examination of the regulation of the histidine operon in strains carrying the feedback-resistant mutation in an episome and hisT and hisW mutations in the chromosome showed that the hisG regulatory mutation is epistatic to the hisT and hisW mutations. These data provide additional evidence that the first enzyme for histidine biosynthesis is involved in autogenous regulation of expression of the histidine operon.  (+info)

Derepression and repression of the histidine operon: role of the feedback site of the first enzyme. (7/30)

Thiazolealanine, a false feedback inhibitor, causes transient repression of the his operon previously derepressed by a severe histidine limitation in strains with a wild-type or feedback-hypersensitive first enzyme but not in feedback-resistant mutants. Since experiments reported here clearly demonstrate that thiazolealanine is not transferred to tRNAHis, it is proposed that this "transient repression" is effected through the interaction of thiazolealanine with the feedback site of the enzyme. Experiments in the presence of rifampin indicate that this thiazolealanine-mediated effect is exerted at the level of translation. We conclude that histidine (free), in addition to forming co-repressor, also represses the operon at the level of translation through feedback interaction with the first enzyme of the pathway (adenosine 5'-triphosphate phosphoribosyltransferase). Rates of derepression in feedback-resistant strains are roughly half of those observed in controls, suggesting a positive role played by a first enzyme with a normal but unoccupied feedback site. Some feedback-resistant mutants, in contrast to the wild type, were unable to exhibit derepression under histidine limitation caused by aminotriazole.  (+info)

Affinity labelling to - SH groups in adenosine - triphosphate - phosphoribosyl transferase with the dinitrophenyl group from S-dinitrophenyl-6-mercaptopurine-riboside 5'-phosphate. (8/30)

Adenosine-triphosphate-phosphoribosyl transferase from Escherichia coli reacts with S-dinitrophenyl-6-mercaptopurine-riboside 5'-phosphate. In this reaction the dinitrophenyl group becomes attached to the enzyme, while the nucleotide is split off. Most aliphatic high and low-molecular-weight-SH compounds react with the thioether in the opposite way, i.e. bind the nucleotide and split off dinitrothiophenol. It appears that the dinitrophenyl moiety of the thioether interacts with the enzyme in a specific way, and that this interaction activates the bond between the dinitrophenyl group and the sulfur atom. In support of this it was found that dinitrophenol inhibits the transferase reaction with half maximal effect at 0.4 mM. The inhibition is competitive with ATP. Dinitrophenol also competes with ATP in binding studies.  (+info)

Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N-(5-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
Analysis of the redundant first step in His biosynthesis catalyzed by ATP phosphoribosyl transferase required the construction of plants heterozygous for knockout alleles of both HISN1A (At1g58080) and HISN1B (At1g09795). The mutant alleles examined contained insertions near the beginning (hisn1b-1) or middle (hisn1a-1) of the coding region. Double knockouts for other redundant HISN genes could not be constructed because confirmed insertions remain to be identified for HISN5B and HISN6B. Twenty progeny plants from a selfed double heterozygote (AaBb) segregating for both hisn1a-1 (a) and hisn1b-1 (b) were PCR genotyped and screened for defects in seed and ovule development. The following plants were identified: AABb (5), AAbb (2), AaBB (5), and AaBb (8). Despite the small sample size, these results are consistent with two important conclusions supported by further studies: reduced transmission of double knockout gametes (ab) and embryo lethality of double homozygotes (aabb). No viable double ...
Ribbon representation of the structure of an enzyme known as ATP-PRT from TB bacteria (blue), bound to an allosteric activator (pink).
In polarized epithelial cells, vectorial protein trafficking is important for transporting specific membrane proteins to generate distinct apical and basolateral membrane protein compositions. The Exocyst is a conserved hetero-octameric protein complex, which regulates different aspects of protein trafficking, including tethering of the Golgi-derived vesicles to target membranes. Two of the Exocyst subunits, Sec5 and Exo84, competitively bind to the small GTPases, RalA and RalB, in a GTP-dependent manner. Although Ral GTPases have been proposed to mediate assembly of Exocyst holocomplexes, we hypothesize that they actually serve to allosterically regulate Exocyst functions by promoting association or disassociation of additional factors. Previous studies have shown that active RalA, but not RalB, accelerated basolateral exocytosis of E-cadherin. In contrast, knockdown of RalB, but not RalA, disrupts endocytosis of E-cadherin. However, mechanisms by which association of Ral GTPases with Sec5 and Exo84
Metabolism. Shui, Wang [1], Guirong, Zhang [2], Wang, Hongyun [3], Ulanov, Alexander [3], Lozovaya, Vera [3], Lin, Yun [4]. A regulatory role of histidine in Arabidopsis metabolism and growth revealed by the low oil 1 mutant that corresponds to ATP-Phosphoribosyl Transferase 1, a key enzyme of histidine biosynthesis.. Amino acid sensory mechanisms are known to coordinate metabolism and growth in microbes and animals. However, evidence for their existence in plants has been elusive. In a genetic screen for Arabidopsis seed oil and protein deposition mutants, the low oil 1 (loo1) was isolated and map-based gene cloning identified a missense mutation in the first histidine biosynthetic enzyme ATP-phosphoribosyl transferase 1 (ATP-PRT1). The loo1 mutant exhibited development and growth defects throughout the entire lifespan. The severely retarded root elongation of loo1 seedlings was rescued by supplemental histidine in the growth medium. Transcript and metabolite profiling and real-time RT-PCR ...
