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[PMID]:29353723
[Au] Autor:Wu YZ; Zhang HW; Sun ZH; Dai JG; Hu YC; Li R; Lin PC; Xia GY; Wang LY; Qiu BL; Zhang JF; Ge GB; Lin S
[Ad] Endereço:State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China.
[Ti] Título:Bysspectin A, an unusual octaketide dimer and the precursor derivatives from the endophytic fungus Byssochlamys spectabilis IMM0002 and their biological activities.
[So] Source:Eur J Med Chem;145:717-725, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Bysspectin A (1), a polyketide-derived octaketide dimer with a novel carbon skeleton, and two new precursor derivatives, bysspectins B and C (2 and 3), were obtained from an organic extract of the endophytic fungus Byssochlamys spectabilis that had been isolated from a leaf tissue of the traditional Chinese medicinal plant Edgeworthia chrysantha, together with a known octaketide, paecilocin A (4). Their structures were determined by HRMS, 1D and 2D NMR spectroscopic analysis. A plausible route for their biosynthetic pathway is proposed. Compounds 1-3 were tested for their antimicrobial activities. Only compound 3 was weakly active against Escherichia coli and Staphyloccocus aureus with MIC values of 32 and 64 µg/mL, respectively. Further, the inhibitory effects on human carboxylesterases (hCE1, hCE2) of compounds 1 and 4 were evaluated. The results demonstrated that bysspectin A (1) was a novel and highly selective inhibitor against hCE2 with the IC value of 2.01 µM. Docking simulation also demonstrated that active compound 1 created interaction with the Ser-288 (the catalytic amino-acid in the catalytic cavity) of hCE2 via hydrogen bonding, revealing its highly selective inhibition toward hCE2.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Byssochlamys/química
Carboxilesterase/antagonistas & inibidores
Hidrolases de Éster Carboxílico/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Escherichia coli/efeitos dos fármacos
Policetídeos/farmacologia
Staphylococcus aureus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Antibacterianos/química
Antibacterianos/isolamento & purificação
Biocatálise
Carboxilesterase/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Dimerização
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/química
Inibidores Enzimáticos/isolamento & purificação
Seres Humanos
Testes de Sensibilidade Microbiana
Simulação de Acoplamento Molecular
Estrutura Molecular
Policetídeos/química
Policetídeos/isolamento & purificação
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Enzyme Inhibitors); 0 (Polyketides); 0 (bysspectin A); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.1 (CES1 protein, human); EC 3.1.1.1 (CES2 protein, human); EC 3.1.1.1 (Carboxylesterase)
[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:180123
[St] Status:MEDLINE


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[PMID]:29264996
[Au] Autor:Chen F; Zhang B; Parker RB; Laizure SC
[Ad] Endereço:a Department of Clinical Pharmacy , College of Pharmacy, University of Tennessee Health Science Center , Memphis , TN , USA.
[Ti] Título:Clinical implications of genetic variation in carboxylesterase drug metabolism.
[So] Source:Expert Opin Drug Metab Toxicol;14(2):131-142, 2018 Feb.
[Is] ISSN:1744-7607
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Mammalian carboxylesterase enzymes are a highly conserved metabolic pathway involved in the metabolism of endogenous and exogenous compounds including many widely prescribed therapeutic agents. Recent advances in our understanding of genetic polymorphisms affecting enzyme activity have exposed potential therapeutic implications. Areas covered: The aims of this review are to provide an overview of carboxylesterase 1 (CES1) and carboxylesterase 2 (CES2) gene structure, to summarize the known polymorphism affecting substrate-drug metabolism, and to assess the potential therapeutic implications of genetic variations affecting enzyme function. Expert opinion: Genetic variability in carboxylesterase drug metabolism is a nascent area of research with only a handful of the thousands of SNPs investigated for their potential effects of enzyme activity or carboxylesterase-substrate disposition and therapeutics. It remains to be determined if the wide variability in enzyme activity can be explained by genetic variation, and used in personalized medicine to improve clinical outcomes.
