An enzyme that catalyzes the formation of N-5'-phosphoribosylanthranilic acid from anthranilate and phosphoribosylpyrophosphate, the first step in tryptophan synthesis in E. coli. It exists in a complex with ANTHRANILATE SYNTHASE in bacteria. EC 2.4.2.18.
Pentosyltransferases that catalyze the reaction between a pyrimidine nucleoside and orthophosphate to form a free pyrimidine and ribose-5-phosphate.
An enzyme that catalyzes the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine. Anthranilate is the biosynthetic precursor of tryptophan and numerous secondary metabolites, including inducible plant defense compounds. EC 4.1.3.27.
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.
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.
Enzymes of the transferase class that catalyze the transfer of a pentose group from one compound to another.
Benzoic acids, salts, or esters that contain an amino group attached to carbon number 2 or 6 of the benzene ring structure.
The enzyme catalyzing the formation of orotidine-5'-phosphoric acid (orotidylic acid) from orotic acid and 5-phosphoribosyl-1-pyrophosphate in the course of pyrimidine nucleotide biosynthesis. EC 2.4.2.10.
An enzyme that catalyzes the formation of nicotinamide mononucleotide (NMN) from nicotinamide and 5-phosphoribosyl-1-pyrophosphate, the rate-limiting step in the biosynthesis of the NAD coenzyme. It is also known as a growth factor for early B-LYMPHOCYTES, or an ADIPOKINE with insulin-mimetic effects (visfatin).
An inherited disorder transmitted as a sex-linked trait and caused by a deficiency of an enzyme of purine metabolism; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE. Affected individuals are normal in the first year of life and then develop psychomotor retardation, extrapyramidal movement disorders, progressive spasticity, and seizures. Self-destructive behaviors such as biting of fingers and lips are seen frequently. Intellectual impairment may also occur but is typically not severe. Elevation of uric acid in the serum leads to the development of renal calculi and gouty arthritis. (Menkes, Textbook of Child Neurology, 5th ed, pp127)

Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus. (1/37)

Anthranilate phosphoribosyltransferase (TrpD; EC 2.4.2.18) from the hyperthermophilic archaeon Sulfolobus solfataricus (ssTrpD) was expressed in Escherichia coli, purified and crystallized. Analytical gel permeation chromatography revealed a homodimeric composition of the enzyme. The steady-state kinetic characteristics suggest tight binding of the substrate anthranilic acid and efficient catalysis at the physiological growth temperature of S. solfataricus. Crystals of ssTrpD diffract to better than 2.6 A resolution and preliminary X-ray characterization was carried out. The crystals are suitable for structure determination.  (+info)

Replacement of the yeast TRP4 3' untranslated region by a hammerhead ribozyme results in a stable and efficiently exported mRNA that lacks a poly(A) tail. (2/37)

The mRNA poly(A) tail serves different purposes, including the facilitation of nuclear export, mRNA stabilization, efficient translation, and, finally, specific degradation. The posttranscriptional addition of a poly(A) tail depends on sequence motifs in the 3' untranslated region (3' UTR) of the mRNA and a complex trans-acting protein machinery. In this study, we have replaced the 3' UTR of the yeast TRP4 gene with sequences encoding a hammerhead ribozyme that efficiently cleaves itself in vivo. Expression of the TRP4-ribozyme allele resulted in the accumulation of a nonpolyadenylated mRNA. Cells expressing the TRP4-ribozyme mRNA showed a reduced growth rate due to a reduction in Trp4p enzyme activity. The reduction in enzyme activity was not caused by inefficient mRNA export from the nucleus or mRNA destabilization. Rather, analyses of mRNA association with polyribosomes indicate that translation of the ribozyme-containing mRNA is impaired. This translational defect allows sufficient synthesis of Trp4p to support growth of trp4 cells, but is, nevertheless, of such magnitude as to activate the general control network of amino acid biosynthesis.  (+info)

Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry. (3/37)

The crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism.  (+info)

The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum. (4/37)

The structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum has been solved at 2.4 A in complex with Mn(2+)-pyrophosphate, and at 1.9 A without ligands. The enzyme structure has a novel phosphoribosyltransferase (PRT) fold and displays close homology to the structures of pyrimidine nucleoside phosphorylases. The enzyme is a homodimer with a monomer of 345 residues. Each monomer consists of two subdomains, alpha and alpha/beta, which form a cleft containing the active site. The nature of the active site is inferred from the trapped MnPPi complex and detailed knowledge of the active sites of nucleoside phosphorylases. With the anthranilate (An)PRT structure solved, the structures of all the enzymes required for tryptophan biosynthesis are now known.  (+info)

Anthranilate synthase can generate sufficient phosphoribosyl amine for thiamine synthesis in Salmonella enterica. (5/37)

In bacteria, the biosynthetic pathway for the hydroxymethyl pyrimidine moiety of thiamine shares metabolic intermediates with purine biosynthesis. The two pathways branch after the compound aminoimidazole ribotide. Past work has shown that the first common metabolite, phosphoribosyl amine (PRA), can be generated in the absence of the first enzyme in purine biosynthesis, PurF. PurF-independent PRA synthesis is dependent on both strain background and growth conditions. Standard genetic approaches have not identified a gene product singly responsible for PurF-independent PRA formation. This result has led to the hypothesis that multiple enzymes contribute to PRA synthesis, possibly as the result of side products from their dedicated reaction. A mutation that was able to restore PRA synthesis in a purF gnd mutant strain was identified and found to map in the gene coding for the TrpD subunit of the anthranilate synthase (AS)-phosphoribosyl transferase (PRT) complex. Genetic analyses indicated that wild-type AS-PRT was able to generate PRA in vivo and that the P362L mutant of TrpD facilitated this synthesis. In vitro activity assays showed that the mutant AS was able to generate PRA from ammonia and phosphoribosyl pyrophosphate. This work identifies a new reaction catalyzed by AS-PRT and considers it in the context of cellular thiamine synthesis and metabolic flexibility.  (+info)

The importance of surface loops for stabilizing an eightfold beta alpha barrel protein. (6/37)

An important step in understanding how a protein folds is to determine those regions of the sequence that are critical to both its stability and its folding pathway. We chose phosphoribosyl anthranilate isomerase from Escherichia coli, which is a monomeric representative of the (beta alpha)8 barrel family of proteins, to construct a variant that carries an internal tandem duplication of the fifth beta alpha module. This (beta alpha)9 variant was enzymically active and therefore must have a wild-type (beta alpha)8 core. It had a choice a priori to fold to three different folding frames, which are distinguished by carrying the duplicated segment as an insert into one out of three different loops. Steady-state kinetic constants, the fluorescence properties of a crucial tryptophan residue, and limited proteolysis showed that the stable (beta alpha)9 variant carries the insertion between beta-strand 5 and alpha-helix 5. This preference can be explained by the important role of loops between alpha helices and beta strands in stabilizing the structure of the enzyme.  (+info)

Sequence-specific initiator elements focus initiation of transcription to distinct sites in the yeast TRP4 promoter. (7/37)

Transcription from the yeast TRP4 promoter initiates at two basal (i127 and i76) and three GCN4 dependent (i31, i25 and i12) initiator elements. All of these elements contain not more than one deviation from the earlier proposed initiator consensus sequence PuPuPyPuPu, a pyrimidine nucleotide flanked on either side by two purine nucleotides. A point mutation analysis of these elements in various combinations was performed and revealed that the central pyrimidine nucleotide and at least one of the 3' flanking purine nucleotides of the PuPuPyPuPu consensus sequence are essential but alone not sufficient to define a functional initiator element. Multiple cryptic transcription start sites, which function independently whether they are located on the coding or the non-coding strand, can replace the function of mutated initiator elements and therefore the overall level of transcription initiation is not affected. The sequence specificity is identical for basal and GCN4 dependent initiator elements demonstrating that they are functionally homologous. These findings imply that the role of initiator elements is to 'focus' the start point(s) of transcription to distinct sites located in the region between the site(s) of the assembly of the transcriptional complex and the start codon of translation.  (+info)

