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  1 / 20172 MEDLINE  
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[PMID]:29216817
[Au] Autor:Nivala O; Faccio G; Arvas M; Permi P; Buchert J; Kruus K; Mattinen ML
[Ad] Endereço:VTT Technical Research Centre of Finland, Ltd., P.O. Box 1000, FI-02044, Espoo, Finland. outi.nivala@helsinki.fi.
[Ti] Título:Characterization of sulfhydryl oxidase from Aspergillus tubingensis.
[So] Source:BMC Biochem;18(1):15, 2017 12 08.
[Is] ISSN:1471-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. RESULTS: The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initial activity was retained after incubation at 50 °C for 20 h. AtSOX contains a non-covalently bound flavin cofactor. The enzyme oxidised a sulfhydryl group of glutathione to form a disulfide bond, as verified by nuclear magnetic resonance spectroscopy. AtSOX preferred glutathione as a substrate over cysteine and dithiothreitol. The activity of the enzyme was totally inhibited by 10 mM zinc sulphate. Peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, were not oxidised by the enzyme. Based on the analysis of 33 fungal genomes, SOX enzyme encoding genes were found close to nonribosomal peptide synthetases (NRPS) but not with polyketide synthases (PKS). In the phylogenetic tree, constructed from 25 SOX and thioredoxin reductase sequences from IPR000103 InterPro family, AtSOX was evolutionary closely related to other Aspergillus SOXs. Oxidoreductases involved in the maturation of nonribosomal peptides of fungal and bacterial origin, namely GliT, HlmI and DepH, were also evolutionary closely related to AtSOX whereas fungal thioreductases were more distant. CONCLUSIONS: AtSOX (55 kDa) is a fungal secreted flavin-dependent enzyme with good stability to both pH and temperature. A Michaelis-Menten behaviour was observed with reduced glutathione as a substrate. Based on the location of SOX enzyme encoding genes close to NRPSs, SOXs could be involved in the secondary metabolism and act as an accessory enzyme in the production of nonribosomal peptides.
[Mh] Termos MeSH primário: Aspergillus/enzimologia
Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Dissulfetos
Estabilidade Enzimática
Glutationa/metabolismo
Concentração de Íons de Hidrogênio
Oxirredutases/química
Oxirredutases/genética
Oxirredutases/isolamento & purificação
Peptídeo Sintases
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Disulfides); EC 1.- (Oxidoreductases); EC 1.8.3.- (sulfhydryl oxidase); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (non-ribosomal peptide synthase); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1186/s12858-017-0090-4


  2 / 20172 MEDLINE  
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[PMID]:28970007
[Au] Autor:Preissler J; Wahlefeld S; Lorent C; Teutloff C; Horch M; Lauterbach L; Cramer SP; Zebger I; Lenz O
[Ad] Endereço:Technische Universität Berlin, Institut für Chemie, Sekr. PC14, Straße des 17. Juni 135, D-10623 Berlin, Germany.
[Ti] Título:Enzymatic and spectroscopic properties of a thermostable [NiFe]­hydrogenase performing H -driven NAD -reduction in the presence of O .
[So] Source:Biochim Biophys Acta;1859(1):8-18, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Biocatalysts that mediate the H -dependent reduction of NAD to NADH are attractive from both a fundamental and applied perspective. Here we present the first biochemical and spectroscopic characterization of an NAD -reducing [NiFe]­hydrogenase that sustains catalytic activity at high temperatures and in the presence of O , which usually acts as an inhibitor. We isolated and sequenced the four structural genes, hoxFUYH, encoding the soluble NAD -reducing [NiFe]­hydrogenase (SH) from the thermophilic betaproteobacterium, Hydrogenophilus thermoluteolus TH-1 (Ht). The HtSH was recombinantly overproduced in a hydrogenase-free mutant of the well-studied, H -oxidizing betaproteobacterium Ralstonia eutropha H16 (Re). The enzyme was purified and characterized with various biochemical and spectroscopic techniques. Highest H -mediated NAD reduction activity was observed at 80°C and pH6.5, and catalytic activity was found to be sustained at low O concentrations. Infrared spectroscopic analyses revealed a spectral pattern for as-isolated HtSH that is remarkably different from those of the closely related ReSH and other [NiFe]­hydrogenases. This indicates an unusual configuration of the oxidized catalytic center in HtSH. Complementary electron paramagnetic resonance spectroscopic analyses revealed spectral signatures similar to related NAD -reducing [NiFe]­hydrogenases. This study lays the groundwork for structural and functional analyses of the HtSH as well as application of this enzyme for H -driven cofactor recycling under oxic conditions at elevated temperatures.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Cupriavidus necator/enzimologia
Temperatura Alta
Hidrogênio/química
Hidrogenase/química
Hydrogenophilaceae/enzimologia
NAD/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Cupriavidus necator/genética
Estabilidade Enzimática
Hidrogênio/metabolismo
Hidrogenase/genética
Hidrogenase/metabolismo
Hydrogenophilaceae/genética
NAD/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0U46U6E8UK (NAD); 7YNJ3PO35Z (Hydrogen); EC 1.12.- (nickel-iron hydrogenase); EC 1.12.7.2 (Hydrogenase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE


  3 / 20172 MEDLINE  
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[PMID]:29194017
[Au] Autor:Abdul Manan FM; Attan N; Widodo N; Aboul-Enein HY; Wahab RA
[Ad] Endereço:a Department of Chemistry, Faculty of Science , Universiti Teknologi Malaysia , Skudai , Malaysia.
[Ti] Título:Rhizomucor miehei lipase immobilized on reinforced chitosan-chitin nanowhiskers support for synthesis of eugenyl benzoate.
[So] Source:Prep Biochem Biotechnol;48(1):92-102, 2018 Jan 02.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An alternative environmentally benign support was prepared from chitosan-chitin nanowhiskers (CS/CNWs) for covalent immobilization of Rhizomucor miehei lipase (RML) to increase the operational stability and recyclability of RML in synthesizing eugenyl benzoate. The CS/CNWs support and RML-CS/CNWs were characterized using X-ray diffraction, fluorescent microscopy, and Fourier transform infrared spectroscopy. Efficiency of the RML-CS/CNWs was compared to the free RML to synthesize eugenyl benzoate for parameters: reaction temperature, stirring rate, reusability, and thermal stability. Under optimal experimental conditions (50°C, 250 rpm, catalyst loading 3 mg/mL), a twofold increase in yield of eugenyl benzoate was observed for RML-CS/CNWs as compared to free RML, with the former achieving maximum yield of the ester at 62.1% after 5 hr. Results demonstrated that the strategy adopted to prepare RML-CS/CNWs was useful, producing an improved and prospectively greener biocatalyst that supported a sustainable process to prepare eugenyl benzoate. Moreover, RML-CS/CNWs are biodegradable and perform esterification reactions under ambient conditions as compared to the less eco-friendly conventional acid catalyst. This research provides a facile and promising approach for improving activity of RML in which the resultant RML-CS/CNWs demonstrated good operational stability for up to eight successive esterification cycles to synthesize eugenyl benzoate.
[Mh] Termos MeSH primário: Benzoatos/metabolismo
Quitina/química
Quitosana/química
Enzimas Imobilizadas/metabolismo
Eugenol/análogos & derivados
Lipase/metabolismo
Rhizomucor/enzimologia
[Mh] Termos MeSH secundário: Benzoatos/química
Estabilidade Enzimática
Enzimas Imobilizadas/química
Esterificação
Eugenol/metabolismo
Microbiologia Industrial
Lipase/química
Nanoestruturas/química
Rhizomucor/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoates); 0 (Enzymes, Immobilized); 1398-61-4 (Chitin); 3T8H1794QW (Eugenol); 9012-76-4 (Chitosan); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2017.1405021


  4 / 20172 MEDLINE  
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[PMID]:29289886
[Au] Autor:Li HY; Lee JD; Chen CW; Sun YC; Cheng WC
[Ad] Endereço:Genomics Research Center, Academia Sinica, 128, Academia Road, Section 2, Nankang, Taipei 115, Taiwan; Institute of Biochemistry and Molecular Biology, National Yang-Ming University, 155, Linong Street, Section 2, Taipei 112, Taiwan.
[Ti] Título:Synthesis of (3S,4S,5S)-trihydroxylpiperidine derivatives as enzyme stabilizers to improve therapeutic enzyme activity in Fabry patient cell lines.
[So] Source:Eur J Med Chem;144:626-634, 2018 Jan 20.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:A series of 3S,4S,5S-trihydroxylated piperidines bearing structural diversity at C-2 or C-6 positions has been synthesized and tested to determine their ability to stabilize the activity of recombinant human α-Galactosidase A (rh-α-Gal A). Hit molecules were identified by rapid inhibitory activity screening, and then further investigated for their ability to protect this enzyme from thermo-induced denaturation and enhance its activity in Fabry patient cell lines. Our study resulted in the identification of a new class of small molecules as enzyme stabilizers for the potential treatment of Fabry disease. Of these, stabilizer 21 was the most effective, showing a 12-fold increase in rh-α-Gal A activity in Fabry disease cell lines.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Doença de Fabry/tratamento farmacológico
Piperidinas/farmacologia
alfa-Galactosidase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Linhagem Celular
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Estabilidade Enzimática
Doença de Fabry/metabolismo
Doença de Fabry/patologia
Seres Humanos
Estrutura Molecular
Piperidinas/síntese química
Piperidinas/química
Proteínas Recombinantes/metabolismo
Relação Estrutura-Atividade
alfa-Galactosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Piperidines); 0 (Recombinant Proteins); EC 3.2.1.22 (alpha-Galactosidase); EC 3.2.1.22 (alpha-galactosidase A, human)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180101
[St] Status:MEDLINE