[Mh] Termos MeSH primário: Carboxilesterase/genética
Hidrolases de Éster Carboxílico/genética
Preparações Farmacêuticas/metabolismo
[Mh] Termos MeSH secundário: Carboxilesterase/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Variação Genética
Seres Humanos
Preparações Farmacêuticas/administração & dosagem
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Pharmaceutical Preparations); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.1 (CES1 protein, human); EC 3.1.1.1 (CES2 protein, human); EC 3.1.1.1 (Carboxylesterase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1080/17425255.2018.1420164


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[PMID]:29337064
[Au] Autor:Knollenberg BJ; Liu J; Yu S; Lin H; Tian L
[Ad] Endereço:Department of Plant Sciences, University of California, Davis, CA, 95616, USA; The Huck Institutes of the Life Sciences, Pennsylvania State University, State College, PA, 16801, USA.
[Ti] Título:Cloning and functional characterization of a p-coumaroyl quinate/shikimate 3'-hydroxylase from potato (Solanum tuberosum).
[So] Source:Biochem Biophys Res Commun;496(2):462-467, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chlorogenic acid (CGA) plays an important role in protecting plants against pathogens and promoting human health. Although CGA accumulates to high levels in potato tubers, the key enzyme p-coumaroyl quinate/shikimate 3'-hydroxylase (C3'H) for CGA biosynthesis has not been isolated and functionally characterized in potato. In this work, we cloned StC3'H from potato and showed that it catalyzed the formation of caffeoylshikimate and CGA (caffeoylquinate) from p-coumaroyl shikimate and p-coumaroyl quinate, respectively, but was inactive towards p-coumaric acid in in vitro enzyme assays. When the expression of StC3'H proteins was blocked through antisense (AS) inhibition under the control of a tuber-specific patatin promoter, moderate changes in tuber yield as well as phenolic metabolites in the core tuber tissue were observed for several AS lines. On the other hand, the AS and control potato lines exhibited similar responses to a bacterial pathogen Pectobacterium carotovorum. These results suggest that StC3'H is implicated in phenolic metabolism in potato. They also suggest that CGA accumulation in the core tissue of potato tubers is an intricately controlled process and that additional C3'H activity may also be involved in CGA biosynthesis in potato.
[Mh] Termos MeSH primário: Ácido Clorogênico/metabolismo
Oxigenases de Função Mista/genética
Proteínas de Plantas/genética
Tubérculos/enzimologia
Solanum tuberosum/enzimologia
[Mh] Termos MeSH secundário: Hidrolases de Éster Carboxílico/genética
Hidrolases de Éster Carboxílico/metabolismo
Ácido Clorogênico/análogos & derivados
Clonagem Molecular
Expressão Gênica
Oxigenases de Função Mista/antagonistas & inibidores
Oxigenases de Função Mista/metabolismo
Oligonucleotídeos Antissenso/genética
Oligonucleotídeos Antissenso/metabolismo
Pectobacterium carotovorum/patogenicidade
Pectobacterium carotovorum/fisiologia
Pichia/genética
Pichia/metabolismo
Proteínas de Plantas/metabolismo
Tubérculos/genética
Tubérculos/microbiologia
Plantas Geneticamente Modificadas
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ácido Chiquímico/análogos & derivados
Ácido Chiquímico/metabolismo
Solanum tuberosum/genética
Solanum tuberosum/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (4-coumaroylshikimic acid); 0 (Oligonucleotides, Antisense); 0 (Plant Proteins); 0 (Recombinant Proteins); 0 (patatin protein, Solanum tuberosum); 29MS2WI2NU (Shikimic Acid); 318ADP12RI (Chlorogenic Acid); 73263-62-4 (5-O-caffeoylshikimic acid); E57A0DKE0B (3,4-di-O-caffeoylquinic acid); EC 1.- (Mixed Function Oxygenases); EC 1.14.13.- (5-O-(4-coumaroyl)shikimate 3'-hydroxylase); EC 3.1.1.- (Carboxylic Ester Hydrolases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE


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[PMID]:29307824
[Au] Autor:Yan J; He H; Fang L; Zhang A
[Ad] Endereço:National Key Laboratory of Crop Genetics and Germplasm Enhancement, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China; College of Life Sciences, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China.