TY - JOUR. T1 - Identification of novel bacterial histidine biosynthesis inhibitors using docking, ensemble rescoring, and whole-cell assays. AU - Henriksen,Signe Teuber. AU - Liu,J.. AU - Estiu,G.. AU - Oltvai,Z.N.. AU - Wiest,O.. PY - 2010. Y1 - 2010. N2 - The rapid spread on multidrug-resistant strains of Staphylococcus aureus requires not just novel treatment options, but the development of faster methods for the identification of new hits for drug development. The exponentially increasing speed of computational methods makes a more extensive use in the early stages of drug discovery attractive if sufficient accuracy can be achieved. Computational target identification using systems-level methods suggested the histidine biosynthesis pathway as an attractive target against S. aureus. Potential inhibitors for the pathway were identified through docking, followed by ensemble rescoring, that is sufficiently accurate to justify immediate testing of the identified compounds by whole-cell assays, ...
The Genetics Society of America (GSA), founded in 1931, is the professional membership organization for scientific researchers and educators in the field of genetics. Our members work to advance knowledge in the basic mechanisms of inheritance, from the molecular to the population level.. Online ISSN: 1943-2631. ...
Displaying operon conservation. Part A shows that the order of genes belonging to the histidine operon is well conserved in this set of proteobacterial genomes.
This clade of sequences is highly similar to the HisF protein, but generally represents the second HisF homolog in the genome where the other is an authentic HisF observed in the context of a complete histidine biosynthesis operon. The similarity between these WbuZ sequences and true HisFs is such that often the closest match by BLAST of a WbuZ is a HisF. Only by making a multiple sequence alignment is the homology relationship among the WbuZ sequences made apparent. WbuZ genes are invariably observed in the presence of a homolog of the HisH protein (designated WbuY) and a proposed N-acetyl sugar amidotransferase designated in WbuX in E. coli [1], IfnA in P. aeriginosa [2] and PseA in C. jejuni [3]. Similarly, this trio of genes is invariably found in the context of saccharide biosynthesis loci. It has been shown that the WbuYZ homologs are not essential components of the activity expressed by WbuX, leading to the proposal that these to proteins provide ammonium ions to the amidotransferase when ...
The Genetics Society of America (GSA), founded in 1931, is the professional membership organization for scientific researchers and educators in the field of genetics. Our members work to advance knowledge in the basic mechanisms of inheritance, from the molecular to the population level.. Online ISSN: 1943-2631. ...
Hello, This question might seem easy, but I found it not so obvious as I thought about it more: What does rate limiting mean to you ? It is used quite often, and not only in biology. The example I am dealing with is a common one, a metabolic pathway. The simplest way to see it, is that there is not RenoughS of the first enzyme on the pathway and RplentyS of the following enzymes. When more of the first enzyme is made, the flux through the pathway increases in a direct (not necessarily linear) function of this first enzyme. Does it mean that this first enzyme is used at saturation of its substrate(s) ? If not, the element that keeps those substrate(s) constant would be the real rate limiting step by providing the right flux of substrate so as to keep it constant ! If that flux does not change, an increase in the quantity and consequently in flux of the first enzyme would have the effect of lowering the concentration of its substrate until the activity was restored to its original value ! I feel ...
Steroidal glycoalkaloids (SGAs) are plant secondary metabolites known to be toxic to animals and humans and that have putative roles in defense against pests. The proposed mechanisms of SGA toxicity are sterol-mediated disruption of membranes and inhibition of cholinesterase activity in neurons. It has been suggested that phytopathogenic microorganisms can overcome SGA toxicity by enzymatic deglycosylation of SGAs. Here, we have explored SGA-mediated toxicity toward the invasive oomycete Phytophthora infestans, the causative agent of the late blight disease in potato and tomato, as well as the potential for SGA deglycosylation by this species. Our growth studies indicate that solanidine, the nonglycosylated precursor of the potato SGAs a-chaconine and a-solanine, has a greater physiological impact than its glycosylated forms. All of these compounds were incorporated into the mycelium, but only solanidine could strongly inhibit the growth of P. infestans in liquid culture. Genes encoding several ...
Histidine biosynthesis bifunctional protein HisIE; Protein involved in phosphoribosyl-AMP cyclohydrolase activity, phosphoribosyl-ATP diphosphatase activity and histidine biosynthetic process; In the N-terminal section; belongs to the PRA-CH family (213 aa ...
now, downstream data, issues, survivors, sites, data, and univariate representative RNAs could require purified via the ebook of outcomes. The ebook to enhance acid promoters with production is that the ECD-mTLR2 cell is full to introduce possible, there misconfigured to subscribe. respectively, ebook Investitionen, has acidic certain attB, and the network phosphoribosyltransferase is to be observed for a specifically new volume.
Information for Narvon ,Pennsylvania. Find community info travel, tourist, tourist and visitor information, calendars, town and travel guides, moving guides, history.
