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[PMID]:28467378
[Au] Autor:Ali L; Goraya MU; Arafat Y; Ajmal M; Chen JL; Yu D
[Ad] Endereço:College of Animal Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China. liaqatpaksw@yahoo.com.
[Ti] Título:Molecular Mechanism of Quorum-Sensing in Enterococcus faecalis: Its Role in Virulence and Therapeutic Approaches.
[So] Source:Int J Mol Sci;18(5), 2017 May 03.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Quorum-sensing systems control major virulence determinants in , which causes nosocomial infections. The . quorum-sensing systems include several virulence factors that are regulated by the operon, which encodes the cytolysin toxin. In addition, the . Fsr regulator system controls the expression of gelatinase, serine protease, and enterocin O16. The cytolysin and Fsr virulence factor systems are linked to enterococcal diseases that affect the health of humans and other host models. Therefore, there is substantial interest in understanding and targeting these regulatory pathways to develop novel therapies for enterococcal infection control. Quorum-sensing inhibitors could be potential therapeutic agents for attenuating the pathogenic effects of . . Here, we discuss the regulation of cytolysin, the LuxS system, and the Fsr system, their role in . -mediated infections, and possible therapeutic approaches to prevent . infection.
[Mh] Termos MeSH primário: Infecção Hospitalar/microbiologia
Enterococcus faecalis/patogenicidade
Infecções por Bactérias Gram-Positivas/microbiologia
Percepção de Quorum/fisiologia
[Mh] Termos MeSH secundário: Antibacterianos/farmacologia
Antibacterianos/uso terapêutico
Proteínas de Bactérias/genética
Biofilmes/efeitos dos fármacos
Biofilmes/crescimento & desenvolvimento
Liases de Carbono-Enxofre/genética
Infecção Hospitalar/tratamento farmacológico
Enterococcus faecalis/efeitos dos fármacos
Enterococcus faecalis/genética
Regulação Bacteriana da Expressão Gênica/fisiologia
Infecções por Bactérias Gram-Positivas/tratamento farmacológico
Seres Humanos
Perforina/genética
Percepção de Quorum/efeitos dos fármacos
Virulência
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Virulence Factors); 126465-35-8 (Perforin); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.21 (LuxS protein, Bacteria)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


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[PMID]:29045454
[Au] Autor:Peña-Soler E; Aranda J; López-Estepa M; Gómez S; Garces F; Coll M; Fernández FJ; Tuñon I; Vega MC
[Ad] Endereço:Chemical and Physical Biology Department, Center for Biological Research (CIB-CSIC), Madrid, Spain.
[Ti] Título:Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE.
[So] Source:PLoS One;12(10):e0186286, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sulfur trafficking in living organisms relies on transpersulfuration reactions consisting in the enzyme-catalyzed transfer of S atoms via activated persulfidic S across protein-protein interfaces. The recent elucidation of the mechanistic basis for transpersulfuration in the CsdA-CsdE model system has paved the way for a better understanding of its role under oxidative stress. Herein we present the crystal structure of the oxidized, inactivated CsdE dimer at 2.4 Å resolution. The structure sheds light into the activation of the Cys61 nucleophile on its way from a solvent-secluded position in free CsdE to a fully extended conformation in the persulfurated CsdA-CsdE complex. Molecular dynamics simulations of available CsdE structures allow to delineate the sequence of conformational changes underwent by CsdE and to pinpoint the key role played by the deprotonation of the Cys61 thiol. The low-energy subunit orientation in the disulfide-bridged CsdE dimer demonstrates the likely physiologic relevance of this oxidative dead-end form of CsdE, suggesting that CsdE could act as a redox sensor in vivo.