[Ti] Título:Pectin methylesterase31 positively regulates salt stress tolerance in Arabidopsis.
[So] Source:Biochem Biophys Res Commun;496(2):497-501, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The alteration of cell wall component and structure is an important adaption to saline environment. Pectins, a major cell wall component, are often present in a highly methylesterified form. The level of methyl esterification determined by pectin methylesterases (PMEs) influences many important wall properties that are believed to relate to the adaption to saline stress. However, little is known about the function of PMEs in response to salt stress. Here, we established a link between pectin methylesterase31 (PME31) and salt stress tolerance. Salt stress significantly increases PME31 expression. PME31 is located in the plasma membrane and the expression level of PME31 was high in dry seeds. Knock-down mutants in PME31 conferred hypersensitive phenotypes to salt stress in seed germination and post-germination growth. Real-time PCR analysis revealed that the transcript levels of several stress genes (DREB2A, RD29A and RD29B) are lower in pme31-2 mutant than that in the wild type in response to salt stress. These results suggested that PME31 could positively modulate salt stress tolerance.
[Mh] Termos MeSH primário: Arabidopsis/efeitos dos fármacos
Hidrolases de Éster Carboxílico/genética
Regulação da Expressão Gênica de Plantas
Células Vegetais/efeitos dos fármacos
Cloreto de Sódio/farmacologia
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Parede Celular/efeitos dos fármacos
Parede Celular/metabolismo
Proteínas e Peptídeos de Choque Frio/genética
Proteínas e Peptídeos de Choque Frio/metabolismo
Germinação/efeitos dos fármacos
Isoenzimas/genética
Isoenzimas/metabolismo
Mutação
Células Vegetais/metabolismo
Salinidade
Tolerância a Sal
Sementes/efeitos dos fármacos
Sementes/genética
Sementes/metabolismo
Estresse Fisiológico
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Cold Shock Proteins and Peptides); 0 (DREB2A protein, Arabidopsis); 0 (Isoenzymes); 0 (RD29B protein, Arabidopsis); 0 (RD29a protein, Arabidopsis); 0 (Transcription Factors); 451W47IQ8X (Sodium Chloride); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.11 (pectinesterase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:29208413
[Au] Autor:Kaur G; Sharma A; Narang T; Dogra S; Kaur J
[Ad] Endereço:Department of Biotechnology, BMS Block-1, South Campus, Panjab University, Chandigarh, 160014, India.
[Ti] Título:Characterization of ML0314c of Mycobacterium leprae and deciphering its role in the immune response in leprosy patients.
[So] Source:Gene;643:26-34, 2018 Feb 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mycobacterium leprae has a reduced genome size due to the reductive evolution over a long period of time. Lipid metabolism plays an important role in the life cycle and pathogenesis of this bacterium. In comparison to 26 lip genes (Lip A-Z) of M. tuberculosis, M. leprae retained only three orthologs indicating their importance in its life cycle. ML0314c (LipU) is one of them. It is conserved throughout the mycobacterium species. Bioinformatics analysis showed the presence of an α/ß hydrolase fold and 'GXSXG' characteristic of the esterases/lipases. The gene was expressed in E. coli and purified to homogeneity. It showed preference towards short chain esters with pNP-acetate as the preferred substrate. The enzyme showed optimal activity at 45°C and pH8.0. ML0314c protein was stable between temperatures ranging from 20 to 60°C and pH5.0-8.0, i.e., relatively acidic and neutral conditions. The active site residues predicted bioinformatically were confirmed to be Ser168, Glu267, and His297 by site directed mutagenesis. E-serine, DEPC and Tetrahydrolipstatin (THL) completely inhibited the activity of ML0314c. The protein was localized in cell wall and extracellular medium. Several antigenic epitopes were predicted in ML0314c. Protein elicited strong humoral immune response in leprosy patients, whereas, a reduced immune response was observed in the relapsed cases. No humoral response was observed in treatment completed patients. Overexpression of ml0314c in the surrogate host M. smegmatis showed marked difference in the colony morphology and growth rate. In conclusion, ML0314c is a secretary carboxyl esterase that could modulate the immune response in leprosy patients.
