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[PMID]:29378242
[Au] Autor:Wang X; Xue M; Zhao M; He F; Li C; Li X
[Ad] Endereço:Center for Translational Medicine, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, Shaanxi, China; Key Laboratory for Tumor Precision Medicine of Shaanxi Province, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, Shaanxi, China.
[Ti] Título:Identification of a novel mutation (Ala66Thr) of SRY gene causes XY pure gonadal dysgenesis by affecting DNA binding activity and nuclear import.
[So] Source:Gene;651:143-151, 2018 Apr 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Sex-determining region of the Y chromosome (SRY) gene plays a crucial role in male sexual differentiation and development. Several mutations in the SRY gene have been reported in the high mobility group (HMG) box domain and can cause gonadal dysgenesis symptoms. In this study, we report that a novel missense mutation in the SRY gene, a G to A transition within the HMG box, causes the Ala66Thr amino acid substitution in a female patient presenting 46,XY karyotype with pure gonadal dysgenesis. The G to A base transition was not found in the SRY sequence after the screening of 100 normal males. Furthermore, Ala66Thr mutation drastically reduced the binding capacity of SRY to DNA sequences, whereas wild-type SRY protein showed the normal binding capacity to DNA sequences in vitro. We also found that the mutant SRY protein was partly localized in cytoplasm, whereas wild-type SRY protein was strictly localized in cell nucleus. In addition, we analyzed the three-dimensional structure of SRY protein by homology modeling methods. In conclusion, we identified a novel SRY mutation in a 46,XY female patient with pure gonadal dysgenesis, demonstrating the importance of the Ala66Thr mutation in DNA binding activity and nuclear transport.
[Mh] Termos MeSH primário: Disgenesia Gonadal 46 XY/genética
Mutação de Sentido Incorreto
Proteína da Região Y Determinante do Sexo/genética
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Adolescente
Adulto
Alanina
DNA/metabolismo
Feminino
Células HEK293
Seres Humanos
Cariotipagem
Masculino
Ligação Proteica
Conformação Proteica
Análise de Sequência de DNA
Proteína da Região Y Determinante do Sexo/química
Proteína da Região Y Determinante do Sexo/metabolismo
Treonina
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sex-Determining Region Y Protein); 2ZD004190S (Threonine); 9007-49-2 (DNA); OF5P57N2ZX (Alanine)
[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:180130
[St] Status:MEDLINE


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[PMID]:29410408
[Au] Autor:Kuncha SK; Mazeed M; Singh R; Kattula B; Routh SB; Sankaranarayanan R
[Ad] Endereço:CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad, 500007, India.
[Ti] Título:A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia.
[So] Source:Nat Commun;9(1):511, 2018 02 06.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:D-aminoacyl-tRNA deacylase (DTD), a bacterial/eukaryotic trans-editing factor, removes D-amino acids mischarged on tRNAs and achiral glycine mischarged on tRNA . An invariant cross-subunit Gly-cisPro motif forms the mechanistic basis of L-amino acid rejection from the catalytic site. Here, we present the identification of a DTD variant, named ATD (Animalia-specific tRNA deacylase), that harbors a Gly-transPro motif. The cis-to-trans switch causes a "gain of function" through L-chiral selectivity in ATD resulting in the clearing of L-alanine mischarged on tRNA (G4•U69) by eukaryotic AlaRS. The proofreading activity of ATD is conserved across diverse classes of phylum Chordata. Animalia genomes enriched in tRNA (G4•U69) genes are in strict association with the presence of ATD, underlining the mandatory requirement of a dedicated factor to proofread tRNA misaminoacylation. The study highlights the emergence of ATD during genome expansion as a key event associated with the evolution of Animalia.
[Mh] Termos MeSH primário: Alanina/química
Aminoaciltransferases/química
Aminoacil-RNA de Transferência/química
Treonina/química
Aminoacilação de RNA de Transferência/genética
[Mh] Termos MeSH secundário: Alanina/genética
Alanina/metabolismo
Sequência de Aminoácidos
Aminoaciltransferases/genética
Aminoaciltransferases/metabolismo
Animais
Apicomplexa/genética
Apicomplexa/metabolismo
Bactérias/genética
Bactérias/metabolismo
Sítios de Ligação
Evolução Biológica
Clonagem Molecular
Cristalografia por Raios X
Expressão Gênica
Seres Humanos
Modelos Moleculares
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Aminoacil-RNA de Transferência/genética
Aminoacil-RNA de Transferência/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Treonina/genética
Treonina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Transfer, Amino Acyl); 0 (Recombinant Proteins); 2ZD004190S (Threonine); EC 2.3.2.- (Aminoacyltransferases); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180208
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02204-w


