Anthranilate Phosphoribosyltransferase: 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.Pyrimidine Phosphorylases: Pentosyltransferases that catalyze the reaction between a pyrimidine nucleoside and orthophosphate to form a free pyrimidine and ribose-5-phosphate.Anthranilate Synthase: 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.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.ortho-Aminobenzoates: Benzoic acids, salts, or esters that contain an amino group attached to carbon number 2 or 6 of the benzene ring structure.Orotate Phosphoribosyltransferase: 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.Nicotinamide Phosphoribosyltransferase: 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).Lesch-Nyhan Syndrome: 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

... 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 ( ...

*List of MeSH codes (D08)

... 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 ... anthranilate synthase MeSH D08.811.520.224.600.700 --- isocitrate lyase MeSH D08.811.520.224.800 --- tryptophanase MeSH D08.811 ...

*List of EC numbers (EC 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: ...

*List of EC numbers (EC 6)

... 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- ...
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)
E. coli trpE polar mutations are 10 times more polar on trpD gene expression than on downstream (trpC, B, or A) gene expression. This effect was shown to be the result of "translational coupling," in which efficient translation of trpD mRNA reqiures efficient translation of the end of trpE mRNA. The trpE-trpD intercistronic punctuation region consists of overlapping stop and start codons, and the trpE and trpD gene products form a functional complex in the cell. In light of these observations and characteristics, several models for the mechanism of translational coupling are considered.. ...
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 transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.
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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 ...
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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 ...
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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.
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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 ...
anthranilate synthase / indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase [EC:4.1.3.27 4.1.1.48 5.3.1.24 ...
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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 ...
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 ...
PRPS1 antibody (phosphoribosyl pyrophosphate synthetase 1) for ICC/IF, IHC-P, WB. Anti-PRPS1 pAb (GTX102570) is tested in Human samples. 100% Ab-Assurance.
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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 ...
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 ...
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...
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Purine phosphoribosyltransferases, purine PRTs, are essential enzymes in the purine salvage pathway of living organisms. They are involved in the formation of C-N glycosidic bonds in purine nucleosides-50-monophosphate (NMPs) through the transfer of the 5-phosphoribosyl group from 5-phospho-a-D-ribosyl-1-pyrophosphate (PRPP) to purine nucleobases in the presence of Mg2þ. Herein, we report a simple and thermostable process for the one-pot, one-step synthesis of some purine NMPs using xanthine phosphoribosyltransferase, XPRT or adenine phosphoribosyltransferase, APRT2, from Thermus thermophilus HB8. In this sense, the cloning, expression and purification of TtXPRT and TtAPRT2 is described for the first time. Both genes, xprt and aprt2 were expressed as his-tagged enzymes in E. coli BL21(DE3) and purified by a heat-shock treatment, followed by Ni-affinity chromatography and a final, polishing gel-filtration chromatography. Biochemical characterization revealed TtXPRT as a tetramer and TtAPRT2 as a ...
ETHYL ANTHRANILATE 87-25-2 NMR spectrum, ETHYL ANTHRANILATE H-NMR spectral analysis, ETHYL ANTHRANILATE C-NMR spectral analysis ect.
A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins ...

Structure Cluster 









- 2BPQ: Anthranilate phosphoribosyltransferase (TrpD) from Mycobacterium tuberculosis (Apo...Structure Cluster - 2BPQ: Anthranilate phosphoribosyltransferase (TrpD) from Mycobacterium tuberculosis (Apo...

Description: ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE protein , Length: 373 No structure alignment results are available for 2BPQ ...
more infohttp://www.rcsb.org/pdb/explore/structureCluster.do?structureId=2BPQ

SWISS-MODEL Repository | A1U6H0SWISS-MODEL Repository | A1U6H0

Anthranilate phosphoribosyltransferase. Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8) ... Anthranilate phosphoribosyltransferase UniProtKBInterProSTRINGInteractive Modelling. 342 aa; Sequence (Fasta) Identical ...
more infohttps://swissmodel.expasy.org/repository/uniprot/A1U6H0

Metabolic engineering for improving anthranilate synthesis from glucose in Escherichia coli | Microbial Cell Factories | Full...Metabolic engineering for improving anthranilate synthesis from glucose in Escherichia coli | Microbial Cell Factories | Full...