[Mh] Termos MeSH primário: Lipólise/genética
Mycobacterium leprae/genética
Mycobacterium leprae/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Domínio Catalítico/genética
Clonagem Molecular/métodos
Escherichia coli/genética
Seres Humanos
Concentração de Íons de Hidrogênio
Hanseníase/metabolismo
Hanseníase/microbiologia
Lipase/genética
Metabolismo dos Lipídeos/genética
Lipídeos
Mutagênese Sítio-Dirigida/métodos
Mycobacterium tuberculosis/genética
Especificidade por Substrato/genética
Fatores de Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Lipids); 0 (Virulence Factors); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.- (LipY protein, Mycobacterium tuberculosis); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180123
[Lr] Data última revisão:
180123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


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[PMID]:29236388
[Au] Autor:Minchenko OH; Garmash IA; Minchenko DO; Kuznetsova AY; Ratushna OO
[Ti] Título:Inhibition of IRE1 modifies hypoxic regulation of G6PD, GPI, TKT, TALDO1, PGLS and RPIA genes expression in U87 glioma cells.
[So] Source:Ukr Biochem J;89(1):38-49, 2017 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:We have studied the effect of hypoxia on the expression level of mRNA of the basic enzymes of pentose-phosphate cycle (G6PD, TKT, TALDO1, PGLS and RPIA) and glucose-6-phosphate isomerase (GPI) in U87 glioma cells in relation to inhibition of IRE1 (inositol requiring enzyme 1). It was shown that hypoxia leads to up-regulation of the expression of GPI and PGLS genes and to down-regulation of TALDO1 and RPIA genes in control glioma cells. Changes for GPI gene were more significant than for other genes. At the same time, inhibition of IRE1 modified the effect of hypoxia on the expression of all studied genes. In particular, it increased sensitivity to hypoxia of G6PD and TKT genes expression and suppressed the effect of hypoxia on the expression of GPI and RPIA genes. Additionally, inhibition of IRE1 eliminated hypoxic regulation of PGLS gene and did not change significantly effect of hypoxia on the expression of TALDO1 gene in glioma cells. Present study demonstrated that hypoxia, which often contributes to tumor growth, affects the expression of most studied genes and inhibition of IRE1 modified the hypoxic regulation of pentose-phosphate cycle gene expressions in a gene specific manner and thus possibly contributes to slower glioma growth, but several aspects of this regulation warrant further investigation.