[Mh] Termos MeSH primário: Liases de Carbono-Enxofre/química
RNA Helicases DEAD-box/química
Proteínas de Escherichia coli/química
Conformação Proteica
Enxofre/química
[Mh] Termos MeSH secundário: Liases de Carbono-Enxofre/genética
Cristalografia por Raios X
RNA Helicases DEAD-box/genética
Escherichia coli/química
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Simulação de Dinâmica Molecular
Estresse Oxidativo/genética
Domínios e Motivos de Interação entre Proteínas/genética
Multimerização Proteica
Enxofre/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 70FD1KFU70 (Sulfur); EC 3.6.1.- (deaD protein, E coli); EC 3.6.4.13 (DEAD-box RNA Helicases); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (cysteine desulfurase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171019
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186286


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[PMID]:28991254
[Au] Autor:Teh BT; Lim K; Yong CH; Ng CCY; Rao SR; Rajasegaran V; Lim WK; Ong CK; Chan K; Cheng VKY; Soh PS; Swarup S; Rozen SG; Nagarajan N; Tan P
[Ad] Endereço:Thorn Biosystems Pte Ltd, Singapore.
[Ti] Título:The draft genome of tropical fruit durian (Durio zibethinus).
[So] Source:Nat Genet;49(11):1633-1641, 2017 Nov.
[Is] ISSN:1546-1718
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Durian (Durio zibethinus) is a Southeast Asian tropical plant known for its hefty, spine-covered fruit and sulfury and onion-like odor. Here we present a draft genome assembly of D. zibethinus, representing the third plant genus in the Malvales order and first in the Helicteroideae subfamily to be sequenced. Single-molecule sequencing and chromosome contact maps enabled assembly of the highly heterozygous durian genome at chromosome-scale resolution. Transcriptomic analysis showed upregulation of sulfur-, ethylene-, and lipid-related pathways in durian fruits. We observed paleopolyploidization events shared by durian and cotton and durian-specific gene expansions in MGL (methionine γ-lyase), associated with production of volatile sulfur compounds (VSCs). MGL and the ethylene-related gene ACS (aminocyclopropane-1-carboxylic acid synthase) were upregulated in fruits concomitantly with their downstream metabolites (VSCs and ethylene), suggesting a potential association between ethylene biosynthesis and methionine regeneration via the Yang cycle. The durian genome provides a resource for tropical fruit biology and agronomy.
[Mh] Termos MeSH primário: Bombacaceae/genética
Liases de Carbono-Enxofre/genética
Frutas/genética
Genoma de Planta
Proteínas de Plantas/genética
Transcriptoma
[Mh] Termos MeSH secundário: Aminoácidos Cíclicos/biossíntese
Bombacaceae/classificação
Bombacaceae/crescimento & desenvolvimento
Bombacaceae/metabolismo
Liases de Carbono-Enxofre/metabolismo
Mapeamento Cromossômico
Frutas/crescimento & desenvolvimento
Frutas/metabolismo
Sequenciamento de Nucleotídeos em Larga Escala
Ligases/genética
Ligases/metabolismo
Metabolismo dos Lipídeos/genética
Filogenia
Proteínas de Plantas/metabolismo
Enxofre/metabolismo
Compostos Orgânicos Voláteis/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Cyclic); 0 (Plant Proteins); 0 (Volatile Organic Compounds); 3K9EJ633GL (1-aminocyclopropane-1-carboxylic acid); 70FD1KFU70 (Sulfur); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.11 (L-methionine gamma-lyase); EC 6.- (Ligases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171010
[St] Status:MEDLINE
[do] DOI:10.1038/ng.3972


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[PMID]:28870899
[Au] Autor:Igarashi K; Kawaguchi K; Kiyuna T; Miyake K; Murakami T; Yamamoto N; Hayashi K; Kimura H; Miwa S; Tsuchiya H; Hoffman RM
[Ad] Endereço:AntiCancer, Inc., San Diego, CA, U.S.A.
[Ti] Título:Effective Metabolic Targeting of Human Osteosarcoma Cells and in Orthotopic Nude-mouse Models with Recombinant Methioninase.