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[PMID]:29318298
[Au] Autor:Jukic M; Grabrijan K; Kadic S; Lera Garrido FJ; Sosic I; Gobec S; Obreza A
[Ti] Título:Chlorocarbonylsulfenyl Chloride Cyclizations Towards Piperidin-3-yl-oxathiazol-2-ones as Potential Covalent Inhibitors of Threonine Proteases.
[So] Source:Acta Chim Slov;64(4):771-781, 2017 Dec.
[Is] ISSN:1318-0207
[Cp] País de publicação:Slovenia
[La] Idioma:eng
[Ab] Resumo:Using rescaffolding approach, we designed piperidine compounds decorated with an electrophilic oxathiazol-2-one moiety that is known to confer selectivity towards threonine proteases. Our efforts to prepare products according to the published procedures were not successful. Furthermore we identified major side products containing nitrile functional group, resulting from carboxamide dehydration. We systematically optimized reaction conditions towards our desired products to identify heating of carboxamides with chlorocarbonylsulfenyl chloride and sodium carbonate as base in dioxane at 100 °C. Our efforts culminated in the preparation of a small series of piperidin-3-yl-oxathiazol-2-ones that are suitable for further biological evaluation.
[Mh] Termos MeSH primário: Piperidinas/química
Inibidores de Proteases/síntese química
Tiazóis/química
Treonina/metabolismo
[Mh] Termos MeSH secundário: Ciclização
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Piperidines); 0 (Protease Inhibitors); 0 (Thiazoles); 2ZD004190S (Threonine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE


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[PMID]:28468956
[Au] Autor:Jasnovidova O; Krejcikova M; Kubicek K; Stefl R
[Ad] Endereço:CEITEC - Central European Institute of Technology, Masaryk University, Brno, Czech Republic olga.jasnovidova@ceitec.muni.cz richard.stefl@ceitec.muni.cz.
[Ti] Título:Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p.
[So] Source:EMBO Rep;18(6):906-913, 2017 Jun.
[Is] ISSN:1469-3178
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phosphorylation patterns of the C-terminal domain (CTD) of largest subunit of RNA polymerase II (called the CTD code) orchestrate the recruitment of RNA processing and transcription factors. Recent studies showed that not only serines and tyrosines but also threonines of the CTD can be phosphorylated with a number of functional consequences, including the interaction with yeast transcription termination factor, Rtt103p. Here, we report the solution structure of the Rtt103p CTD-interacting domain (CID) bound to Thr4 phosphorylated CTD, a poorly understood letter of the CTD code. The structure reveals a direct recognition of the phospho-Thr4 mark by Rtt103p CID and extensive interactions involving residues from three repeats of the CTD heptad. Intriguingly, Rtt103p's CID binds equally well Thr4 and Ser2 phosphorylated CTD A doubly phosphorylated CTD at Ser2 and Thr4 diminishes its binding affinity due to electrostatic repulsion. Our structural data suggest that the recruitment of a CID-containing CTD-binding factor may be coded by more than one letter of the CTD code.
[Mh] Termos MeSH primário: RNA Polimerase II/química
Proteínas de Saccharomyces cerevisiae/química
Treonina/química
Fatores de Transcrição/química
[Mh] Termos MeSH secundário: Fosforilação
Ligação Proteica
Proteínas Quinases/metabolismo
Estrutura Terciária de Proteína
Proteólise
RNA Polimerase II/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Serina/metabolismo
Treonina/metabolismo
Fatores de Transcrição/metabolismo
Transcrição Genética
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Rtt103 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 2ZD004190S (Threonine); 42HK56048U (Tyrosine); 452VLY9402 (Serine); EC 2.7.- (Protein Kinases); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.15252/embr.201643723