In Escherichia coli anthranilate is synthesized from chorismate by anthranilate synthase (TrpED) and then converted to ... but maintaining anthranilate synthase activity, thus causing anthranilate accumulation. The effects of expressing genes ... Chemical synthesis of anthranilate is an unsustainable process since it implies the use of nonrenewable benzene and the ... With the purpose of generating a microbial strain for anthranilate production from glucose, E. coli W3110 trpD9923, a mutant in ...
more infohttps://microbialcellfactories.biomedcentral.com/articles/10.1186/1475-2859-8-19

anthranilate phosphoribosyltransferase [Psychromonas ingrahamii 37] - Protein - NCBIanthranilate phosphoribosyltransferase [Psychromonas ingrahamii 37] - Protein - NCBI

anthranilate phosphoribosyltransferase [Psychromonas ingrahamii 37]. * Record removed. The sequence YP_942496 is 100% identical ...
more infohttps://www.ncbi.nlm.nih.gov/protein/119944816

Anthranilate phosphoribosyltransferase - WikipediaAnthranilate phosphoribosyltransferase - Wikipedia

... 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 ( ...
more infohttps://en.wikipedia.org/wiki/Anthranilate_phosphoribosyltransferase

Remediated Sequence 









- 2BPQ: Anthranilate phosphoribosyltransferase (TrpD) from Mycobacterium tuberculosis (Apo...Remediated Sequence - 2BPQ: Anthranilate phosphoribosyltransferase (TrpD) from Mycobacterium tuberculosis (Apo...

Chain A: ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE. Chain Downloadable Files. Download FASTA File. View Sequence & DSSP Image. ...
more infohttp://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2BPQ

Anthranilate phosphoribosyl transferase (TrpD) generates phosphoribosylamine for thiamine synthesis from enamines and...Anthranilate phosphoribosyl transferase (TrpD) generates phosphoribosylamine for thiamine synthesis from enamines and...

Anthranilate phosphoribosyl transferase (TrpD) has been well characterized for its role in the tryptophan biosynthetic pathway ... Anthranilate phosphoribosyl transferase (TrpD) generates phosphoribosylamine for thiamine synthesis from enamines and ... Anthranilate phosphoribosyl transferase (TrpD) generates phosphoribosylamine for thiamine synthesis from enamines and ... Anthranilate phosphoribosyl transferase (TrpD) generates phosphoribosylamine for thiamine synthesis from enamines and ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/23101964

Anthranilate Phosphoribosyltransferase - Biochemical KineticsAnthranilate Phosphoribosyltransferase - Biochemical Kinetics

Anthranilate Phosphoribosyltransferase. Tue, 29 May 2012 , Biochemical Kinetics This enzyme [EC 2.4.2.18], also referred to as ... phospho-ribosyl-anthranilate pyrophosphorylase, catalyzes the reaction of anthranilate with phosphoribosylpyrophos-phate to ... anthranilate synthase, tryptophan synthase, and phos-phoribosylanthranilate isomerase). ...
more infohttps://www.pharmacologicalsciences.us/biochemical-kinetics/anthranilate-phosphoribosyltransferase.html

trpF - N-(5-phosphoribosyl)anthranilate isomerase - Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) - trpF gene...trpF - N-(5'-phosphoribosyl)anthranilate isomerase - Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) - trpF gene...

Anthranilate phosphoribosyltransferase (trpD). *N-(5-phosphoribosyl)anthranilate isomerase (trpF). *Indole-3-glycerol ... N-(5-phosphoribosyl)anthranilate isomeraseUniRule annotation. Manual assertion according to rulesi ... N-(5-phospho-β-D-ribosyl)anthranilate*Search proteins in UniProtKB for this molecule. ... N-(5-phospho-β-D-ribosyl)anthranilate*Search proteins in UniProtKB for this molecule. ...
more infohttps://www.uniprot.org/uniprot/Q5N322

trpGD - Bifunctional protein TrpGD - Escherichia coli (strain K12) - trpGD gene & proteintrpGD - Bifunctional protein TrpGD - Escherichia coli (strain K12) - trpGD gene & protein

... to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high ... In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl ... In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine ... Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the ...
more infohttp://www.uniprot.org/uniprot/P00904

EC 2.4.2EC 2.4.2

... anthranilate phosphoribosyltransferase Reaction: N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho- ... EC 2.4.2.17 ATP phosphoribosyltransferase EC 2.4.2.18 anthranilate phosphoribosyltransferase EC 2.4.2.19 nicotinate-nucleotide ... anthranilate-PP-ribose-P phosphoribosyltransferase Systematic name: N-(5-phospho-D-ribosyl)-anthranilate:diphosphate phospho-α- ... EC 2.4.2.11 nicotinate phosphoribosyltransferase EC 2.4.2.12 nicotinamide phosphoribosyltransferase EC 2.4.2.13 now EC 2.5.1.6 ...
more infohttps://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC2/0402.html

