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PMID:27411165
Autor:Paritala H; Palde PB; Carroll KS
Endereço:Department of Chemistry, The Scripps Research Institute, 130 Scripps Way, 2B2, Jupiter, FL, 33458, USA.
Título:Functional Site Discovery in a Sulfur Metabolism Enzyme by Using Directed Evolution.
Fonte:Chembiochem; 17(19):1873-1878, 2016 10 04.
ISSN:1439-7633
País de publicação:Germany
Idioma:eng
Resumo:In human pathogens, the sulfate assimilation pathway provides reduced sulfur for biosynthesis of essential metabolites, including cysteine and low-molecular-weight thiol compounds. Sulfonucleotide reductases (SRs) catalyze the first committed step of sulfate reduction. In this reaction, activated sulfate in the form of adenosine-5'-phosphosulfate (APS) or 3'-phosphoadenosine 5'-phosphosulfate (PAPS) is reduced to sulfite. Gene knockout, transcriptomic and proteomic data have established the importance of SRs in oxidative stress-inducible antimicrobial resistance mechanisms. In previous work, we focused on rational and high-throughput design of small-molecule inhibitors that target the active site of SRs. However, another critical goal is to discover functionally important regions in SRs beyond the traditional active site. As an alternative to conservation analysis, we used directed evolution to rapidly identify functional sites in PAPS reductase (PAPR). Four new regions were discovered that are essential to PAPR function and lie outside the substrate binding pocket. Our results highlight the use of directed evolution as a tool to rapidly discover functionally important sites in proteins.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
Nome de substância:485-84-7 (Adenosine Phosphosulfate); 70FD1KFU70 (Sulfur); EC 1.- (Oxidoreductases)


  2 / 100 MEDLINE  
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PMID:27206694
Autor:Koprivova A; Kopriva S
Endereço:Botanical Institute, Cluster of Excellence on Plant Sciences (CEPLAS), University of Cologne, Zülpicher Str. 47b, 50674, Cologne, Germany. Electronic address: a.koprivova@uni-koeln.de.
Título:Sulfation pathways in plants.
Fonte:Chem Biol Interact; 259(Pt A):23-30, 2016 Nov 25.
ISSN:1872-7786
País de publicação:Ireland
Idioma:eng
Resumo:Plants take up sulfur in the form of sulfate. Sulfate is activated to adenosine 5'-phosphosulfate (APS) and reduced to sulfite and then to sulfide when it is assimilated into amino acid cysteine. Alternatively, APS is phosphorylated to 3'-phosphoadenosine 5'-phosphosulfate (PAPS), and sulfate from PAPS is transferred onto diverse metabolites in its oxidized form. Traditionally, these pathways are referred to as primary and secondary sulfate metabolism, respectively. However, the synthesis of PAPS is essential for plants and even its reduced provision leads to dwarfism. Here the current knowledge of enzymes involved in sulfation pathways of plants will be summarized, the similarities and differences between different kingdoms will be highlighted, and major open questions in the research of plant sulfation will be formulated.
Tipo de publicação: JOURNAL ARTICLE; REVIEW
Nome de substância:0 (Plant Proteins); 0 (Sulfates); 482-67-7 (Phosphoadenosine Phosphosulfate); 485-84-7 (Adenosine Phosphosulfate)


  3 / 100 MEDLINE  
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PMID:26860640
Autor:Wang D; Xu S; Song D; Knight S; Mao X
Endereço:1​ Department of Biochemistry, School of Medicine, Key Laboratory of Ministry of Education for Developmental Genes and Human Diseases, Southeast University, Nanjing, Jiangsu 210009, PR China.
Título:A gene encoding a potential adenosine 5'-phosphosulphate kinase is necessary for timely development of Myxococcus xanthus.
Fonte:Microbiology; 162(4):672-83, 2016 Apr.
ISSN:1465-2080
País de publicação:England
Idioma:eng
Resumo:A Myxococcus xanthus gene, MXAN3487, was identified by transposon mutagenesis to be required for the expression of mcuABC, an operon coding for part of the chaperone-usher (CU) system in this bacterium. The MXAN3487 protein displays sequence and structural homology to adenosine 5'-phosphosulphate (APS) kinase family members and contains putative motifs for ATP and APS binding. Although the MXAN3487 locus is not linked to other sulphate assimilation genes, its protein product may have APS kinase activity in vivo and the importance of the ATP-binding site for activity was demonstrated. Expression of MXAN3487 was not affected by sulphate availability, suggesting that MXAN3487 may not function in a reductive sulphate assimilation pathway. Deletion of MXAN3487 significantly delayed fruiting body formation and the production of McuA, a spore coat protein secreted by the M. xanthus Mcu CU system. Based on these observations and data from our previous studies, we propose that MXAN3487 may phosphorylate molecules structurally related to APS, generating metabolites necessary for M. xanthus development, and that MXAN3487 exerts a positive effect on the mcuABC operon whose expression is morphogenesis dependent.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (DNA Transposable Elements); 485-84-7 (Adenosine Phosphosulfate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.25 (adenylylsulfate kinase)