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[PMID]:29324779
[Au] Autor:Price MN; Zane GM; Kuehl JV; Melnyk RA; Wall JD; Deutschbauer AM; Arkin AP
[Ad] Endereço:Environmental Genomics & Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, California, United States of America.
[Ti] Título:Filling gaps in bacterial amino acid biosynthesis pathways with high-throughput genetics.
[So] Source:PLoS Genet;14(1):e1007147, 2018 01.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For many bacteria with sequenced genomes, we do not understand how they synthesize some amino acids. This makes it challenging to reconstruct their metabolism, and has led to speculation that bacteria might be cross-feeding amino acids. We studied heterotrophic bacteria from 10 different genera that grow without added amino acids even though an automated tool predicts that the bacteria have gaps in their amino acid synthesis pathways. Across these bacteria, there were 11 gaps in their amino acid biosynthesis pathways that we could not fill using current knowledge. Using genome-wide mutant fitness data, we identified novel enzymes that fill 9 of the 11 gaps and hence explain the biosynthesis of methionine, threonine, serine, or histidine by bacteria from six genera. We also found that the sulfate-reducing bacterium Desulfovibrio vulgaris synthesizes homocysteine (which is a precursor to methionine) by using DUF39, NIL/ferredoxin, and COG2122 proteins, and that homoserine is not an intermediate in this pathway. Our results suggest that most free-living bacteria can likely make all 20 amino acids and illustrate how high-throughput genetics can uncover previously-unknown amino acid biosynthesis genes.
[Mh] Termos MeSH primário: Aminoácidos/biossíntese
Aminoácidos/genética
Bactérias/genética
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Processos Heterotróficos
Sequenciamento de Nucleotídeos em Larga Escala/métodos
Histidina/biossíntese
Metionina/biossíntese
Análise de Sequência de DNA/métodos
Serina/biossíntese
Treonina/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Bacterial Proteins); 2ZD004190S (Threonine); 452VLY9402 (Serine); 4QD397987E (Histidine); AE28F7PNPL (Methionine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007147


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[PMID]:28988535
[Au] Autor:Malinovsky AV
[Ad] Endereço:Biofizpribor, Branch of Federal Medical-Biological Agency, St. Petersburg, 197183, Russia. info@biofizpribor.ru.
[Ti] Título:Reason for Indispensability of Threonine in Humans and Other Mammals in Comparative Aspect.
[So] Source:Biochemistry (Mosc);82(9):1055-1060, 2017 Sep.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The essential amino acid threonine is not synthesized in vertebrates, so it must be obtained from food. During evolution, the decomposition of threonine has changed. Because the decomposition of threonine catalyzed by threonine dehydratase is irreversible, in the present work attention is focused on threonine dehydrogenase to show the inability of this enzyme to synthesize threonine in a reaction that would be the reverse of the reaction of threonine decomposition. The reason why threonine dehydrogenase cannot be used for the biosynthesis of threonine in mammalian tissues is discussed. It is concluded that some quantity of threonine is involved in transamination.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/metabolismo
Aminoácidos Essenciais
Mamíferos/metabolismo
Treonina/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Amino Acids, Essential); 2ZD004190S (Threonine); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.103 (L-threonine 3-dehydrogenase)
[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:171010
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917090097


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[PMID]:28858528
[Au] Autor:Chen ES; Weng JH; Chen YH; Wang SC; Liu XX; Huang WC; Matsui T; Kawano Y; Liao JH; Lim LH; Bessho Y; Huang KF; Wu WJ; Tsai MD
[Ad] Endereço:Institute of Biological Chemistry, Academia Sinica , Taipei 115, Taiwan.
[Ti] Título:Phospho-Priming Confers Functionally Relevant Specificities for Rad53 Kinase Autophosphorylation.
[So] Source:Biochemistry;56(38):5112-5124, 2017 Sep 26.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The vast majority of in vitro structural and functional studies of the activation mechanism of protein kinases use the kinase domain alone. Well-demonstrated effects of regulatory domains or allosteric factors are scarce for serine/threonine kinases. Here we use a site-specifically phosphorylated SCD1-FHA1-kinase three-domain construct of the serine/threonine kinase Rad53 to show the effect of phospho-priming, an in vivo regulatory mechanism, on the autophosphorylation intermediate and specificity. Unphosphorylated Rad53 is a flexible monomer in solution but is captured in an asymmetric enzyme:substrate complex in crystal with the two FHA domains separated from each other. Phospho-priming induces formation of a stable dimer via intermolecular pT-FHA binding in solution. Importantly, autophosphorylation of unprimed and phospho-primed Rad53 produced predominantly inactive pS350-Rad53 and active pT354-Rad53, respectively. The latter mechanism was also demonstrated in vivo. Our results show that, while Rad53 can display active conformations under various conditions, simulation of in vivo regulatory conditions confers functionally relevant autophosphorylation.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/química
Proteínas de Ciclo Celular/metabolismo
Quinase do Ponto de Checagem 2/química
Quinase do Ponto de Checagem 2/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Ciclo Celular/genética
Quinase do Ponto de Checagem 2/genética
Dano ao DNA
Modelos Moleculares
Ressonância Magnética Nuclear Biomolecular
Fosforilação
Fosfotreonina/metabolismo
Domínios Proteicos
Multimerização Proteica
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Espalhamento a Baixo Ângulo
Serina/química
Treonina/química
Treonina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Saccharomyces cerevisiae Proteins); 1114-81-4 (Phosphothreonine); 2ZD004190S (Threonine); 452VLY9402 (Serine); EC 2.7.1.- (DUN1 protein, S cerevisiae); EC 2.7.1.11 (Checkpoint Kinase 2); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.12.1 (RAD53 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00689