EC 2.4.2EC 2.4.2

... 17 ATP phosphoribosyltransferase EC 2.4.2.18 anthranilate phosphoribosyltransferase EC 2.4.2.19 nicotinate-nucleotide ... EC 2.4.2.9 uracil phosphoribosyltransferase EC 2.4.2.10 orotate phosphoribosyltransferase EC 2.4.2.11 transferred now EC 6.3. ... EC 2.4.2.7 adenine phosphoribosyltransferase EC 2.4.2.8 hypoxanthine phosphoribosyltransferase ... EC 2.4.2.22 xanthine phosphoribosyltransferase EC 2.4.2.23 transferred now covered by EC 2.4.2.2, EC 2.4.2.3 and EC 2.4.2.4. EC ...
more infohttps://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC2/4/2/

Publications - BiozentrumPublications - Biozentrum

Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus ...
more infohttps://www.biozentrum.unibas.ch/nc/de/forschung/publications/publications/?tx_x4epublication_pi1%5Byearfrom%5D=2006&tx_x4epublication_pi1%5Byearto%5D=2006

KEGG SSDB Best Search Result: abe:ARB 01830KEGG SSDB Best Search Result: abe:ARB 01830

mpd:MCP_2910 anthranilate phosphoribosyltransferase K00766 340 102 ( -) 29 0.317 82 -, 1 nph:NP_3476A metal-dependent hydrolase ...
more infohttp://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=abe:ARB_01830

KEGG SSDB Best Search Result: rno:100364027KEGG SSDB Best Search Result: rno:100364027

vsc:VSVS12_01414 Anthranilate phosphoribosyltransferase K00766 332 102 ( -) 29 0.302 159 ,-, 1 xbv:XBW1_3507 Potassium- ...
more infohttp://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=rno:100364027

Phosphate starvation of maize inhibits lateral root formation and alters gene expression in the lateral root primordium zone |...Phosphate starvation of maize inhibits lateral root formation and alters gene expression in the lateral root primordium zone |...

... anthranilate synthase/indole-3-glycerol phosphate synthase; trpD: anthranilate phosphoribosyltransferase; TRP1: anthranilate ... Moreover, anthranilate synthase/indole-3-glycerol phosphate synthase (TRP), which encodes a product that catalyzes the ... The tryptophan synthase alpha chain (trpA, TM00027996) was upregulated 1.94-fold and the anthranilate synthase alpha 2 subunit ... With respect to the synthesis of tryptophan, anthranilate synthase/indole-3-glycerol phosphate synthase (TRP), a key enzyme ...
more infohttps://bmcplantbiol.biomedcentral.com/articles/10.1186/1471-2229-12-89

Code System ConceptCode System Concept

Anthranilate phosphoribosyltransferase (substance). Code System Preferred Concept Name. Anthranilate phosphoribosyltransferase ... Anthranilate phosphoribosyltransferase Current Synonym true false 69015019 Phosphoribosyl-anthranilate pyrophosphorylase ...
more infohttps://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=41372005

Publications RSS feed from the libraryPublications RSS feed from the library

Anthranilate phosphoribosyltransferase from the hyperthermophilic archaeon Thermococcus kodakarensis shows maximum activity ... Structural insights into the forward and reverse enzymatic reactions in human adenine phosphoribosyltransferase Huyet J., Ozeir ... Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis ...
more infohttp://www.esrf.eu/home/UsersAndScience/Experiments/MX/About_our_beamlines/id30a-1--massif-1/publicationsRSS.html

Publication archives - btkPublication archives - btk

Anthranilate phosphoribosyltransferase from the hyperthermophilic archaeon Thermococcus kodakarensis shows maximum activity ...
more infohttps://www.btk.fi/btk/publication-archives/

sll0063 protein (Synechocystis sp. PCC6803) - STRING interaction networksll0063 protein (Synechocystis sp. PCC6803) - STRING interaction network

Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1- ... Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1- ... pyrophosphate (PRPP) to anthranilate to yield N-(5-phosphoribosyl)-anthranilate (PRA) (348 aa) ...
more infohttps://string-db.org/network/1148.SYNGTS_2320
  • The effects of expressing genes encoding a feedback inhibition resistant version of the enzyme 3-deoxy-D- arabino -heptulosonate-7-phosphate synthase ( aroG fbr ), transketolase ( tktA ), glucokinase ( glk ) and galactose permease ( galP ), as well as phosphoenolpyruvate:sugar phosphotransferase system (PTS) inactivation on anthranilate production capacity, were evaluated. (biomedcentral.com)
  • The anthranilate synthase activity is the result of aminase and amidotransferase activities that are encoded by trpE and the amino terminal region encoded by trpGD , respectively (Fig. 2a ). (biomedcentral.com)
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