  4 / 100 MEDLINE  
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PMID:26294763
Autor:Herrmann J; Nathin D; Lee SG; Sun T; Jez JM
Endereço:From the Department of Biology, Washington University, St. Louis, Missouri 63130.
Título:Recapitulating the Structural Evolution of Redox Regulation in Adenosine 5'-Phosphosulfate Kinase from Cyanobacteria to Plants.
Fonte:J Biol Chem; 290(41):24705-14, 2015 Oct 09.
ISSN:1083-351X
País de publicação:United States
Idioma:eng
Resumo:In plants, adenosine 5'-phosphosulfate (APS) kinase (APSK) is required for reproductive viability and the production of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a sulfur donor in specialized metabolism. Previous studies of the APSK from Arabidopsis thaliana (AtAPSK) identified a regulatory disulfide bond formed between the N-terminal domain (NTD) and a cysteine on the core scaffold. This thiol switch is unique to mosses, gymnosperms, and angiosperms. To understand the structural evolution of redox control of APSK, we investigated the redox-insensitive APSK from the cyanobacterium Synechocystis sp. PCC 6803 (SynAPSK). Crystallographic analysis of SynAPSK in complex with either APS and a non-hydrolyzable ATP analog or APS and sulfate revealed the overall structure of the enzyme, which lacks the NTD found in homologs from mosses and plants. A series of engineered SynAPSK variants reconstructed the structural evolution of the plant APSK. Biochemical analyses of SynAPSK, SynAPSK H23C mutant, SynAPSK fused to the AtAPSK NTD, and the fusion protein with the H23C mutation showed that the addition of the NTD and cysteines recapitulated thiol-based regulation. These results reveal the molecular basis for structural changes leading to the evolution of redox control of APSK in the green lineage from cyanobacteria to plants.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
Nome de substância:25612-73-1 (Adenylyl Imidodiphosphate); 485-84-7 (Adenosine Phosphosulfate); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.25 (adenylylsulfate kinase); I38ZP9992A (Magnesium)


  5 / 100 MEDLINE  
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PMID:25826698
Autor:Wojdyla-Mamon AM; Zimny J; Romanowska J; Kraszewski A; Stawinski J; Bieganowski P; Guranowski A
Endereço:*Department of Biochemistry and Biotechnology, Poznan University of Life Science, 11 Dojazd St., 60-632 Poznan, Poland.
Título:Novel reactivity of Fhit proteins: catalysts for fluorolysis of nucleoside 5'-phosphoramidates and nucleoside 5'-phosphosulfates to generate nucleoside 5'-phosphorofluoridates.
Fonte:Biochem J; 468(2):337-44, 2015 Jun 01.
ISSN:1470-8728
País de publicação:England
Idioma:eng
Resumo:Fragile histidine triad (HIT) proteins (Fhits) occur in all eukaryotes but their function is largely unknown. Human Fhit is presumed to function as a tumour suppressor. Previously, we demonstrated that Fhits catalyse hydrolysis of not only dinucleoside triphosphates but also natural adenosine 5'-phosphoramidate (NH2-pA) and adenosine 5'-phosphosulfate (SO4-pA) as well as synthetic adenosine 5'-phosphorofluoridate (F-pA). In the present study, we describe an Fhit-catalysed displacement of the amino group of nucleoside 5'-phosphoramidates (NH2-pNs) or the sulfate moiety of nucleoside 5'-phosphosulfates (SO4-pNs) by fluoride anion. This results in transient accumulation of the corresponding nucleoside 5'-phosphorofluoridates (F-pNs). Substrate specificity and kinetic characterization of the fluorolytic reactions catalysed by the human Fhit and other examples of involvement of fluoride in the biochemistry of nucleotides are described. Among other HIT proteins, human histidine triad nucleotide-binding protein (Hint1) catalysed fluorolysis of NH2-pA 20 times and human Hint2 40 times more slowly than human Fhit.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Neoplasm Proteins); 0 (Phosphates); 0 (fragile histidine triad protein); 15181-43-8 (fluorophosphate); 415SHH325A (Adenosine Monophosphate); 485-84-7 (Adenosine Phosphosulfate); 6154-31-0 (adenosine 5'-phosphoramidate); EC 3.6.- (Acid Anhydride Hydrolases); Q80VPU408O (Fluorides)