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[PMID]:28820083
[Au] Autor:Dong YW; Jiang WD; Liu Y; Wu P; Jiang J; Kuang SY; Tang L; Tang WN; Zhang YA; Zhou XQ; Feng L
[Ad] Endereço:1Animal Nutrition Institute,Sichuan Agricultural University,Chengdu 611130,People's Republic of China.
[Ti] Título:Threonine deficiency decreased intestinal immunity and aggravated inflammation associated with NF-κB and target of rapamycin signalling pathways in juvenile grass carp (Ctenopharyngodon idella) after infection with Aeromonas hydrophila.
[So] Source:Br J Nutr;118(2):92-108, 2017 Jul.
[Is] ISSN:1475-2662
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:This study aimed to investigate the impacts of dietary threonine on intestinal immunity and inflammation in juvenile grass carp. Six iso-nitrogenous semi-purified diets containing graded levels of threonine (3·99-21·66 g threonine/kg) were formulated and fed to fishes for 8 weeks, and then challenged with Aeromonas hydrophila for 14 d. Results showed that, compared with optimum threonine supplementation, threonine deficiency (1) decreased the ability of fish against enteritis, intestinal lysozyme activities (except in the distal intestine), acid phosphatase activities, complement 3 (C3) and C4 contents and IgM contents (except in the proximal intestine (PI)), and it down-regulated the transcript abundances of liver-expressed antimicrobial peptide (LEAP)-2A, LEAP-2B, hepcidin, IgZ, IgM and ß-defensin1 (except in the PI) (P<0·05); (2) could up-regulate intestinal pro-inflammatory cytokines TNF-α, IL-1ß, IL-6, IL-8 and IL-17D mRNA levels partly related to NF-κB signalling; (3) could down-regulate intestinal anti-inflammatory cytokine transforming growth factor (TGF)-ß1, TGF-ß2, IL-4/13A (not IL-4/13B) and IL-10 mRNA levels partly by target of rapamycin signalling. Finally, on the basis of the specific growth rate, against the enteritis morbidity and IgM contents, the optimum threonine requirements were estimated to be 14·53 g threonine/kg diet (4·48 g threonine/100 g protein), 15.05 g threonine/kg diet (4·64 g threonine/100 g protein) and 15·17 g threonine/kg diet (4·68 g threonine/100 g protein), respectively.
[Mh] Termos MeSH primário: Carpas/microbiologia
Doenças dos Peixes/microbiologia
Infecções por Bactérias Gram-Negativas/veterinária
Intestinos/imunologia
Serina-Treonina Quinases TOR/metabolismo
Treonina/deficiência
[Mh] Termos MeSH secundário: Aeromonas hydrophila
Animais
Peptídeos Catiônicos Antimicrobianos/genética
Proteínas Sanguíneas
Carpas/imunologia
Citocinas/genética
Citocinas/metabolismo
Dieta/veterinária
Regulação para Baixo/efeitos dos fármacos
Enterite/veterinária
Doenças dos Peixes/imunologia
Proteínas de Peixes/genética
Hepcidinas
Imunoglobulina M
Intestinos/enzimologia
Muramidase/metabolismo
NF-kappa B/metabolismo
Transdução de Sinais/fisiologia
Treonina/administração & dosagem
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Blood Proteins); 0 (Cytokines); 0 (Fish Proteins); 0 (Hepcidins); 0 (Immunoglobulin M); 0 (NF-kappa B); 0 (liver-expressed antimicrobial peptide 2, human); 2ZD004190S (Threonine); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 3.2.1.17 (Muramidase)
[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:170819
[St] Status:MEDLINE
[do] DOI:10.1017/S0007114517001830