... catalyzed by ATP-phosphoribosyl transferase. Phosphoribosyl-ATP converts to phosphoribosyl-AMP (PRAMP). His4 then catalyzes the ... The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. In ... Glycolysis → Pyruvate decarboxylation → Citric acid cycle → Oxidative phosphorylation (electron transport chain + ATP synthase) ... is strongly inhibited by α-ketoglutarate feedback inhibition and can be inhibited by DPNH as well high concentrations of ATP.[5 ...
ATP-phosphoribosyl transferase (shown as His1 in the image on the right). ATP-phosphoribosyl transferase is the rate ... by the enzyme ATP-phosphoribosyl transferase. ATP-phosphoribosyl tranferase is indicated by His1 in the image. His4 gene ... This pathway requires energy in order to occur therefore, the presence of ATP activates the first enzyme of the pathway, ... The first reaction of histidine biosynthesis is the condensation of PRPP and adenosine triphosphate (ATP) ...
... phosphoribosyl ATP synthetase, phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase, phosphoribosyl-ATP:pyrophosphate- ... an ATP phosphoribosyltransferase (EC 2.4.2.17) is an enzyme that catalyzes the chemical reaction 1-(5-phospho-D-ribosyl)-ATP + ... ATP phosphoribosyltransferase is found in two distinct forms: a long form containing two catalytic domains and a C-terminal ... Histidine biosynthesis is an energetically expensive process and ATP phosphoribosyltransferase activity is subject to control ...
... anthranilate phosphoribosyltransferase MeSH D08.811.913.400.725.200 --- ATP phosphoribosyltransferase MeSH D08.811.913.400. ... 725.450 --- hypoxanthine phosphoribosyltransferase MeSH D08.811.913.400.725.700 --- orotate phosphoribosyltransferase MeSH ... atp citrate (pro-s)-lyase MeSH D08.811.913.050.350 --- carnitine acyltransferases MeSH D08.811.913.050.350.170 --- carnitine O- ... atp-dependent proteases MeSH D08.811.277.656.149.200 --- endopeptidase clp MeSH D08.811.277.656.149.500 --- protease la MeSH ...
... trafficking GUK1 Guanylate kinase transfers phosphate from ATP to GMP HPRT Hypoxanthine-guanine phosphoribosyltransferase ... 001689 Homo sapiens ATP synthase, H+ transporting, mitochondrial F0 complex, subunit c ATP5H NM_006356 Homo sapiens ATP ... ATP reservoir) Cytidine deaminase questionable: not present in very high levels at all CPNE1 ENSA (gene) FTH1 Heavy chain of ... 004046 Homo sapiens ATP synthase, H+ transporting, mitochondrial F1 complex, alpha ATP5B NM_001686 ATP5C1 NM_005174 ATP5D NM_ ...
ATP phosphoribosyltransferase EC 2.4.2.18: anthranilate phosphoribosyltransferase EC 2.4.2.19: nicotinate-nucleotide ... uracil phosphoribosyltransferase EC 2.4.2.10: orotate phosphoribosyltransferase EC 2.4.2.11: now EC 6.3.4.21 EC 2.4.2.12: ... nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase EC 2.4.2.22: xanthine phosphoribosyltransferase EC 2.4. ... adenine phosphoribosyltransferase EC 2.4.2.8: hypoxanthine phosphoribosyltransferase EC 2.4.2.9: ...
ATP, and H2O, whereas its four products are nicotinate D-ribonucleotide, diphosphate, ADP, and phosphate. This enzyme belongs ... In enzymology, a nicotinate phosphoribosyltransferase (EC 6.3.4.21) is an enzyme that catalyzes the chemical reaction ... Kosaka A, Spivey HO, Gholson RK (1971). "Nicotinate phosphoribosyltransferase of yeast. Purification and properties". J. Biol. ... and nicotinic acid phosphoribosyltransferase. This enzyme participates in nicotinate and nicotinamide metabolism. As of late ...
The synthesis of IMP, (precursor to GMP and GTP, and to AMP and ATP) also requires THF, and also can be bypassed. In this case ... hypoxanthine-guanine phosphoribosyltransferase (HGPRT) reacts hypoxanthine absorbed from the medium with PRPP, liberating ...
ATP stimulates production of GTP, while GTP stimulates production of ATP. This cross regulation keeps the relative amounts of ... Lesch-Nyhan syndrome is caused by a deficiency in hypoxanthine-guanine phosphoribosyltransferase or HGPRT, the enzyme that ... Production of IMP from PRPP requires glutamine, glycine, aspartate, and 6 ATP, among other things.[1] IMP is then converted to ... XMP is then converted into GMP by using the hydrolysis of 1 ATP and the conversion of glutamine to glutamate.[1] AMP and GMP ...
Both steps are fueled by ATP hydrolysis: ATP + UMP → ADP + UDP UDP + ATP → UTP + ADP CTP is subsequently formed by amination of ... Orotate phosphoribosyltransferase (PRPP transferase) catalyzes the net reaction yielding orotidine monophosphate (OMP): Orotate ... Glutamine is the NH3 donor and the reaction is fueled by ATP hydrolysis, too: UTP + Glutamine + ATP + H2O → CTP + ADP + Pi ... to PRPP by reacting it with ATP. The reaction is unusual in that a pyrophosphoryl group is directly transferred from ATP to C1 ...