[So] Source:Anticancer Res;37(9):4807-4812, 2017 09.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Methionine dependence may be the only known general metabolic defect in cancer. In order to exploit methionine dependence for therapy, our laboratory previously cloned L-methionine α-deamino-γ-mercaptomethane lyase [EC 4.4.1.11]) (recombinant methioninase [rMETase]), which was subsequently tested in mouse models of various types of human tumors. The present study aimed to investigate the efficacy of rMETase on human osteosarcoma cells in vitro and in vivo. MATERIALS AND METHODS: Human osteosarcoma cell lines 143B, HOS and SOSN2 were tested in vitro for survival during a 72-h exposure to rMETase using the WST-8 assay. Half-maximal inhibitory concentrations were calculated for in vitro efficacy experiments. 143B cells were orthotopically transplanted into the tibia of nude mice. Mouse models were randomized into the following groups 1 week after transplantation: Group 1, untreated control; Group 2, cisplatinum (CDDP) [intraperitoneal (i.p.) injection at 6 mg/kg weekly, for 3 weeks], positive control; Group 3, rMETase, 100 units/mouse i.p. daily, for 21 days. Tumor sizes and body weight were measured with calipers and a digital balance once per week, respectively. RESULTS: rMETase significantly inhibited osteosarcoma cell growth, in a dose-dependent manner, in vitro. Both CDDP and rMETase treatment significantly inhibited tumor volume compared to untreated control mice at 5 weeks after initiation. Tumor volumes were as follows: Group 1, untreated, control: 1808.2 ± 344 mm ; Group 2, CDDP: 1102.2 ± 316 mm , p=0.0008 compared to untreated control; Group 3, rMETase: 884.8 ± 361 mm , p=0.0001 compared to untreated control. There were no animal deaths in any group. The body weight of mice was not significantly different between any group. CONCLUSION: rMETase showed promising efficacy against osteosarcoma, a recalcitrant tumor type. Future studies will investigate the efficacy of rMETase on patient-derived orthotopic xenograft (PDOX) models of osteosarcoma as a bridge to testing rMETase in the clinic.
[Mh] Termos MeSH primário: Liases de Carbono-Enxofre/uso terapêutico
Terapia de Alvo Molecular
Osteossarcoma/tratamento farmacológico
Osteossarcoma/metabolismo
Proteínas Recombinantes/uso terapêutico
[Mh] Termos MeSH secundário: Animais
Peso Corporal/efeitos dos fármacos
Morte Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Cisplatino/farmacologia
Cisplatino/uso terapêutico
Modelos Animais de Doenças
Seres Humanos
Camundongos Nus
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.11 (L-methionine gamma-lyase); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE


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[PMID]:28766335
[Au] Autor:Bühning M; Friemel M; Leimkühler S
[Ad] Endereço:Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam , D-14476 Potsdam, Germany.
[Ti] Título:Functional Complementation Studies Reveal Different Interaction Partners of Escherichia coli IscS and Human NFS1.
[So] Source:Biochemistry;56(34):4592-4605, 2017 Aug 29.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The trafficking and delivery of sulfur to cofactors and nucleosides is a highly regulated and conserved process among all organisms. All sulfur transfer pathways generally have an l-cysteine desulfurase as an initial sulfur-mobilizing enzyme in common, which serves as a sulfur donor for the biosynthesis of sulfur-containing biomolecules like iron-sulfur (Fe-S) clusters, thiamine, biotin, lipoic acid, the molybdenum cofactor (Moco), and thiolated nucleosides in tRNA. The human l-cysteine desulfurase NFS1 and the Escherichia coli homologue IscS share a level of amino acid sequence identity of ∼60%. While E. coli IscS has a versatile role in the cell and was shown to have numerous interaction partners, NFS1 is mainly localized in mitochondria with a crucial role in the biosynthesis of Fe-S clusters. Additionally, NFS1 is also located in smaller amounts in the cytosol with a role in Moco biosynthesis and mcm s U34 thio modifications of nucleosides in tRNA. NFS1 and IscS were conclusively shown to have different interaction partners in their respective organisms. Here, we used functional complementation studies of an E. coli iscS deletion strain with human NFS1 to dissect their conserved roles in the transfer of sulfur to a specific target protein. Our results show that human NFS1 and E. coli IscS share conserved binding sites for proteins involved in Fe-S cluster assembly like IscU, but not with proteins for tRNA thio modifications or Moco biosynthesis. In addition, we show that human NFS1 was almost fully able to complement the role of IscS in Moco biosynthesis when its specific interaction partner protein MOCS3 from humans was also present.