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[PMID]:28772192
[Au] Autor:Sica VP; Rees ER; Raja HA; Rivera-Chávez J; Burdette JE; Pearce CJ; Oberlies NH
[Ad] Endereço:Department of Chemistry and Biochemistry, University of North Carolina at Greensboro, Greensboro, NC 27402, United States.
[Ti] Título:In situ mass spectrometry monitoring of fungal cultures led to the identification of four peptaibols with a rare threonine residue.
[So] Source:Phytochemistry;143:45-53, 2017 Nov.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Peptaibols are an intriguing class of fungal metabolites due both to their wide range of reported bioactivities and to the structural variability that can be generated by the exchange of variable amino acid building blocks. In an effort to streamline the discovery of structurally diverse peptaibols, a mass spectrometry surface sampling technique was applied to screen the chemistry of fungal cultures in situ. Four previously undescribed peptaibols, all containing a rare threonine residue, were identified from a fungal culture (MSX53554), which was identified as Nectriopsis Maire (Bionectriaceae, Hypocreales, Ascomycota). These compounds not only increased the known threonine-containing peptaibols by nearly 20%, but also, the threonine residue was situated in a unique place compared to the other reported threonine-containing peptaibols. After the initial in situ detection and characterization, a large-scale solid fermentation culture was grown. The four peptaibols were isolated and characterized by mass spectrometry. In addition, one of the peptaibols was fully characterized by NMR and amino acid analysis using Marfey's reagent and exhibited moderate in vitro anticancer activity.
[Mh] Termos MeSH primário: Hypocreales/química
Peptaibols/química
Peptaibols/isolamento & purificação
Treonina/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aminoácidos/metabolismo
Antibacterianos/química
Estrutura Molecular
Ressonância Magnética Nuclear Biomolecular
Trichoderma/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Anti-Bacterial Agents); 0 (Peptaibols); 2ZD004190S (Threonine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE


  10 / 8984 MEDLINE  
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[PMID]:28738503
[Au] Autor:Gajaria TK; Suthar P; Baghel RS; Balar NB; Sharnagat P; Mantri VA; Reddy CRK
[Ad] Endereço:Division of Marine Biotechnology and Ecology, CSIR-Central Salt and Marine Chemicals Research Institute, Bhavnagar 364002, India; Academy of Scientific and Innovative Research (AcSIR), New Delhi, India.
[Ti] Título:Integration of protein extraction with a stream of byproducts from marine macroalgae: A model forms the basis for marine bioeconomy.
[So] Source:Bioresour Technol;243:867-873, 2017 Nov.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The present study describes an advanced biorefinery model for marine macroalgae that assumes significant importance in the context of marine bio-economy. The method investigated in this study integrates the extraction of crude proteins with recovery of minerals rich sap, lipids, ulvan and cellulose from fresh biomass of Ulva lactuca. The protein content extracted was 11±2.12% on dry weight basis with recovery efficiency of 68.75±4.01%. The amino acid composition of crude protein fraction showed iso-leucine as the most abundant amino acid with 16.51±0.03% followed by histidine, arginine, tyrosine, serine, aspartic acid, threonine, phenyl alanine, leucine, alanine, lysine, glycine and glutamic acid (0.22±0.24%). The digestibility of protein was as high as 85.86±5.92% indicating its suitability for use in food supplements. The protein production with co-recovery of other products would not only result in effective utilisation marine macroalgal resources but also forms the basis for marine bio-economy.
[Mh] Termos MeSH primário: Microalgas
Proteínas/isolamento & purificação
[Mh] Termos MeSH secundário: Aminoácidos
Glutamatos
Alga Marinha
Treonina
Valina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Glutamates); 0 (Proteins); 2ZD004190S (Threonine); HG18B9YRS7 (Valine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE



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