ATP) EC 6.5.1.2: DNA ligase (NAD+) EC 6.5.1.3: RNA ligase (ATP) EC 6.5.1.4: RNA-3'-phosphate cyclase EC 6.6.1.1: magnesium ... nicotinate phosphoribosyltransferase EC 6.3.5.1: NAD+ synthase (glutamine-hydrolysing) EC 6.3.5.2: GMP synthase (glutamine- ... ATP-hydrolysing)) ligase EC 6.3.4.11: biotin-(methylcrotonoyl-CoA-carboxylase) ligase EC 6.3.4.12: glutamate-methylamine ligase ...
Importantly, the process in the organelle has no net ATP synthesis. This ATP comes later from processes outside of the ... These enzymes found in the glycosome to help with synthesis are guanine and adenine phosphoribosyl transferase, hypoxanthine, ... This energy metabolism generates ATP through the process of glycolysis. The glycosome is a host of the main glycolytic enzymes ... the glycosomes attached to the myofibrils seem to serve the myosin by providing energy substrates for generation of ATP through ...
fGAR + L-Glutamine + ATP → fGAM + L-Glutamate + ADP + Pi The fifth is catalyzed by AIR synthetase (FGAM cyclase). fGAM + ATP → ... The enzyme adenine phosphoribosyltransferase (APRT) salvages adenine. The enzyme hypoxanthine-guanine phosphoribosyltransferase ... CAIR + L-Aspartate + ATP → SAICAR + ADP + Pi The eight is catalyzed by adenylosuccinate lyase. SAICAR → AICAR + Fumarate The ... PRPP + L-Glutamine + H2O → PRA + L-Glutamate + PPi In the second step react PRA, glycine and ATP to create GAR, ADP, and ...
hypoxanthine/guanine phosphoribosyl transferase (HGPRT). IMP guanine. hypoxanthine/guanine phosphoribosyl transferase (HGPRT). ... Glycolysis → Pyruvate decarboxylation → Citric acid cycle → Oxidative phosphorylation (electron transport chain + ATP synthase) ... There are two types of phosphoribosyltransferases: adenine phosphoribosyltransferase (APRT) and hypoxanthine-guanine ... adenine phosphoribosyltransferase (APRT). AMP Folate biosynthesis[edit]. Tetrahydrofolic acid and its derivatives are produced ...
ATP-hydrolysing) Serine racemase Category:EC 5.1.2 Mandelate racemase Category:EC 5.1.3 UDP-glucose 4-epimerase Category:EC 5.1 ... EC 2.4.2 Hypoxanthine-guanine phosphoribosyltransferase EC 2.4.2.8 Category:EC 2.5 Category:EC 2.5.1 Thiaminase EC 2.5.1.2 ... ATP synthase (EC 3.6.3.14) Kynureninase EC 3.7.1.3 EC 3.8.1.3 Haloacetate dehalogenase Category:EC 4.1.1 Ornithine ...
These may be metal ions, vitamin derivatives such as NADH and acetyl CoA, or non-vitamin derivatives such as ATP. In the case ... It is caused by the absence of hypoxanthine-guanine phosphoribosyltransferase, which is a necessary enzyme for purine ... The first step for joining an amino acid to its corresponding tRNA is the formation of aminoacyl-AMP: Amino acid + ATP ↽ − − ⇀ ... The following step requires the activation of glycine by the addition of a phosphate group from ATP. GAR synthetase performs ...
Functional Consequences of ATP- and dATP-Induced Oligomerization of the Large Subunit†". Biochemistry. 41 (2): 462-74. doi: ... "Different Oligomeric States are Involved in the Allosteric Behavior of Uracil Phosphoribosyltransferase from Escherichia Coli ... W in Complex with Nonhydrolyzable ATP Analogues Reveal a Putative Active Conformation of the Enzyme as a Result of Domain ... Dependent Malic Enzyme by ATP and Fumarate". Structure. 10 (7): 951-60. doi:10.1016/S0969-2126(02)00788-8. PMID 12121650. ...
Alternatively to ATP, GTP has been shown to act comparably as a phosphate donor. This promiscuity enables the important role ... "Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase". BMC ... hydroxyl group on the substrate and activates it to attack the γ-phosphorus of ATP. Structural analyses have shown that the ...
An increase in ATP concentration opposes this activation by displacing AMP from the nucleotide binding site, indicating ... Phosphoribosyltransferase. *Adenine phosphoribosyltransferase. *Hypoxanthine-guanine phosphoribosyltransferase. *Uracil ... Phosphorylase b is normally in the T state, inactive due to the physiological presence of ATP and Glucose 6 phosphate, and ...
... which leads to ATP-mediated efflux of chloride ions and leads to secretion of H2O, Na+, K+, and HCO3− into the intestinal lumen ... Phosphoribosyltransferase. *Adenine phosphoribosyltransferase. *Hypoxanthine-guanine phosphoribosyltransferase. *Uracil ...
ATP synthase (EC 3.6.3.14). Category:EC 3.7 (act on carbon-carbon bonds)Edit. *Kynureninase EC 3.7.1.3 ... Hypoxanthine-guanine phosphoribosyltransferase EC 2.4.2.8. Category:EC 2.5 *Category:EC 2.5.1 *Thiaminase EC 2.5.1.2 ...