  5 / 20172 MEDLINE  
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[PMID]:29200284
[Au] Autor:He X; Liao X; Li H; Xia W; Sun H
[Ad] Endereço:MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University , Guangzhou 510275, China.
[Ti] Título:Bismuth-Induced Inactivation of Ferric Uptake Regulator from Helicobacter pylori.
[So] Source:Inorg Chem;56(24):15041-15048, 2017 Dec 18.
[Is] ISSN:1520-510X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ferric uptake regulator (Fur) of Helicobacter pylori is a global regulator that is important for bacterial colonization and survival within the gastric mucosa. H. pylori Fur (HpFur) is unique in its ability to regulate gene expression in both metal-bound (holo-Fur) and metal-free (apo-Fur) forms. Bismuth-based drugs are widely used for the treatment of H. pylori infection. However, the mechanism of action of bismuth drug was not fully understood. Recently, it has been reported that bismuth drugs could interfere with the bacterial ferric uptake pathway and inhibit bacterial growth, implying intrinsic correlation between bismuth drug and bacterial iron metabolism. Herein, we demonstrate that Bi(III) binds to HpFur protein specifically at the physiologically important S1 site, which further leads to protein oligomerization and loss of DNA binding capability. The targeting of HpFur by bismuth drugs significantly reduced transcription levels of its regulated genes, which are crucial for bacterial physiology and metabolism. Our studies present direct evidence that perturbation of iron metabolism in H. pylori by bismuth might serve as one of the mechanisms for the antimicrobial activity of bismuth drugs.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Bactérias/antagonistas & inibidores
Bismuto/farmacologia
Inibidores Enzimáticos/farmacologia
Helicobacter pylori/efeitos dos fármacos
Proteínas Repressoras/antagonistas & inibidores
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
DNA Bacteriano/metabolismo
Estabilidade Enzimática/efeitos dos fármacos
Infecções por Helicobacter/tratamento farmacológico
Infecções por Helicobacter/microbiologia
Helicobacter pylori/metabolismo
Seres Humanos
Modelos Moleculares
Conformação Proteica/efeitos dos fármacos
Multimerização Proteica/efeitos dos fármacos
Proteínas Repressoras/química
Proteínas Repressoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Enzyme Inhibitors); 0 (Repressor Proteins); 0 (ferric uptake regulating proteins, bacterial); U015TT5I8H (Bismuth)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1021/acs.inorgchem.7b02380