  6 / 100 MEDLINE  
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PMID:25807013
Autor:Poyraz Ö; Brunner K; Lohkamp B; Axelsson H; Hammarström LG; Schnell R; Schneider G
Endereço:Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Título:Crystal structures of the kinase domain of the sulfate-activating complex in Mycobacterium tuberculosis.
Fonte:PLoS One; 10(3):e0121494, 2015.
ISSN:1932-6203
País de publicação:United States
Idioma:eng
Resumo:In Mycobacterium tuberculosis the sulfate activating complex provides a key branching point in sulfate assimilation. The complex consists of two polypeptide chains, CysD and CysN. CysD is an ATP sulfurylase that, with the energy provided by the GTPase activity of CysN, forms adenosine-5'-phosphosulfate (APS) which can then enter the reductive branch of sulfate assimilation leading to the biosynthesis of cysteine. The CysN polypeptide chain also contains an APS kinase domain (CysC) that phosphorylates APS leading to 3'-phosphoadenosine-5'-phosphosulfate, the sulfate donor in the synthesis of sulfolipids. We have determined the crystal structures of CysC from M. tuberculosis as a binary complex with ADP, and as ternary complexes with ADP and APS and the ATP mimic AMP-PNP and APS, respectively, to resolutions of 1.5 Å, 2.1 Å and 1.7 Å, respectively. CysC shows the typical APS kinase fold, and the structures provide comprehensive views of the catalytic machinery, conserved in this enzyme family. Comparison to the structure of the human homolog show highly conserved APS and ATP binding sites, questioning the feasibility of the design of specific inhibitors of mycobacterial CysC. Residue Cys556 is part of the flexible lid region that closes off the active site upon substrate binding. Mutational analysis revealed this residue as one of the determinants controlling lid closure and hence binding of the nucleotide substrate.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Nucleotides); 0 (Peptides); 0 (Sulfates); 482-67-7 (Phosphoadenosine Phosphosulfate); 485-84-7 (Adenosine Phosphosulfate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.25 (adenylylsulfate kinase); EC 2.7.7.4 (Sulfate Adenylyltransferase)


  7 / 100 MEDLINE  
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PMID:24584934
Autor:Herrmann J; Ravilious GE; McKinney SE; Westfall CS; Lee SG; Baraniecka P; Giovannetti M; Kopriva S; Krishnan HB; Jez JM
Endereço:From the Department of Biology, Washington University, St. Louis, Missouri 63130.
Título:Structure and mechanism of soybean ATP sulfurylase and the committed step in plant sulfur assimilation.
Fonte:J Biol Chem; 289(15):10919-29, 2014 Apr 11.
ISSN:1083-351X
País de publicação:United States
Idioma:eng
Resumo:Enzymes of the sulfur assimilation pathway are potential targets for improving nutrient content and environmental stress responses in plants. The committed step in this pathway is catalyzed by ATP sulfurylase, which synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP. To better understand the molecular basis of this energetically unfavorable reaction, the x-ray crystal structure of ATP sulfurylase isoform 1 from soybean (Glycine max ATP sulfurylase) in complex with APS was determined. This structure revealed several highly conserved substrate-binding motifs in the active site and a distinct dimerization interface compared with other ATP sulfurylases but was similar to mammalian 3'-phosphoadenosine 5'-phosphosulfate synthetase. Steady-state kinetic analysis of 20 G. max ATP sulfurylase point mutants suggests a reaction mechanism in which nucleophilic attack by sulfate on the α-phosphate of ATP involves transition state stabilization by Arg-248, Asn-249, His-255, and Arg-349. The structure and kinetic analysis suggest that ATP sulfurylase overcomes the energetic barrier of APS synthesis by distorting nucleotide structure and identifies critical residues for catalysis. Mutations that alter sulfate assimilation in Arabidopsis were mapped to the structure, which provides a molecular basis for understanding their effects on the sulfur assimilation pathway.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
Nome de substância:485-84-7 (Adenosine Phosphosulfate); 70FD1KFU70 (Sulfur); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.7.4 (Sulfate Adenylyltransferase)