[Mh] Termos MeSH primário: Estresse do Retículo Endoplasmático/genética
Endorribonucleases/genética
Regulação Neoplásica da Expressão Gênica
Neuroglia/metabolismo
Via de Pentose Fosfato/genética
Proteínas Serina-Treonina Quinases/genética
[Mh] Termos MeSH secundário: Aldose-Cetose Isomerases/genética
Aldose-Cetose Isomerases/metabolismo
Hidrolases de Éster Carboxílico/genética
Hidrolases de Éster Carboxílico/metabolismo
Hipóxia Celular
Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Endorribonucleases/deficiência
Técnicas de Silenciamento de Genes
Glucose-6-Fosfato Isomerase/genética
Glucose-6-Fosfato Isomerase/metabolismo
Glucosefosfato Desidrogenase/genética
Glucosefosfato Desidrogenase/metabolismo
Seres Humanos
Neuroglia/patologia
Proteínas Serina-Treonina Quinases/deficiência
Transdução de Sinais
Transaldolase/genética
Transaldolase/metabolismo
Transcetolase/genética
Transcetolase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.1.1.49 (Glucosephosphate Dehydrogenase); EC 2.2.1.1 (Transketolase); EC 2.2.1.2 (Transaldolase); EC 2.7.11.1 (ERN1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.1.- (Endoribonucleases); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.31 (6-phosphogluconolactonase); EC 5.3.1.- (Aldose-Ketose Isomerases); EC 5.3.1.6 (ribosephosphate isomerase); EC 5.3.1.9 (Glucose-6-Phosphate Isomerase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj89.01.038


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[PMID]:29236376
[Au] Autor:Ellidag HY; Eren E; Akdag M; Giray O; Kiraz K; Yilmaz N
[Ti] Título:The relationship between serum ferritin levels and serum lipids and HDL function with respect to age and gender.
[So] Source:Ukr Biochem J;88(6):76-86, 2016 Nov-Dec.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Elevated serum ferritin (SFer) levels have been associated with chronic diseases such as coronary heart disease and diabetes mellitus type 2. The aim of this study was to examine the relationship between SFer levels and serum lipid parameters, and how this relation changes in terms of age and gender. Additionally, we investigated a possible relationship between SFer levels and high-density lipoprotein (HDL) function. SFer levels and lipid panel (total cholesterol (TC), triglyceride (TG), low-density lipoprotein-cholesterol (LDL-C) and HDL-C) of 4205 people (3139 women, 1066 men) were examined retrospectively. Study population was classified according to age and gender. Separately, 100 subjects (52 women, 48 men) were randomly recruited to investigate the relation between SFer levels, and HDL dependent paraoxonase-1 (PON1) and arylesterase (ARE) activities. In all age groups, women's SFer levels were found to be significantly lower and HDL-C levels significantly higher compared to men. In the 50-70 ages range, TC and LDL-C levels of women were found to be significantly higher than those of men (P < 0.01). SFer levels tended to increase with age in women. Correlation analyses revealed a negative correlation between levels of SFer and HDL-C, while positive correlations existed between levels of SFer, and TC, TG and LDL-C. There was no significant correlation between SFer levels and PON1 or ARE activities. The finding that increased SFer levels are accompanied by increased serum TC, TG and LDL-C levels may help us to explain the increased risk of metabolic disorders and cardiovascular disease in postmenopausal women.
[Mh] Termos MeSH primário: HDL-Colesterol/sangue
LDL-Colesterol/sangue
Ferritinas/sangue
Triglicerídeos/sangue
[Mh] Termos MeSH secundário: Adulto
Fatores Etários
Idoso
Arildialquilfosfatase/sangue
Arildialquilfosfatase/genética
Hidrolases de Éster Carboxílico/sangue
Hidrolases de Éster Carboxílico/genética
Feminino
Ferritinas/genética
Expressão Gênica
Seres Humanos
Masculino
Meia-Idade
Fatores Sexuais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholesterol, HDL); 0 (Cholesterol, LDL); 0 (Triglycerides); 9007-73-2 (Ferritins); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.2 (arylesterase); EC 3.1.8.1 (Aryldialkylphosphatase); EC 3.1.8.1 (PON1 protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.06.076


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[PMID]:29253879
[Au] Autor:Chen J; Liu X; Li F; Li Y; Yuan D
[Ad] Endereço:Hainan Key Laboratory of Banana Genetic Improvement, Haikou Experimental Station, Chinese Academy of Tropical Agricultural Sciences, Haikou, China.
[Ti] Título:Cold shock treatment extends shelf life of naturally ripened or ethylene-ripened avocado fruits.