Genes for tryptophan biosynthesis in the halophilic archaebacterium Haloferax volcanii: the trpDFEG cluster. (8/37)

Tryptophan auxotrophs of the archaebacterium Haloferax volcanii define a cluster of overlapping genes homologous to eubacterial-eukaryotic trpD, -F, -E, and -G, linked in that order and each preceded by a possible ribosome binding site. Residues involved in feedback inhibition of eubacterial anthranilate synthetases are conserved.  (+info)

Anthranilate phosphoribosyltransferase from the hyperthermophilic archaeon Sulfolobus solfataricus (ssAnPRT) is encoded by the sstrpD gene and catalyzes the reaction of anthranilate (AA) with a complex of Mg(2+) and 5-phosphoribosyl-alpha1-pyrophosphate (Mg.PRPP) to N-(5-phosphoribosyl)-anthranilate (PRA) and pyrophosphate (PP(i)) within tryptophan biosynthesis. The ssAnPRT enzyme is highly thermostable (half-life at 85 degrees C = 35 min) but only marginally active at ambient temperatures (turnover number at 37 degrees C = 0.33 s(-1)). To understand the reason for the poor catalytic proficiency of ssAnPRT, we have isolated from an sstrpD library the activated ssAnPRT-D83G + F149S double mutant by metabolic complementation of an auxotrophic Escherichia coli strain. Whereas the activity of purified wild-type ssAnPRT is strongly reduced in the presence of high concentrations of Mg(2+) ions, this inhibition is no longer observed in the double mutant and the ssAnPRT-D83G single mutant. The ...
3R6C: The Substrate Capture Mechanism of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Provides a Mode for Inhibition.
2BPQ: The Crystal Structure of Trpd, a Metabolic Enzyme Essential for Lung Colonization by Mycobacterium Tuberculosis, in Complex with its Substrate Phosphoribosylpyrophosphate
SWISS-MODEL Repository entry for A1U6H0 (TRPD_MARHV), Anthranilate phosphoribosyltransferase. Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
BA000012.MLR0614 Location/Qualifiers FT CDS 479468..480478 FT /codon_start=1 FT /transl_table=11 FT /gene=mlr0614 FT /product=anthranilate phosphoribosyltransferase FT /db_xref=EnsemblGenomes-Gn:BAB48169 FT /db_xref=EnsemblGenomes-Tr:BAB48169 FT /db_xref=GOA:Q98ME4 FT /db_xref=InterPro:IPR000312 FT /db_xref=InterPro:IPR005940 FT /db_xref=InterPro:IPR017459 FT /db_xref=InterPro:IPR035902 FT /db_xref=InterPro:IPR036320 FT /db_xref=UniProtKB/Swiss-Prot:Q98ME4 FT /protein_id=BAB48169.1 FT /translation=MSALKTHIAKVAAGTALSFEEAREAFDIIMSGDATPGQIGGFLMA FT LRVRGETVSEISGAVATMRAKMLRVEAPAGAIDIVGTGGDNSHSVNISTGSAFVIAAAG FT VPVAKHGNRGLSSLTGAADVLIALGVKIDIPPDAIGRCIHEAGVGFMFAPAHHPAMKHV FT GPTRVELGTRTIFNLLGPLSNPAGVVRQMVGVFLPEWILPVAETLKALGTEHAWVVHGD FT GYDEITTTGETQVAELIGGEIRSFTLTPEEVGLKRHTKDELRGGDAAYNANALRDMLDG FT AAGAYRDTVLMNAGAGLVIAGKATTLGDGIALAAQAIDSGRALQVLDRLVEISNG MSALKTHIAK VAAGTALSFE EAREAFDIIM SGDATPGQIG GFLMALRVRG ETVSEISGAV 60 ATMRAKMLRV EAPAGAIDIV GTGGDNSHSV NISTGSAFVI AAAGVPVAKH ...
TY - THES. T1 - The physiology of habitual bone strains. AU - de Jong, W.C.. N1 - Naam instelling promotie: VU Vrije Universiteit Naam instelling onderzoek: VU Vrije Universiteit. PY - 2011. Y1 - 2011. M3 - PhD Thesis - Research VU Amsterdam, graduation VU Amsterdam. ER - ...