  8 / 100 MEDLINE  
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PMID:24296033
Autor:Todisco S; Di Noia MA; Castegna A; Lasorsa FM; Paradies E; Palmieri F
Endereço:Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, via Orabona 4, 70125 Bari, Italy; Center of Excellence in Comparative Genomics, University of Bari, Italy.
Título:The Saccharomyces cerevisiae gene YPR011c encodes a mitochondrial transporter of adenosine 5'-phosphosulfate and 3'-phospho-adenosine 5'-phosphosulfate.
Fonte:Biochim Biophys Acta; 1837(2):326-34, 2014 Feb.
ISSN:0006-3002
País de publicação:Netherlands
Idioma:eng
Resumo:The genome of Saccharomyces cerevisiae contains 35 members of the mitochondrial carrier family, nearly all of which have been functionally characterized. In this study, the identification of the mitochondrial carrier for adenosine 5'-phosphosulfate (APS) is described. The corresponding gene (YPR011c) was overexpressed in bacteria. The purified protein was reconstituted into phospholipid vesicles and its transport properties and kinetic parameters were characterized. It transported APS, 3'-phospho-adenosine 5'-phosphosulfate, sulfate and phosphate almost exclusively by a counter-exchange mechanism. Transport was saturable and inhibited by bongkrekic acid and other inhibitors. To investigate the physiological significance of this carrier in S. cerevisiae, mutants were subjected to thermal shock at 45°C in the presence of sulfate and in the absence of methionine. At 45°C cells lacking YPR011c, engineered cells (in which APS is produced only in mitochondria) and more so the latter cells, in which the exit of mitochondrial APS is prevented by the absence of YPR011cp, were less thermotolerant. Moreover, at the same temperature all these cells contained less methionine and total glutathione than wild-type cells. Our results show that S. cerevisiae mitochondria are equipped with a transporter for APS and that YPR011cp-mediated mitochondrial transport of APS occurs in S. cerevisiae under thermal stress conditions.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Mutant Proteins); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (YPR011c protein, s cerevisiae); 482-67-7 (Phosphoadenosine Phosphosulfate); 485-84-7 (Adenosine Phosphosulfate); AE28F7PNPL (Methionine); GAN16C9B8O (Glutathione); SAA04E81UX (Coenzyme A)


  9 / 100 MEDLINE  
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PMID:24100135
Autor:Stevenson CE; Hughes RK; McManus MT; Lawson DM; Kopriva S
Endereço:Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.
Título:The X-ray crystal structure of APR-B, an atypical adenosine 5'-phosphosulfate reductase from Physcomitrella patens.
Fonte:FEBS Lett; 587(22):3626-32, 2013 Nov 15.
ISSN:1873-3468
País de publicação:England
Idioma:eng
Resumo:Sulfonucleotide reductases catalyse the first reductive step of sulfate assimilation. Their substrate specificities generally correlate with the requirement for a [Fe4S4] cluster, where adenosine 5'-phosphosulfate (APS) reductases possess a cluster and 3'-phosphoadenosine 5'-phosphosulfate reductases do not. The exception is the APR-B isoform of APS reductase from the moss Physcomitrella patens, which lacks a cluster. The crystal structure of APR-B, the first for a plant sulfonucleotide reductase, is consistent with a preference for APS. Structural conservation with bacterial APS reductase rules out a structural role for the cluster, but supports the contention that it enhances the activity of conventional APS reductases.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Plant Proteins); 485-84-7 (Adenosine Phosphosulfate); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.99.2 (adenylylsulfate reductase)


  10 / 100 MEDLINE  
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PMID:24073218
Autor:Parey K; Demmer U; Warkentin E; Wynen A; Ermler U; Dahl C
Endereço:Max-Planck-Institut für Biophysik, Frankfurt, Germany ; Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Regensburg, Germany.
Título:Structural, biochemical and genetic characterization of dissimilatory ATP sulfurylase from Allochromatium vinosum.
Fonte:PLoS One; 8(9):e74707, 2013.
ISSN:1932-6203
País de publicação:United States
Idioma:eng
Resumo:ATP sulfurylase (ATPS) catalyzes a key reaction in the global sulfur cycle by reversibly converting inorganic sulfate (SO4 (2-)) with ATP to adenosine 5'-phosphosulfate (APS) and pyrophosphate (PPi). In this work we report on the sat encoded dissimilatory ATP sulfurylase from the sulfur-oxidizing purple sulfur bacterium Allochromatium vinosum. In this organism, the sat gene is located in one operon and co-transcribed with the aprMBA genes for membrane-bound APS reductase. Like APS reductase, Sat is dispensible for growth on reduced sulfur compounds due to the presence of an alternate, so far unidentified sulfite-oxidizing pathway in A. vinosum. Sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase. We produced the purple bacterial sat-encoded ATP sulfurylase as a recombinant protein in E. coli, determined crucial kinetic parameters and obtained a crystal structure in an open state with a ligand-free active site. By comparison with several known structures of the ATPS-APS complex in the closed state a scenario about substrate-induced conformational changes was worked out. Despite different kinetic properties ATPS involved in sulfur-oxidizing and sulfate-reducing processes are not distinguishable on a structural level presumably due to the interference between functional and evolutionary processes.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Bacterial Proteins); 0 (Diphosphates); 0 (Recombinant Proteins); 0 (Sulfates); 485-84-7 (Adenosine Phosphosulfate); 4E862E7GRQ (diphosphoric acid); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.7.4 (Sulfate Adenylyltransferase)



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