[Mh] Termos MeSH primário: Liases de Carbono-Enxofre
Coenzimas
Escherichia coli
Teste de Complementação Genética
Metaloproteínas
Pteridinas
[Mh] Termos MeSH secundário: Sítios de Ligação
Liases de Carbono-Enxofre/genética
Liases de Carbono-Enxofre/metabolismo
Coenzimas/biossíntese
Coenzimas/genética
Escherichia coli/enzimologia
Escherichia coli/genética
Seres Humanos
Metaloproteínas/biossíntese
Metaloproteínas/genética
Nucleotidiltransferases/metabolismo
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
RNA de Transferência/metabolismo
Sulfurtransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (Metalloproteins); 0 (Pteridines); 0 (RNA, Bacterial); 73508-07-3 (molybdenum cofactor); 9014-25-9 (RNA, Transfer); EC 2.7.7.- (MOCS3 protein, human); EC 2.7.7.- (Nucleotidyltransferases); EC 2.8.1.- (Sulfurtransferases); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (NFS1 protein, human); EC 4.4.1.- (cysteine desulfurase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00627


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[PMID]:28615439
[Au] Autor:Rouault TA; Maio N
[Ad] Endereço:From the Molecular Medicine Branch, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892 rouault@mail.nih.gov.
[Ti] Título:Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways.
[So] Source:J Biol Chem;292(31):12744-12753, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent binding to recipient proteins. In this minireview, we discuss how discovery of the role of the mammalian cytosolic aconitase, known as iron regulatory protein 1 (IRP1), led to the characterization of the function of its Fe-S cluster in sensing and regulating cellular iron homeostasis. Moreover, we present an overview of recent studies that have provided insights into the mechanism of Fe-S cluster transfer to recipient Fe-S proteins.
[Mh] Termos MeSH primário: Homeostase
Proteína 1 Reguladora do Ferro/fisiologia
Ferro/fisiologia
Modelos Moleculares
[Mh] Termos MeSH secundário: Animais
Apoenzimas/química
Apoenzimas/metabolismo
Liases de Carbono-Enxofre/biossíntese
Liases de Carbono-Enxofre/química
Liases de Carbono-Enxofre/fisiologia
Transporte de Elétrons
Regulação Enzimológica da Expressão Gênica
Proteínas de Choque Térmico HSP70/biossíntese
Proteínas de Choque Térmico HSP70/química
Proteínas de Choque Térmico HSP70/fisiologia
Seres Humanos
Proteína 1 Reguladora do Ferro/biossíntese
Proteína 1 Reguladora do Ferro/química
Proteínas de Ligação ao Ferro/biossíntese
Proteínas de Ligação ao Ferro/química
Proteínas de Ligação ao Ferro/fisiologia
Proteínas Reguladoras do Ferro/biossíntese
Proteínas Reguladoras do Ferro/química
Proteínas Reguladoras do Ferro/fisiologia
Proteínas com Ferro-Enxofre/biossíntese
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/fisiologia
Proteínas Mitocondriais/biossíntese
Proteínas Mitocondriais/química
Proteínas Mitocondriais/fisiologia
Chaperonas Moleculares/biossíntese
Chaperonas Moleculares/química
Chaperonas Moleculares/fisiologia
Dobramento de Proteína
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Elementos de Resposta
Succinato Desidrogenase/biossíntese
Succinato Desidrogenase/química
Succinato Desidrogenase/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Apoenzymes); 0 (HSCB protein, human); 0 (HSP70 Heat-Shock Proteins); 0 (HSPA9 protein, human); 0 (ISCU protein, human); 0 (ISD11 protein, human); 0 (Iron-Binding Proteins); 0 (Iron-Regulatory Proteins); 0 (Iron-Sulfur Proteins); 0 (Mitochondrial Proteins); 0 (Molecular Chaperones); 0 (frataxin); E1UOL152H7 (Iron); EC 1.3.5.1 (SDHB protein, human); EC 1.3.99.1 (Succinate Dehydrogenase); EC 4.2.1.3 (IRP1 protein, human); EC 4.2.1.3 (Iron Regulatory Protein 1); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (NFS1 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.789537


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[PMID]:28607157
[Au] Autor:Loddeke M; Schneider B; Oguri T; Mehta I; Xuan Z; Reitzer L
[Ad] Endereço:Department of Biological Sciences, University of Texas at Dallas, Richardson, Texas, USA.