  6 / 20172 MEDLINE  
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[PMID]:29327928
[Au] Autor:Zhu ZJ; Chen HM; Chen JJ; Yang R; Yan XJ
[Ad] Endereço:Key Laboratory of Marine Biotechnology of Zhejiang Province, Ningbo University , Ningbo, Zhejiang 315211, China.
[Ti] Título:One-Step Bioconversion of Fatty Acids into C8-C9 Volatile Aroma Compounds by a Multifunctional Lipoxygenase Cloned from Pyropia haitanensis.
[So] Source:J Agric Food Chem;66(5):1233-1241, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The multifunctional lipoxygenase PhLOX cloned from Pyropia haitanensis was expressed in Escherichia coli with 24.4 mg·L yield. PhLOX could catalyze the one-step bioconversion of C18-C22 fatty acids into C8-C9 volatile organic compounds (VOCs), displaying higher catalytic efficiency for eicosenoic and docosenoic acids than for octadecenoic acids. C20:5 was the most suitable substrate among the tested fatty acids. The C8-C9 VOCs were generated in good yields from fatty acids, e.g., 2E-nonenal from C20:4, and 2E,6Z-nonadienal from C20:5. Hydrolyzed oils were also tested as substrates. The reactions mainly generated 2E,4E-pentadienal, 2E-octenal, and 2E,4E-octadienal from hydrolyzed sunflower seed oil, corn oil, and fish oil, respectively. PhLOX showed good stability after storage at 4 °C for 2 weeks and broad tolerance to pH and temperature. These desirable properties of PhLOX make it a promising novel biocatalyst for the industrial production of volatile aroma compounds.
[Mh] Termos MeSH primário: Ácidos Graxos/metabolismo
Lipoxigenase/genética
Lipoxigenase/metabolismo
Proteínas Recombinantes/metabolismo
Rodófitas/enzimologia
Compostos Orgânicos Voláteis/metabolismo
[Mh] Termos MeSH secundário: Clonagem Molecular
Óleo de Milho/metabolismo
Estabilidade Enzimática
Ácidos Erúcicos/metabolismo
Escherichia coli/genética
Ácidos Graxos Monoinsaturados/metabolismo
Óleos de Peixe/metabolismo
Expressão Gênica
Concentração de Íons de Hidrogênio
Rodófitas/genética
Especificidade por Substrato
Óleo de Girassol/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Erucic Acids); 0 (Fatty Acids); 0 (Fatty Acids, Monounsaturated); 0 (Fish Oils); 0 (Recombinant Proteins); 0 (Sunflower Oil); 0 (Volatile Organic Compounds); 8001-30-7 (Corn Oil); EC 1.13.11.12 (Lipoxygenase); UDX6WPL94T (eicosenoic acid)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05341


  7 / 20172 MEDLINE  
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[PMID]:28742253
[Au] Autor:Bai Y; Wang C; Liang G; Lai W; Xue H; Ling Y; Cheng M; Liu K
[Ad] Endereço:State Key Laboratory of Toxicology and Medical Countermeasures, Beijing Institute of Pharmacology and Toxicology, Beijing, 100850, China.
[Ti] Título:Precisely Designed Isopeptide Bridge-Crosslinking Endows Artificial Hydrolases with High Stability and Catalytic Activity under Extreme Denaturing Conditions.
[So] Source:Chem Asian J;12(19):2539-2543, 2017 Oct 05.
[Is] ISSN:1861-471X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Enzymes normally lose their activities under extreme conditions due to the dissociation of their active tertiary structure. If an enzyme could maintain its catalytic activity under non-physiological or denaturing conditions, it might be used in more applications in the pharmaceutical and chemical industries. Recently, we reported a coiled-coil six-helical bundle (6HB) structure as a scaffold for designing artificial hydrolytic enzymes. Here, intermolecular isopeptide bonds were incorporated to enhance the stability and activity of such biomolecules under denaturing conditions. These isopeptide bridge-tethered 6HB enzymes showed exceptional stability against unfolding and retained or even had increased catalytic activity for a model hydrolysis reaction under thermal and chemical denaturing conditions. Thus, isopeptide bond-tethering represents an efficient route to construct ultrastable artificial hydrolases, with promising potential to maintain biocatalysis under extreme conditions.
[Mh] Termos MeSH primário: Reagentes para Ligações Cruzadas/química
Hidrolases/química
Peptídeos/química
[Mh] Termos MeSH secundário: Biocatálise
Reagentes para Ligações Cruzadas/metabolismo
Estabilidade Enzimática
Hidrolases/metabolismo
Cinética
Peptídeos/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (Peptides); EC 3.- (Hydrolases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/asia.201701021


  8 / 20172 MEDLINE  
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[PMID]:29307827
[Au] Autor:Manning ME; Danson EJ; Calderone CT
[Ad] Endereço:Department of Chemistry, Carleton College, 1 North College Street, Northfield, MN 55057, United States.
[Ti] Título:Functional chararacterization of the enzymes TabB and TabD involved in tabtoxin biosynthesis by Pseudomonas syringae.
[So] Source:Biochem Biophys Res Commun;496(1):212-217, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pseudomonas syringae pv. tabaci ATCC 11528 produces tabtoxin, a ß-lactam-containing dipeptide phytotoxin. Tabtoxinine-ß-lactam (TßL), one of tabtoxin's constituent amino acids, structurally mimics lysine, and many of the proteins encoded by the tabtoxin biosynthetic gene cluster are homologs of lysine biosynthetic enzymes, suggesting that the tabtoxin and lysine biosynthetic routes parallel one another. We cloned and expressed TabB and TabD, predicted homologs of tetrahydrodipicolinate (THDPA)-N-acyltransferase and N-acyl-THDPA aminotransferase, respectively, to determine their activities in vitro. We confirmed that TabB succinylates THDPA and that TabD is a PLP-dependent aminotransferase that utilizes glutamate as an amine donor. Surprisingly, we also found that though TabD could utilize the TabB product N-succinyl-THDPA as a substrate, THDPA itself was also recognized. These observations reveal that TabB functionally duplicates DapD, the THDPA-N-succinyltransferase involved in lysine biosynthesis, and reinforce the close relationship between the metabolic logics underpinning the respective biosynthetic pathways.
[Mh] Termos MeSH primário: Acetiltransferases/química
Acetiltransferases/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Dipeptídeos/biossíntese
Pseudomonas syringae/metabolismo
Transaminases/química
Transaminases/metabolismo
[Mh] Termos MeSH secundário: Ativação Enzimática
Estabilidade Enzimática
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Dipeptides); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (TabB protein, Pseudomonas syringae); EC 2.6.1.- (Transaminases); H3YX70R64N (tabtoxin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