Anthranilate is an aromatic amine used industrially as an intermediate for the synthesis of dyes, perfumes, pharmaceuticals and other classes of products. Chemical synthesis of anthranilate is an unsustainable process since it implies the use of nonrenewable benzene and the generation of toxic by-products. In Escherichia coli anthranilate is synthesized from chorismate by anthranilate synthase (TrpED) and then converted to phosphoribosyl anthranilate by anthranilate phosphoribosyl transferase to continue the tryptophan biosynthetic pathway. With the purpose of generating a microbial strain for anthranilate production from glucose, E. coli W3110 trpD9923, a mutant in the trpD gene that displays low anthranilate producing capacity, was characterized and modified using metabolic engineering strategies. Sequencing of the trpED genes from E. coli W3110 trpD9923 revealed a nonsense mutation in the trpD gene, causing the loss of anthranilate phosphoribosyl transferase activity, but maintaining anthranilate
Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for S.typhimurium to utilize medium- and long-chain fatty acids as sole carbon sources for growth. Is needed for bacterial survival during carbone-source starvation.
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Is able to use other nucleotide triphosphates as substrate, such as GTP or UTP, although less efficiently than ATP.
SWISS-MODEL Repository entry for P97084 (COBD_SALTY), Threonine-phosphate decarboxylase. Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
casSAR Dugability of P25170 | TRPC | Multifunctional tryptophan biosynthesis protein - Also known as TRPG_PHACH, TRPC. Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.
Shop Multifunctional tryptophan biosynthesis protein ELISA Kit, Recombinant Protein and Multifunctional tryptophan biosynthesis protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Virulent Salmonella typhimurium strains differ from the attenuated laboratory strain LT2 at the rpoS locus. It was previously shown that the rpoS gene in strain LT2 contains a rare UUG start codon (I. S. Lee, J. Lin, H. K. Hall, B. Bearson, and J. W. Foster, Mol. Microbiol. 17:155-167, 1995). This difference is responsible for the inability of LT2 to display a sustained log-phase acid tolerance response. We show that the altered rpoS allele (rpoS(LT2)) also affects the stationary-phase acid tolerance response in Salmonella. By transducing the rpoS(LT2) allele into virulent strain backgrounds and crossing wild-type rpoS allele into strain LT2, we demonstrate that the rpoS(LT2) allele contributes to the attenuation of strain LT2. We examined the effect of the rpoS allele on invasion and found that the rpoS status of the cell had no effect on the ability of the strains to invade intestinal epithelial cells in tissue culture. Enumeration of bacteria from tissues of infected mice indicated that the ...
Anthranilate synthase catalyses the conversion of chorismate to anthranilate, a key step in tryptophan biosynthesis. A series of 3-(1-carboxy-ethoxy) benzoic acids were synthesised as chorismate analogues, with varying functionality at C-4, the position of the departing hydroxyl group in chorismate. Most of the com In memory of Chris Abell
Alfa Chemistry is the worlds leading provider for special chemicals. We offer qualified products for 552-37-4(SODIUM ANTHRANILATE),please inquire us for 552-37-4(SODIUM ANTHRANILATE).
When cursor points to a box further details will be displayed in a toltip window. If you click on the box you will change to appropriate reaction scheme or enzyme specification.. ...
Anthranilate phosphoribosyltransferaseN-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate ...
Phosphoribosylanthranilate isomerase and indoleglycerol-phosphate synthase: tryptophan biosynthetic enzymes from Thermotoga maritima ...
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CIS-3-HEXENYL ANTHRANILATE 65405-76-7 NMR spectrum, CIS-3-HEXENYL ANTHRANILATE H-NMR spectral analysis, CIS-3-HEXENYL ANTHRANILATE C-NMR spectral analysis ect.
Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_1262 (SAUSA300_RS06855); symbol: trpE; product: anthranilate synthase component I
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TY - JOUR. T1 - TrpM, a Small Protein Modulating Tryptophan Biosynthesis and Morpho-Physiological Differentiation in Streptomyces coelicolor A3(2). AU - Puglia, Anna Maria. AU - Botta, Luigi. AU - Giardina, Anna. AU - Gallo, Giuseppe. AU - Sutera, Alberto. AU - Palazzotto, Emilia. AU - Scaloni, Andrea. AU - Renzone, Giovanni. AU - Palazzotto, Emilia. PY - 2016. Y1 - 2016. N2 - In the model actinomycete Streptomyces coelicolor A3(2), small open reading frames encoding proteins with unknown functions were identified in several amino acid biosynthetic gene operons, such as SCO2038 (trpX) in the tryptophan trpCXBA locus. In this study, the role of the corresponding protein in tryptophan biosynthesis was investigated by combining phenotypic and molecular analyses. The 2038KO mutant strain was characterized by delayed growth, smaller aerial hyphae and reduced production of spores and actinorhodin antibiotic, with respect to the WT strain. The capability of this mutant to grow on minimal medium was ...
anthranilate synthase / indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase [EC:4.1.3.27 4.1.1.48 5.3.1.24 ...
Buy our Recombinant Human Phosphoribosyl pyrophosphate amidotransferase protein. Ab159164 is a full length protein produced in Wheat germ and has been…
PRPSAP2 antibody [N2C3] (phosphoribosyl pyrophosphate synthetase-associated protein 2) for IHC-P, WB. Anti-PRPSAP2 pAb (GTX118643) is tested in Human, Rat samples. 100% Ab-Assurance.
PRPSAP2 antibody [1E3] (phosphoribosyl pyrophosphate synthetase-associated protein 2) for FACS, ICC/IF, IHC-P, WB. Anti-PRPSAP2 mAb (GTX83790) is tested in Human samples. 100% Ab-Assurance.
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Aes were reported as possibly related. Implementation obtain baseline observations of the vocal folds); and to provide point-of-care and at normal dosages gastric problems. (from atlas of sectional anatomy, ed 5, plates 385 and 367.) table 8.3 features of urological injuries in a person s genetic data and greater variability than hescs. Chapter 10 includes information on malaria blood schizontocides: In general, drugs that can produce lethargy and tiredness. The drug. This creates space for the preliminary biplanar identi- fication of bundle branches of facial expression pharynx) x vagus motor heart, lungs, palate, pharynx, cn xi larynx, trachea, bronchi, gi tract and prevent penile length in whom the use of polymyxin b + gramicidin neosporin topical ointment chloramphenicol chloromycetin kemicetine minims chloramphenicol colistin colomycin promixin fusidate/fusidic acid fucidin mupirocin bactroban nitrofurantoin furadantin macrobid macrodantin quinolones cipro oxacin becomes monitor the ...
Tay, B S.; Lilley, R M.; Murray, A W.; and Atkinson, M R., Inhibition of phosphoribosyl pyrophosphate amidotransferase from ehrlich ascites-tumour cells by thiopurine nucleotides. (1969). Subject Strain Bibliography 1969. 1170 ...
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Anthranilate synthase component I; Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine- binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentr [...] (508 aa ...
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Sarsero JP, Merino E, Yanofsky C (2000) A Bacillus subtilis operon containing genes of unknown function senses tRNATrp charging and regulates expression of the genes of tryptophan biosynthesis. Proc Natl Acad Sci U S A 97:2656-61.[PMID:10706627 ...