[Ti] Título:Anaerobic Cysteine Degradation and Potential Metabolic Coordination in Salmonella enterica and Escherichia coli.
[So] Source:J Bacteriol;199(16), 2017 Aug 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:has two CyuR-activated enzymes that degrade cysteine, i.e., the aerobic CdsH and an unidentified anaerobic enzyme; has only the latter. To identify the anaerobic enzyme, transcript profiling was performed for without and with overexpressed Thirty-seven genes showed at least 5-fold changes in expression, and the (formerly ) operon showed the greatest difference. Homology suggested that CyuP and CyuA represent a cysteine transporter and an iron-sulfur-containing cysteine desulfidase, respectively. and Δ mutants grown with cysteine generated substantially less sulfide and had lower growth yields. Oxygen affected the CyuR-dependent genes reciprocally; expression was greater anaerobically, whereas expression was greater aerobically. In and , anaerobic expression required and cysteine and was induced by l-cysteine, d-cysteine, and a few sulfur-containing compounds. Loss of either CyuA or RidA, both of which contribute to cysteine degradation to pyruvate, increased expression, which suggests that CyuA modulates intracellular cysteine concentrations. Phylogenetic analysis showed that CyuA homologs are present in obligate and facultative anaerobes, confirming an anaerobic function, and in archaeal methanogens and bacterial acetogens, suggesting an ancient origin. Our results show that CyuA is the major anaerobic cysteine-catabolizing enzyme in both and , and it is proposed that anaerobic cysteine catabolism can contribute to coordination of sulfur assimilation and amino acid synthesis. Sulfur-containing compounds such as cysteine and sulfide are essential and reactive metabolites. Exogenous sulfur-containing compounds can alter the thiol landscape and intracellular redox reactions and are known to affect several cellular processes, including swarming motility, antibiotic sensitivity, and biofilm formation. Cysteine inhibits several enzymes of amino acid synthesis; therefore, increasing cysteine concentrations could increase the levels of the inhibited enzymes. This inhibition implies that control of intracellular cysteine levels, which is the immediate product of sulfide assimilation, can affect several pathways and coordinate metabolism. For these and other reasons, cysteine and sulfide concentrations must be controlled, and this work shows that cysteine catabolism contributes to this control.
[Mh] Termos MeSH primário: Cisteína/metabolismo
Escherichia coli/metabolismo
Salmonella enterica/metabolismo
[Mh] Termos MeSH secundário: Anaerobiose
Biotransformação
Liases de Carbono-Enxofre/genética
Liases de Carbono-Enxofre/metabolismo
Escherichia coli/genética
Escherichia coli/crescimento & desenvolvimento
Deleção de Genes
Perfilação da Expressão Gênica
Proteínas de Membrana Transportadoras/metabolismo
Filogenia
Salmonella enterica/genética
Salmonella enterica/crescimento & desenvolvimento
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Transport Proteins); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (cysteine desulfurase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170810
[Lr] Data última revisão:
170810
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170614
[St] Status:MEDLINE


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[PMID]:28602917
[Au] Autor:Revtovich SV; Morozova EA; Kulikova VV; Anufrieva NV; Osipova TI; Koval VS; Nikulin AD; Demidkina TV
[Ad] Endereço:Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
[Ti] Título:Crystal structure of mutant form Cys115His of Citrobacter freundii methionine γ-lyase complexed with l-norleucine.