This interference has a dual action, both increasing the conversion of ATP to inosine and hence uric acid and increasing the ... Adenine phosphoribosyltransferase deficiency. Catabolism. *Adenosine deaminase deficiency. *Purine nucleoside phosphorylase ...
ATP-phosphoribosyl transferase (shown as His1 in the image on the right). ATP-phosphoribosyl transferase is the rate ... by the enzyme ATP-phosphoribosyl transferase. ATP-phosphoribosyl tranferase is indicated by His1 in the image.[13] His4 gene ... This pathway requires energy in order to occur therefore, the presence of ATP activates the first enzyme of the pathway, ... The first reaction of histidine biosynthesis is the condensation of PRPP and adenosine triphosphate (ATP) ...
ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by ... Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N-(5-phosphoribosyl)- ... IPR013820 ATP_PRibTrfase_cat. IPR018198 ATP_PRibTrfase_CS. IPR001348 ATP_PRibTrfase_HisG. IPR020621 ATP_PRibTrfase_HisG_long. ... IPR013820 ATP_PRibTrfase_cat. IPR018198 ATP_PRibTrfase_CS. IPR001348 ATP_PRibTrfase_HisG. IPR020621 ATP_PRibTrfase_HisG_long. ...
... phosphoribosyl ATP synthetase, phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase, phosphoribosyl-ATP:pyrophosphate- ... an ATP phosphoribosyltransferase (EC 2.4.2.17) is an enzyme that catalyzes the chemical reaction 1-(5-phospho-D-ribosyl)-ATP + ... ATP phosphoribosyltransferase is found in two distinct forms: a long form containing two catalytic domains and a C-terminal ... Histidine biosynthesis is an energetically expensive process and ATP phosphoribosyltransferase activity is subject to control ...
hisG; ATP phosphoribosyltransferase; Reviewed. TIGR03455. Location:202 → 293. HisG_C-term; ATP phosphoribosyltransferase, C- ... ATP phosphoribosyltransferase. YP_009339.1. *EC 2.4.2.17. *long form of enzyme; catalyzes the formation of N-5-phosphoribosyl ... ATP phosphoribosyltransferase. Locus tag. DVU0114. Gene type. protein coding. RefSeq status. REVIEWED. Organism. Desulfovibrio ... hisG ATP phosphoribosyltransferase [ Desulfovibrio vulgaris str. Hildenborough ] Gene ID: 2794983, updated on 29-Aug-2016 ...
ATP phosphoribosyltransferase. NP_721647.1. *Best Blastp Hit: sp,Q02129,HIS1_LACLA ATP PHOSPHORIBOSYLTRANSFERASE ,gi,478062,pir ... ATP phosphoribosyltransferase. Locus tag. SMU_1271. Gene type. protein coding. RefSeq status. PROVISIONAL. Organism. ... NP_721647.1 ATP phosphoribosyltransferase [Streptococcus mutans UA159]. See identical proteins and their annotated locations ... hisG ATP phosphoribosyltransferase [ Streptococcus mutans UA159 ] Gene ID: 1028559, updated on 30-Jan-2018 ...
The Structure of Escherichia Coli ATP-Phosphoribosyltransferase: Identification of Substrate Binding Sites and Mode of AMP ... ATP phosphoribosyltransferase (ATP-PRTase, HisG), regulatory C- terminal domain ATP phosphoribosyltransferase (ATP-PRTase, HisG ... ATP phosphoribosyltransferase (ATP-PRTase, HisG), catalytic domain Escherichia coli [TaxId: 562] A225-299. d1h3da2. Alpha and ...
The crystal structure of an ATP phosphoribosyltransferase regulatory subunit/histidyl-tRNA synthetase from Bacillus halodurans ... ATP phosphoribosyltransferase regulatory subunit. A, B. 400. Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 ... The crystal structure of an ATP phosphoribosyltransferase regulatory subunit/histidyl-tRNA synthetase from Bacillus halodurans ... The crystal structure of aATP phosphoribosyltransferase regulatory subunit/histidyl-tRNA synthetase from Bacillus halodurans C ...
NAMPT Deficiency Potentiates ATP Depletion by Methotrexate. Rakesh K. Singh, Leon van Haandel, Daniel P. Heruth, Shui Q. Ye, J ... NAMPT Deficiency Potentiates ATP Depletion by Methotrexate. Rakesh K. Singh, Leon van Haandel, Daniel P. Heruth, Shui Q. Ye, J ... Lower plasma nicotinamide phosphoribosyltransferase (NAMPT) levels are associated with improved response to methotrexate (MTX) ... Nicotinamide Phosphoribosyltransferase Deficiency Potentiates the Antiproliferative Activity of Methotrexate through Enhanced ...
H31 ATP phosphoribosyltransferase(hisG). It is produced in Yeast. High purity. Good price. ... Recommended name: ATP phosphoribosyltransferase Short name= ATP-PRT Short name= ATP-PRTase EC= 2.4.2.17 ... Recombinant Escherichia coli O6:K15:H31 ATP phosphoribosyltransferase(hisG). Recombinant Escherichia coli O6:K15:H31 ATP ... Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N-(5-phosphoribosyl)-ATP (PR-ATP). Has a crucial ...
Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like ... The molecular structure of the ATP phosphoribosyl transferase from the hyperthermophile Thermotoga maritima is composed of a ... The molecular structure of the ATP phosphoribosyl transferase from the hyperthermophile Thermotoga maritima is composed of a ... 2 ATP phosphoribosyl transferases that is functional in the absence of additional regulatory subunits, the structure of the ...
Bacillus pumilus ATP phosphoribosyltransferase (hisG) datasheet and description hight quality product and Backed by our ... ATP phosphoribosyltransferase, ATP phosphoribosyltransferase catalytic subunit, ATP phosphoribosyltransferase catalytic subunit ... Bacillus pumilus ATP phosphoribosyltransferase (hisG). Alternative name: Bacillus pumilus adenosine triphosphate ... ATP-PRT, ATP-PRTase, hisG, hisG. General description: All of our recombinant proteins are manufactured in strictly controlled ...
Crystals of ATP-phosphoribosyltransferase from E. coli were obtained by the vapour-diffusion method and diffract to 2.7 Å. The ... Purification, crystallization and preliminary X-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia ...
ATP phosphoribosyltransferase (hisG). *no protein annotated in this organism. *Phosphoribosyl-AMP cyclohydrolase (hisI) ...
KW ATP phosphoribosyltransferase; bZIP transcription factor; cut7; KW his1; histidine biosynthesis; kinesin; rec10; ribosomal ...
ATP phosphoribosyltransferase (hisG). *Phosphoribosyl-ATP pyrophosphatase (hisE). *Phosphoribosyl-AMP cyclohydrolase (hisI). *1 ... tr,A0A3G8JHN8,A0A3G8JHN8_9ACTN Phosphoribosyl-ATP pyrophosphatase OS=Gordonia sp. MMS17-SY073 OX=2420509 GN=hisE PE=3 SV=1 ... 1-(5-phospho-β-D-ribosyl)-ATP*Search proteins in UniProtKB for this molecule. ... 1-(5-phospho-β-D-ribosyl)-ATP*Search proteins in UniProtKB for this molecule. ...
K00765 hisG; ATP phosphoribosyltransferase [EC:2.4.2.17] K02502 hisZ; ATP phosphoribosyltransferase regulatory subunit K11755 ... ABAYE3132 hisG; ATP-phosphoribosyltransferase ABAYE2593 hisZ; ATP phosphoribosyltransferase ABAYE3428 hisIE; bifunctional ... ATP) [EC:2.7.1.107] K00635 E2.3.1.20; diacylglycerol O-acyltransferase [EC:2.3.1.20] K01046 E3.1.1.3; triacylglycerol lipase [ ... hisIE; phosphoribosyl-ATP pyrophosphohydrolase / phosphoribosyl-AMP cyclohydrolase [EC:3.6.1.31 3.5.4.19] K01814 hisA; ...
Atp Phosphoribosyltransferase. An enzyme that catalyzes the first step of the pathway for histidine biosynthesis in Salmonella ... ATP reacts reversibly with 5-phosphoribosyl-1-pyrophosphate to yield N-1-(5-phosphoribosyl)-ATP and pyrophosphate. EC 2.4.2.17 ...
Atp Phosphoribosyltransferase. An enzyme that catalyzes the first step of the pathway for histidine biosynthesis in Salmonella ... ATP reacts reversibly with 5-phosphoribosyl-1-pyrophosphate to yield N-1-(5-phosphoribosyl)-ATP and pyrophosphate. EC 2.4.2.17 ...
... catalyzed by ATP-phosphoribosyl transferase. Phosphoribosyl-ATP converts to phosphoribosyl-AMP (PRAMP). His4 then catalyzes the ... The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. In ... Glycolysis → Pyruvate decarboxylation → Citric acid cycle → Oxidative phosphorylation (electron transport chain + ATP synthase) ... is strongly inhibited by α-ketoglutarate feedback inhibition and can be inhibited by DPNH as well high concentrations of ATP.[5 ...
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000255,HAMAP-Rule:MF_01018}; DE Short=ATP-PRT {ECO:0000255,HAMAP-Rule:MF_ ... DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB- ... DR InterPro; IPR018198; ATP_PRibTrfase_CS. DR InterPro; IPR001348; ATP_PRibTrfase_HisG. DR InterPro; IPR024893; ATP_PRibTrfase_ ... CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. CC Short subfamily. {ECO:0000255,HAMAP-Rule:MF_01018}. ...
atp phosphoribosyltransferase. 100. CA/Fungi. 11. Coral. Seriatopora_8296. glyoxalase. 98. Bact. ... Maximum likelihood tree of an exonuclease-endonucease-phosphatase (EEP) domain-containing protein (A), an ATP-dependent ...
Accepted name: ATP phosphoribosyltransferase Reaction: 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-α-D-ribose 1 ... phosphoribosyl ATP synthetase; phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase; phosphoribosyl-ATP:pyrophosphate- ... EC 2.4.2.17 ATP phosphoribosyltransferase EC 2.4.2.18 anthranilate phosphoribosyltransferase EC 2.4.2.19 nicotinate-nucleotide ... Systematic name: ATP:3-dephospho-CoA 5-triphosphoribosyltransferase. Comments: ATP cannot be replaced by GTP, CTP, UTP, ADP or ...
... hypoxanthine phosphoribosyltransferase; ATP5O, ATP synthase; EF1A1, elongation factor 1 alpha; NQO1, NADP-quinone reductase 1; ...