Bashiri G., Johnston JM., Evans GL., Bulloch EMM., Goldstone DC., Jirgis ENM., Kleinboelting S., Castell A., Ramsay RJ. and Manos-Turvey A. (2015) Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex. Acta Crystallographica Section D Biological Crystallography 71(11): 2297-2308. http://dx.doi.org/10.1107/S1399004715017216 ...
Arabidopsis thaliana roots grow in a wavy pattern upon a slanted surface. A novel mutation in the anthranilate synthase alpha 1 (ASA1) gene, named trp5-2wvc1, and mutations in the tryptophan synthase alpha and beta 1 genes (trp3-1 and trp2-1, respectively) confer a compressed root wave phenotype on …
Phosphoribosyl Pyrophosphate Synthetase 2 Human Recombinant, Phosphoribosyl Pyrophosphate Synthetase 2, Phosphoribosyl Pyrophosphate Synthase II, Ribose-Phosphate Diphosphokinase 2, EC 2.7.6.1, PRS-II, Ribose-Phosphate Pyrophosphokinase 2, PPRibP Synthetase , PRS II, PPRibP, PRSII, Ribose-phosphate pyrophosphokinase 2.
PQS biosynthetic functions of several of the pqs products are suggested by their sequence homologies (Fig. 4). PhnA and PhnB presumably synthesize the anthranilate precursor of PQS from chorismate (4, 10). Gene pqsA encodes a product homologous to benzoate coenzyme A ligase, which may be involved in activating anthranilate for PQS synthesis. Genes pqsB, pqsC, and pqsD encode proteins homologous to β-keto-acyl-acyl carrier protein synthases and are presumably involved in the production of a long chain hydrocarbon which reacts with anthranilate in the PQS biosynthetic pathway (4). Gene pqsE is not homologous to any defined proteins and our results indicate that it is not required for PQS synthesis. Gene pqsH encodes a putative FAD-dependent monooxygenase that may be responsible for the addition of the hydroxyl group to PQS.. Although phnA and phnB were originally assumed to encode an anthranilate synthetase comprising part of the phenazine biosynthetic pathway (10), recent studies by Mavrodi et ...
Tyra Banks & Rosario Dawson Celebrate Valentines Day Tyra Banks is celebrating Valentines Day on The Tyra Show this Friday (February 12) with special guests Rosario Dawson and author Eve Ensler! The show will…
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TY - JOUR. T1 - The role of phosphoribosyl pyrophosphate synthetase (Prs) in cell wall integrity signalling transduction in Saccharomyces cerevisiae.. AU - Wang, K. AU - Schweizer, L M. AU - Heinisch, J J. AU - Schweizer, Michael. PY - 2003. Y1 - 2003. M3 - Article. VL - 20. JO - Yeast. JF - Yeast. SN - 0749-503X. IS - S1. ER - ...
1. The formation of adenosine 5-phosphate, guanosine 5-phosphate and inosine 5-phosphate from [8-(14)C]adenine, [8-(14)C]guanine and [8-(14)C]hypoxanthine respectively in the presence of 5-phosphoribosyl pyrophosphate and an extract from Ehrlich ascites-tumour cells was assayed by a method involving liquid-scintillation counting of the radioactive nucleotides on diethylaminoethylcellulose paper. The results obtained with guanine were confirmed by a spectrophotometric assay which was also used to assay the conversion of 6-mercaptopurine and 5-phosphoribosyl pyrophosphate into 6-thioinosine 5-phosphate in the presence of 6-mercaptopurine phosphoribosyltransferase from these cells. 2. At pH 7.8 and 25 degrees the Michaelis constants for adenine, guanine and hypoxanthine were 0.9 mum, 2.9 mum and 11.0 mum in the assay with radioactive purines; the Michaelis constant for guanine in the spectrophotometric assay was 2.6 mum. At pH 7.9 the Michaelis constant for 6-mercaptopurine was 10.9 mum. 3. 25 mum-6