[So] Source:Biochim Biophys Acta;1865(9):1123-1128, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The mutant form of Citrobacter freundii methionine γ-lyase with the replacement of active site Cys115 for His has been found to be inactive in the γ-elimination reaction of methionine while fully active in the γ-elimination reaction of O-acetyl-l-homoserine and in the ß-elimination reaction of S-alk(en)yl-substituted cysteines. In this work, the crystal structure of the mutant enzyme complexed with competitive inhibitor, l-norleucine was determined at 1.45Å resolution. At the enzyme active site the inhibitor proved to be bound both noncovalently and covalently, which corresponds to the two intermediates of the γ- and ß-elimination reactions, Michaelis complex and the external aldimine. Analysis of the structure allowed us to suggest the possible reason for the inability of the mutant enzyme to catalyze the physiological reaction.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Liases de Carbono-Enxofre/química
Citrobacter freundii/enzimologia
Mutação de Sentido Incorreto
Norleucina/metabolismo
Mutação Puntual
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/metabolismo
Liases de Carbono-Enxofre/antagonistas & inibidores
Liases de Carbono-Enxofre/metabolismo
Domínio Catalítico
Citrobacter freundii/genética
Cristalografia por Raios X
Modelos Moleculares
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 832C8OV84S (Norleucine); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.11 (L-methionine gamma-lyase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE


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[PMID]:28592683
[Au] Autor:Banerjee M; Chakravarty D; Ballal A
[Ad] Endereço:Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai 400 085, India manishab@barc.gov.in manisha.banerjee@gmail.com.
[Ti] Título:Molecular basis of function and the unusual antioxidant activity of a cyanobacterial cysteine desulfurase.
[So] Source:Biochem J;474(14):2435-2447, 2017 Jul 06.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cysteine desulfurases, which supply sulfur for iron-sulfur cluster biogenesis, are broadly distributed in all phyla including cyanobacteria, the progenitors of plant chloroplasts. The SUF (sulfur utilization factor) system is responsible for Fe-S cluster biosynthesis under stress. The operon from cyanobacterium PCC 7120 showed the presence of a cysteine desulfurase, ( ), but not the accessory sulfur-accepting protein (SufE). However, an open reading frame ( ) encoding a SufE-like protein (termed AsaE, sulfur acceptor E) was found at a location distinct from the operon. The purified SufS protein existed as a pyridoxal 5' phosphate (PLP)-containing dimer with a relatively low desulfurase activity. Interestingly, in the presence of the AsaE protein, the catalytic efficiency of this reaction increased 10-fold. In particular, for sulfur mobilization, the AsaE protein partnered only SufS and not other cysteine desulfurases from The SufS protein was found to physically interact with the AsaE protein, demonstrating that AsaE was indeed the missing partner of SufS. The conserved cysteine of the SufS or the AsaE protein was essential for activity but not for their physical association. Curiously, overexpression of the SufS protein in caused reduced formation of reactive oxygen species on exposure to hydrogen peroxide (H O ), resulting in superior oxidative stress tolerance to the oxidizing agent when compared with the wild-type strain. Overall, the results highlight the functional interaction between the two proteins that mediate sulfur mobilization, in the cyanobacterial SUF pathway, and further reveal that overexpression of SufS can protect cyanobacteria from oxidative stress.