[So] Source:PLoS One;12(12):e0189991, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Avocado is an important tropical fruit with high commercial value, but has a relatively short storage life. In this study, the effects of cold shock treatment (CST) on shelf life of naturally ripened and ethylene-ripened avocado fruits were investigated. Fruits were immersed in ice water for 30 min, then subjected to natural or ethylene-induced ripening. Fruit color; firmness; respiration rate; ethylene production; and the activities of polygalacturonase (PG), pectin methylesterase (PME), and endo-ß-1,4-glucanase were measured. Immersion in ice water for 30 min effectively delayed ripening-associated processes, including peel discoloration, pulp softening, respiration rate, and ethylene production during shelf life. The delay in fruit softening by CST was associated with decreased PG and endo-ß-1,4-glucanase activities, but not PME activity. This method could potentially be a useful postharvest technology to extend shelf life of avocado fruits.
[Mh] Termos MeSH primário: Temperatura Baixa
Etilenos/farmacologia
Frutas
Persea
[Mh] Termos MeSH secundário: Hidrolases de Éster Carboxílico/química
Parede Celular
Celulase/química
Pectinas/química
Poligalacturonase/química
Fatores de Tempo
Água
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ethylenes); 0 (Pectins); 059QF0KO0R (Water); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.11 (pectinesterase); EC 3.2.1.15 (Polygalacturonase); EC 3.2.1.4 (Cellulase); EC 3.2.1.4 (endoglucanase EGL1)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189991


  9 / 7605 MEDLINE  
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[PMID]:29205472
[Au] Autor:Maas RR; Iwanicka-Pronicka K; Kalkan Ucar S; Alhaddad B; AlSayed M; Al-Owain MA; Al-Zaidan HI; Balasubramaniam S; Baric I; Bubshait DK; Burlina A; Christodoulou J; Chung WK; Colombo R; Darin N; Freisinger P; Garcia Silva MT; Grunewald S; Haack TB; van Hasselt PM; Hikmat O; Hörster F; Isohanni P; Ramzan K; Kovacs-Nagy R; Krumina Z; Martin-Hernandez E; Mayr JA; McClean P; De Meirleir L; Naess K; Ngu LH; Pajdowska M; Rahman S; Riordan G; Riley L; Roeben B; Rutsch F; Santer R; Schiff M; Seders M; Sequeira S; Sperl W; Staufner C; Synofzik M; Taylor RW; Trubicka J; Tsiakas K; Unal O; Wassmer E
[Ad] Endereço:Translational Metabolic Laboratory, Department of Laboratory Medicine, Radboud University Medical Center, Nijmegen, the Netherlands.
[Ti] Título:Progressive deafness-dystonia due to SERAC1 mutations: A study of 67 cases.
[So] Source:Ann Neurol;82(6):1004-1015, 2017 Dec.
[Is] ISSN:1531-8249
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: 3-Methylglutaconic aciduria, dystonia-deafness, hepatopathy, encephalopathy, Leigh-like syndrome (MEGDHEL) syndrome is caused by biallelic variants in SERAC1. METHODS: This multicenter study addressed the course of disease for each organ system. Metabolic, neuroradiological, and genetic findings are reported. RESULTS: Sixty-seven individuals (39 previously unreported) from 59 families were included (age range = 5 days-33.4 years, median age = 9 years). A total of 41 different SERAC1 variants were identified, including 20 that have not been reported before. With the exception of 2 families with a milder phenotype, all affected individuals showed a strikingly homogeneous phenotype and time course. Severe, reversible neonatal liver dysfunction and hypoglycemia were seen in >40% of all cases. Starting at a median age of 6 months, muscular hypotonia (91%) was seen, followed by progressive spasticity (82%, median onset = 15 months) and dystonia (82%, 18 months). The majority of affected individuals never learned to walk (68%). Seventy-nine percent suffered hearing loss, 58% never learned to speak, and nearly all had significant intellectual disability (88%). Magnetic resonance imaging features were accordingly homogenous, with bilateral basal ganglia involvement (98%); the characteristic "putaminal eye" was seen in 53%. The urinary marker 3-methylglutaconic aciduria was present in virtually all patients (98%). Supportive treatment focused on spasticity and drooling, and was effective in the individuals treated; hearing aids or cochlear implants did not improve communication skills. INTERPRETATION: MEGDHEL syndrome is a progressive deafness-dystonia syndrome with frequent and reversible neonatal liver involvement and a strikingly homogenous course of disease. Ann Neurol 2017;82:1004-1015.