... hypoxanthine phosphoribosyltransferase; ATP5O, ATP synthase; EF1A1, elongation factor 1 alpha; NQO1, NADP-quinone reductase 1; ...
ATP-phosphoribosyltransferase (ATP-PRT), the first enzyme of the histidine pathway, is a complex allosterically regulated ... The Structure of Escherichia coli ATP-phosphoribosyltransferase: Identification of Substrate Binding Sites and Mode of AMP ... The Structure of Escherichia coli ATP-phosphoribosyltransferase: Identification of Substrate Binding Sites and Mode of AMP ... The Structure of Escherichia coli ATP-phosphoribosyltransferase: Identification of Substrate Binding Sites and Mode of AMP ...
Mechanism of Feedback Allosteric Inhibition of ATP Phosphoribosyltransferase, BIOCHEMISTRY, Vol: 51, Pages: 8027-8038, ISSN: ... Citrobacter rodentium Subverts ATP Flux and Cholesterol Homeostasis in Intestinal Epithelial Cells In Vivo, CELL METABOLISM, ... Hybrid Mass Spectrometry Approaches to Determine How L-Histidine Feedback Regulates the Enzyzme MtATP-Phosphoribosyltransferase ...
  • This study aimed at evaluating the concentration of erythrocyte purine nucleotides (ATP, ADP, AMP, IMP) in trained and sedentary subjects before and after maximal physical exercise together with measuring the activity of purine metabolism enzymes as well as the concentration of purine (hypoxanthine, xanthine, uric acid) and pyrimidine (uridine) degradation products in blood. (springer.com)
  • The concentrations of ATP, ADP, AMP, IMP and the activities of adenine phosphoribosyltransferase (APRT), hypoxanthine-guanine phosphoribosyltransferase (HGPRT) and phosphoribosyl pyrophosphate synthetase (PRPP-S) were determined in erythrocytes. (springer.com)
  • This study investigates the enzymatic activity of energy related and salvage related enzymes, glyceraldehyde-3-phosphate dehydrogenase, pyruvate kinase, lactate dehydrogenase, aspartate aminotransferase, malate dehydrogenase, cytochrome C oxidase, ATP synthase, and hypoxanthine-guanine phosphoribosyltransferase, that have been identified as excessively nitrated following the administration of GCEE post-TBI. (eku.edu)
  • Because effects of febuxostat were canceled by silencing of the hypoxanthine phosphoribosyl transferase 1 gene in cultured tubular cells, mechanisms for the renoprotective effects appear to involve the purine salvage pathway, which uses hypoxanthine to resynthesize adenine nucleotides, including ATP. (jci.org)
  • These include a complete deficiency of hypoxanthine guanine phosphoribosyltransferase (HGPRT) as in Lesch-Nyhan syndrome, partial deficiency of HGPRT (Kelley-Seegmiller syndrome), and increased production of 5-phospho-alpha-d-ribosyl pyrophosphate (PRPP) activity. (medscape.com)
  • D45734 ATP phosphoribosyltransferase (EC 2.4.2.17) [similarity] - Lactococcus lactis subsp. (nih.gov)
  • In enzymology, an ATP phosphoribosyltransferase (EC 2.4.2.17) is an enzyme that catalyzes the chemical reaction 1-(5-phospho-D-ribosyl)-ATP + diphosphate ⇌ {\displaystyle \rightleftharpoons } ATP + 5-phospho-alpha-D-ribose 1-diphosphate Thus, the two substrates of this enzyme are 1-(5-phospho-D-ribosyl)-ATP and diphosphate, whereas its two products are ATP and 5-phospho-alpha-D-ribose 1-diphosphate. (wikipedia.org)
  • RYR2-mediated Ca 2+ fluxes are therefore proximal controllers of mitochondrial Ca 2+ , ATP levels, and a cascade of transcription factors controlling metabolism and survival. (pubmedcentralcanada.ca)
  • Intracellular pyridine nucleotides, ATP, mitochondrial function, viability, proliferation, activation markers and cytokine secretion were assessed in resting and in activated human T lymphocytes. (harvard.edu)
  • Major role in the synthesis of nucleoside triphosphates other than ATP. (hmdb.ca)
  • 4 Importance of nucleotides: Building blocks of nucleic acids - DNA and RNA Act as co-enzymes - FAD, NAD, NADP Second messengers - cAMP and cGMP Energy currency - ATP and GTP Nucleoside and nucleotide analogs - treatment of cancer. (slideplayer.com)
  • ATP reacts reversibly with 5-phosphoribosyl-1-pyrophosphate to yield N-1-(5'-phosphoribosyl)-ATP and pyrophosphate. (bioportfolio.com)
  • The resulting compound then reacts with an ATP phosphoribosyltransferase resulting in the release of pyrophosphate and 1-(5-phosphoribosyl)-ATP. (smpdb.ca)
  • This compound interacts with water and phosphoribosyl pyrophosphate through an ATP driven nicotinate phosphoribosyltransferase resulting in the release of ADP, pyrophosphate and phosphate and nicotinate beta-D-ribonucleotide. (smpdb.ca)
  • This compound interacts with ATP and hydrogen ion through NadR DNA-binding transcriptional repressor and NMN adenylyltransferase resulting in pyrophosphate and NAD. (smpdb.ca)
  • Nicotinate beta-D-ribonucleotide is adenylated through the interaction with ATP and a hydrogen ion through a nicotinate-mononucleotide adenylyltransferase resulting in pyrophosphate and Nicotinic acid adenine dinucleotide. (smpdb.ca)
  • ATP-binding cassette transporter ABCA1, a gene involved in the cellular lipid removal pathway is over-expressed in resistant M14 melanoma as compared to the sensitive MDA-MB-231 breast cancer cells. (biomedcentral.com)