  9 / 20172 MEDLINE  
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[PMID]:29236500
[Au] Autor:Liu X; Liu T; Zhang Y; Xin F; Mi S; Wen B; Gu T; Shi X; Wang F; Sun L
[Ad] Endereço:Laboratory of Biomanufacturing and Food Engineering, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences , Beijing 100193, P.R. China.
[Ti] Título:Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-ß-Xylanase from Caldicellulosiruptor owensensis.
[So] Source:J Agric Food Chem;66(1):187-193, 2018 Jan 10.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Xylanases (EC 3.2.1.8) are a kind of enzymes degrading xylan to xylooligosaccharides (XOS) and have been widely used in a variety of industrial applications. Among them, xylanases from thermophilic microorganisms have distinct advantages in industries that require high temperature conditions. The CoXynA gene, encoding a glycoside hydrolase (GH) family 10 xylanase, was identified from thermophilic Caldicellulosiruptor owensensis and was overexpressed in Escherichia coli. Recombinant CoXynA showed optimal activity at 90 °C with a half-life of about 1 h at 80 °C and exhibited highest activity at pH 7.0. The activity of CoXynA activity was affected by a variety of cations. CoXynA showed distinct substrate specificities for beechwood xylan and birchwood xylan. The crystal structure of CoXynA was solved and a molecular dynamics simulation of CoXynA was performed. The relatively high thermostability of CoXynA was proposed to be due to the increased overall protein rigidity resulting from the reduced length and fluctuation of Loop 7.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Endo-1,4-beta-Xilanases/química
Endo-1,4-beta-Xilanases/metabolismo
Firmicutes/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Betula/química
Cristalografia por Raios X
Endo-1,4-beta-Xilanases/genética
Estabilidade Enzimática
Escherichia coli/genética
Fagus/química
Concentração de Íons de Hidrogênio
Cinética
Simulação de Dinâmica Molecular
Conformação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Madeira/química
Xilanos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); 0 (Xylans); EC 3.2.1.8 (Endo-1,4-beta Xylanases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b03607


  10 / 20172 MEDLINE  
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[PMID]:29242153
[Au] Autor:Raj R; Mitra S; Gopal B
[Ad] Endereço:Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
[Ti] Título:Characterization of Staphylococcus epidermidis Polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2.
[So] Source:Biochem Biophys Res Commun;495(2):2078-2084, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polynucleotide phosphorylase catalyzes both 3'-5' exoribonuclease and polyadenylation reactions. The crystal structure of Staphylococcus epidermidis PNPase revealed a bound phosphate in the PH2 domain of each protomer coordinated by three adjacent serine residues. Mutational analysis suggests that phosphate coordination by these serine residues is essential to maintain the catalytic center in an active conformation. We note that PNPase forms a complex with RNase J1 and RNase J2 without substantially altering either exo-ribonuclease or polyadenylation activity of this enzyme. This decoupling of catalytic activity from protein-protein interactions suggests that association of these endo- or exo-ribonucleases with PNPase could be more relevant for cellular localization or concerted targeting of structured RNA for recycling.
[Mh] Termos MeSH primário: Simulação de Acoplamento Molecular
Nucleotidiltransferases/química
Nucleotidiltransferases/ultraestrutura
Ribonucleases/química
Ribonucleases/ultraestrutura
Staphylococcus epidermidis/enzimologia
[Mh] Termos MeSH secundário: Sítios de Ligação
Ativação Enzimática
Estabilidade Enzimática
Modelos Químicos
Complexos Multienzimáticos
Ligação Proteica
Conformação Proteica
Relação Estrutura-Atividade
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Multienzyme Complexes); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.- (polynucleotide pyrophosphorylase); EC 3.1.- (Ribonucleases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE



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