[Mh] Termos MeSH primário: Hidrolases de Éster Carboxílico/genética
Transtornos da Surdocegueira/diagnóstico por imagem
Transtornos da Surdocegueira/genética
Progressão da Doença
Distonia/diagnóstico por imagem
Distonia/genética
Deficiência Intelectual/diagnóstico por imagem
Deficiência Intelectual/genética
Mutação/genética
Atrofia Óptica/diagnóstico por imagem
Atrofia Óptica/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Sequência de Aminoácidos
Criança
Pré-Escolar
Estudos de Coortes
Transtornos da Surdocegueira/terapia
Distonia/terapia
Feminino
Seres Humanos
Lactente
Recém-Nascido
Deficiência Intelectual/terapia
Masculino
Atrofia Óptica/terapia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; MULTICENTER STUDY
[Nm] Nome de substância:
EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.- (SERAC1 protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180101
[Lr] Data última revisão:
180101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1002/ana.25110


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[PMID]:28967962
[Au] Autor:Singh MK; Shivakumaraswamy S; Gummadi SN; Manoj N
[Ad] Endereço:Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences Indian Institute of Technology Madras, Chennai 600036, India.
[Ti] Título:Role of an N-terminal extension in stability and catalytic activity of a hyperthermostable α/ß hydrolase fold esterase.
[So] Source:Protein Eng Des Sel;30(8):559-570, 2017 Aug 01.
[Is] ISSN:1741-0134
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The carbohydrate esterase family 7 (CE7) enzymes catalyze the deacetylation of acetyl esters of a broad range of alcohols and is unique in its activity towards cephalosporin C. The CE7 fold contains a conserved N-terminal extension that distinguishes it from the canonical α/ß hydrolase fold. The hexameric quaternary structure indicates that the N-terminus may affect activity and specificity by controlling access of substrates to the buried active sites via an entrance tunnel. In this context, we characterized the catalytic parameters, conformation and thermal stability of two truncation variants lacking four and ten residues of the N-terminal region of the hyperthermostable Thermotoga maritima CE7 acetyl esterase (TmAcE). The truncations did not affect the secondary structure or the fold but modulated the oligomerization dynamics. A modest increase was observed in substrate specificity for acetylated xylose compared with acetylated glucose. A drastic reduction of ~30-40°C in the optimum temperature for activity of the variants indicated lower thermal stability. The loss of hyperthermostability appears to be an indirect effect associated with an increase in the conformational flexibility of an otherwise rigid neighboring loop containing a catalytic triad residue. The results suggest that the N-terminal extension was evolutionarily selected to preserve the stability of the enzyme.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Hidrolases de Éster Carboxílico/química
Proteínas Recombinantes de Fusão/química
[Mh] Termos MeSH secundário: Acetilação
Bactérias/enzimologia
Bactérias/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Hidrolases de Éster Carboxílico/genética
Hidrolases de Éster Carboxílico/metabolismo
Estabilidade Enzimática
Escherichia coli/genética
Temperatura Alta
Concentração de Íons de Hidrogênio
Modelos Moleculares
Maleabilidade
Desdobramento de Proteína
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Fusion Proteins); EC 3.1.1.- (Carboxylic Ester Hydrolases)
[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:171003
[St] Status:MEDLINE
[do] DOI:10.1093/protein/gzx049



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