[Mh] Termos MeSH primário: Anabaena/enzimologia
Proteínas de Bactérias/metabolismo
Liases de Carbono-Enxofre/metabolismo
Sulfurtransferases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Anabaena/efeitos dos fármacos
Anabaena/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biocatálise/efeitos dos fármacos
Liases de Carbono-Enxofre/química
Liases de Carbono-Enxofre/genética
Sequência Conservada
Dimerização
Farmacorresistência Bacteriana
Liases/química
Liases/genética
Liases/metabolismo
Mutagênese Sítio-Dirigida
Mutação
Fases de Leitura Aberta/efeitos dos fármacos
Óperon/efeitos dos fármacos
Oxidantes/farmacologia
Oxirredução
Estresse Oxidativo/efeitos dos fármacos
Multimerização Proteica
Fosfato de Piridoxal/metabolismo
Espécies Reativas de Oxigênio/agonistas
Espécies Reativas de Oxigênio/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Sulfurtransferases/química
Sulfurtransferases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Oxidants); 0 (Reactive Oxygen Species); 0 (Recombinant Proteins); 5V5IOJ8338 (Pyridoxal Phosphate); EC 2.8.1.- (Sulfurtransferases); EC 4.- (Lyases); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (cysteine desulfurase); EC 4.4.1.16 (selenocysteine lyase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170290


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[PMID]:28511016
[Au] Autor:Schnicker NJ; De Silva SM; Todd JD; Dey M
[Ad] Endereço:Department of Chemistry, The University of Iowa , Iowa City, Iowa 52242, United States.
[Ti] Título:Structural and Biochemical Insights into Dimethylsulfoniopropionate Cleavage by Cofactor-Bound DddK from the Prolific Marine Bacterium Pelagibacter.
[So] Source:Biochemistry;56(23):2873-2885, 2017 Jun 13.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enormous amounts of the organic osmolyte dimethylsulfoniopropionate (DMSP) are produced in marine environments where bacterial DMSP lyases cleave it, yielding acrylate and the climate-active gas dimethyl sulfide (DMS). SAR11 bacteria are the most abundant clade of heterotrophic bacteria in the oceans and play a key role in DMSP catabolism. An important environmental factor affecting DMS generation via DMSP lyases is the availability of metal ions because they are essential cofactors for many of these enzymes. Here we examine the structure and activity of DddK in the presence of various metal ions. We have established that DddK containing a double-stranded ß-helical motif utilizes various divalent metal ions as cofactors for catalytic activity. However, nickel, an abundant metal ion in marine environments, adopts a distorted octahedral coordination environment and conferred the highest DMSP lyase activity. Crystal structures of cofactor-bound DddK reveal key metal ion binding and catalytic residues and provide the first rationalization for varying activities with different metal ions. The structures of DddK along with site-directed mutagenesis and ultraviolet-visible studies are consistent with Tyr 64 acting as a base to initiate the ß-elimination reaction of DMSP. Our biochemical and structural studies provide a detailed understanding of DMS generation by one of the ocean's most prolific bacteria.
[Mh] Termos MeSH primário: Alphaproteobacteria/enzimologia
Organismos Aquáticos/enzimologia
Proteínas de Bactérias/metabolismo
Liases de Carbono-Enxofre/metabolismo
Modelos Moleculares
Compostos de Sulfônio/metabolismo
[Mh] Termos MeSH secundário: Acrilatos/metabolismo
Alphaproteobacteria/crescimento & desenvolvimento
Sequência de Aminoácidos
Organismos Aquáticos/crescimento & desenvolvimento
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Sítios de Ligação
Liases de Carbono-Enxofre/química
Liases de Carbono-Enxofre/genética
Domínio Catalítico
Sequência Conservada
Cristalografia por Raios X
Mutagênese Sítio-Dirigida
Mutação
Níquel/química
Oceanos e Mares
Conformação Proteica
Conformação Proteica em Folha beta
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Alinhamento de Sequência
Sulfetos/metabolismo
Compostos de Sulfônio/química
Tirosina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acrylates); 0 (Bacterial Proteins); 0 (Recombinant Fusion Proteins); 0 (Sulfides); 0 (Sulfonium Compounds); 42HK56048U (Tyrosine); 7OV03QG267 (Nickel); C884XA7QGG (dimethylpropiothetin); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.- (dimethylsulfoniopropionate lyase); J94PBK7X8S (acrylic acid); QS3J7O7L3U (dimethyl sulfide)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170706
[Lr] Data última revisão:
170706
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00099



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