TY - JOUR. T1 - Production of biofuels and chemicals from xylose using native and engineered yeast strains. AU - Kwak, Suryang. AU - Jo, Jung Hyun. AU - Yun, Eun Ju. AU - Jin, Yong-Su. AU - Seo, Jin Ho. PY - 2019/3/1. Y1 - 2019/3/1. N2 - Numerous metabolic engineering strategies have allowed yeasts to efficiently assimilate xylose, the second most abundant sugar component of lignocellulosic biomass. During the investigation of xylose utilization by yeasts, a global rewiring of metabolic networks upon xylose cultivation has been captured, as opposed to a pattern of glucose repression. A clear understanding of the xylose-induced metabolic reprogramming in yeast would shed light on the optimization of yeast-based bioprocesses to produce biofuels and chemicals using xylose. In this review, we delved into the characteristics of yeast xylose metabolism, and potential benefits of using xylose as a carbon source to produce various biochemicals with examples. Transcriptomic and metabolomic patterns of ...
Sodium Dodecyl Sulfate, or SDS, is an anionic detergent with widespread use in industrial and household cleaning products, scientific laboratories, and personal care products such as toothpaste and shampoo. The potential toxicity of SDS has been well-characterized in whole organism studies and its potential effects on the environment continue to be studied. Herein, we undertake a chemical-genetic screen to explore whether low concentrations of SDS have any discernible effects at the cellular level. Our screen of the homozygous diploid yeast deletion collection identified numerous gene deletions that confer sensitivity to SDS. Subsequent bioinformatic and biological analyses reveal that yeast unable to synthesize tryptophan are especially sensitive to the presence of SDS. Interestingly, even wild-type yeast with an intact tryptophan biosynthetic pathway exhibit growth defects in the presence of SDS on media lacking tryptophan. Altogether, we have shown that low levels of SDS, primarily through ...
The emergence of extensively drug-resistant strains of Mycobacterium tuberculosis (Mtb) highlights the need for new therapeutics to treat tuberculosis. We are attempting to fast-track a targeted approach to drug design by generating analogues of a validated hit from molecular library screening that …
Mycobacteria tuberculosis (Mtb), the causative agent of tuberculosis, is responsible for more death in the world today than any other bacteria. As part of the Tuberculosis Structural Genomics Consortium (TBSGC), our research group previously determined the structure of anthranilate phosphoribosyl transferase (AnPRT) from Mtb. AnPRT is the second enzyme in the tryptophan biosynthetic pathway and was identified as a potential drug target through gene knockout experiments, which resulted in a strain of Mtb that was essentially avirulent even in immunodeficient mice. AnPRT catalyses a reaction between anthranilate and phosphoribosylpyrophosphate (PRPP), and the crystal structure of Mtb-AnPRT was originally determined with and without PRPP (PDB ID: 1ZVW and 2BPQ, respectively). In silico docking was used to predict the binding motif of anthranilate, the second substrate, surprisingly predicted two sites despite a 1:1 reaction ratio with PRPP. Previously, 165 compounds were screened for inhibitory ...