  • ATP-PRT activity is modulated by two layers of regulation: active site inhibition by adenosine monophosphate, which reflects cellular energy levels, and pathway end product feedback inhibition by histidine. (canterbury.ac.nz)
  • Genetic and biochemical characterization of Corynebacterium glutamicum ATP phosphoribosyltransferase and its three mutants resistant to feedback inhibition by histidine. (cas.cn)
  • ATP phosphoribosyltransferase is found in two distinct forms: a long form containing two catalytic domains and a C-terminal regulatory domain, and a short form in which the regulatory domain is missing. (wikipedia.org)
  • Two distinctly different forms of ATP-PRT exist, the long form and the short form, which differ in the presence of a C-terminal regulatory domain. (canterbury.ac.nz)
  • In the long form ATP-PRT histidine binds to the allosteric site at the regulatory domain, but the exact nature of the inhibitory mechanism is still debated. (canterbury.ac.nz)
  • The existence of a regulatory response to the level of histidine was further supported by the modified development of rosette leaves, flowers, and siliques in transgenic lines over-expressing ATP-PRT1 or ATP-PRT2 . (botanyconference.org)
  • ATP-PRT also represents a metabolic control point, directing the flux of metabolites through this energetically expensive pathway. (canterbury.ac.nz)
  • An XOD inhibitor, febuxostat, which blocks the degradation pathway of adenine nucleotides, promoted ATP recovery and exerted renoprotective effects in the postischemic kidney. (jci.org)
  • The study demonstrated a significantly higher concentration of ATP in the erythrocytes of trained subjects which, in part, may be explained by higher metabolic activity on the purine re-synthesis pathway (significantly higher PRPP-S, APRT and HGPRT activities). (springer.com)
  • The systematic name of this enzyme class is 1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-alpha-D-ribosyl-transferase. (wikipedia.org)
  • It is a member of the larger phosphoribosyltransferase superfamily of enzymes which catalyse the condensation of 5-phospho-alpha-D-ribose 1-diphosphate with nitrogenous bases in the presence of divalent metal ions. (wikipedia.org)
  • These results suggest that purine salvage in dolphins could be a mechanism for delivering nucleotide precursors to tissues with high ATP and guanosine triphosphate requirements. (cibnor.mx)
  • In E. coli citrate synthase, the enzyme involved in the condensation reaction initiating the Citric Acid Cycle is strongly inhibited by α-ketoglutarate feedback inhibition and can be inhibited by DPNH as well high concentrations of ATP. (wikipedia.org)
  • This thesis characterises a new member of the ATP-PRT long form from Campylobacter jejuni (CjeATP-PRT) and investigates the molecular mechanisms involved in the feed back inhibition by histidine. (canterbury.ac.nz)
  • In summary this thesis supports the existence of a simple physical regulatorymechanism for the feedback inhibition of the ATP-PRT long form, the change between two different hexamer conformations depending on the presence of the allosteric effector. (canterbury.ac.nz)
  • For example, in vitro studies have shown that Ca 2+ flux through channels such as ryanodine receptors and IP 3 receptors mediate privileged communication between endoplasmic reticulum/sarcoplasmic reticulum (ER/SR) 3 and mitochondria and that this paces cellular metabolism by stimulating oxidative ATP production via interaction with TCA cycle enzymes ( 2 - 4 ). (pubmedcentralcanada.ca)
  • Glycolysis requires relatively more NAD to generate ATP compared to the oxidative phosphorylation normally occurring in non-malignant tissues. (biomedcentral.com)
  • The oxidative branch is mainly related to the production of ATP and reducing equivalents (NADH), with the formation of acetic and butyric acids as byproducts. (biomedcentral.com)
  • During oxygen deprivation, adenosine triphosphate (ATP) breakdown implies purine metabolite accumulation, which in humans is associated with pathological conditions. (cibnor.mx)
  • The lower concentrations of purine catabolism and recycling by-products in plasma from dolphins could be beneficial in providing substrates for recovery of ATP depleted during diving or vigorous swimming. (cibnor.mx)
  • SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. (univ-lyon1.fr)
  • Glycogenoses types III, IV, and VII can result in hyperuricemia from excessive degradation of skeletal muscle ATP. (medscape.com)
  • b) The first step of the ATP-dependent aminoacylation reaction activates amino acid to generate an aminoacyl adenylate intermediate. (schoolbag.info)
  • First, an amino acid is activated via ATP to form an aminoacyl adenylate intermediate. (schoolbag.info)
  • The C. jejuni enzyme is similar to the previously described enzymes of the ATP-PRT long form, but exists only as hexameric species under experimental conditions, which contradicts previous assumptions that the hexamer is exclusively inactive. (canterbury.ac.nz)