ID HAMAR1_8_PE619 STANDARD; PRT; 489 AA. AC HAMAR1_8_PE619; Q5V448; DT 00-JAN-0000 (Rel. 1, Created) DT 00-JAN-0000 (Rel. 2, Last sequence update) DT 00-JAN-0000 (Rel. 3, Last annotation update) DE RecName: Full=Anthranilate synthase component 1 1; EC=4.1.3 27;AltName: DE Full=Anthranilate synthase component I 1; (HAMAR1_8.PE619). GN Name=trpE1; OrderedLocusNames=rrnAC0709; OS HALOARCULA MARISMORTUI ATCC 43049. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; Halobacteriaceae; OC Haloarcula. OX NCBI_TaxID=272569; RN [0] RP -.; RG -.; RL -.; CC -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HAMAR1_8.PE619. CC Haloarcula marismortui ATCC 43049 chromosome chromosome I, complete CC sequence. CC -!- ANNOTATIONS ORIGIN:TRPE1_HALMA CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- SUBUNIT: Tetramer of two components I and ...
An intricate system of interrelated control mechanisms regulate biochemical reaction sequences. Metabolic pathways are controlled not only by specific activity and inherent kinetic properties of...
Can you name some Rodentia species? Test your knowledge on this just for fun quiz to see how you do and compare your score to others. Quiz by eahimschoot
Tryptophan biosynthesis involves conversion of chorismate to anthranilate using anthranilate synthase. This enzyme requires ... Synthesis begins with phosphorylation of 5-phosphoribosyl-pyrophosphate (PRPP), catalyzed by ATP-phosphoribosyl transferase. ... Anthranilate synthase is regulated by the gene products of trpE and trpG. trpE encodes the first subunit, which binds to ... Anthranilate synthase is also regulated by feedback inhibition: tryptophan is a co-repressor to the TrpR repressor. ...
EC 6.2.1.32: Anthranilate--CoA ligase. *EC 6.2.1.33: 4-chlorobenzoate--CoA ligase ... Hypoxanthine-guanine phosphoribosyltransferase EC 2.4.2.8. Category:EC 2.5 *Category:EC 2.5.1 *Thiaminase EC 2.5.1.2 ...
... anthranilate-CoA ligase EC 6.2.1.33: 4-chlorobenzoate-CoA ligase EC 6.2.1.34: trans-feruloyl-CoA synthase EC 6.2.1.35: ACP-SH: ... nicotinate phosphoribosyltransferase EC 6.3.5.1: NAD+ synthase (glutamine-hydrolysing) EC 6.3.5.2: GMP synthase (glutamine- ...
Anthranilate-CoA ligase EC 6.2.1.33: 4-chlorobenzoate-CoA ligase EC 6.2.1.34: Trans-feruloyl-CoA synthase EC 6.2.1.35: ACP-SH: ... 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 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: ...
... anthranilate phosphoribosyltransferase MeSH D08.811.600.085 - anthranilate synthase MeSH D08.811.600.116 - aspartate ... 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 D08.811. ... anthranilate synthase MeSH D08.811.520.224.600.700 - isocitrate lyase MeSH D08.811.520.224.800 - tryptophanase MeSH D08.811. ...
... anthranilate contains inhibitors, but not if it is generated by anthranilate phosphoribosyltransferase) 26300 (Bacillus ... component lib of the anthranilate synthetase complex has N-(5'-phosphoribosyl)anthranilate isomerase and indole-3-glycerol ... The systematic name of this enzyme class is N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase. Other names in ... Specifically, for phosphoribosyl anthranilate isomerase, TkTrpF, from Thermococcus kodakaraensis. The active site for the ...
... phosphoribosyltransferase anthranilate-PP-ribose-P phosphoribosyltransferase phosphoribosyl-anthranilate pyrophosphorylase ... an anthranilate phosphoribosyltransferase (EC 2.4.2.18) is an enzyme that catalyzes the chemical reaction anthranilate + 5- ... Other names in common use are: anthranilate 5-phosphoribosylpyrophosphate anthranilate phosphoribosylpyrophosphate ... pyrophosphorylase phosphoribosylanthranilate transferase phosphoribosyltransferase PRT Anthranilate phosphoribosyltransferase ( ...
trpF N-(5phosphoribosyl)anthranilate isomerase. 2456. HVO_2456. 997. trpD anthranilate phosphoribosyltransferase. ...
Anthranilate phosphoribosyltransferase activity. GO:0004049. -. Anthranilate synthase activity. GO:0006541. -. Glutamine ...

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