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[PMID]:29017767
[Au] Autor:Kwak MK; Ku M; Kang SO
[Ad] Endereço:Laboratory of Biophysics, School of Biological Sciences, Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea. Electronic address: genie6@snu.ac.kr.
[Ti] Título:Inducible NAD(H)-linked methylglyoxal oxidoreductase regulates cellular methylglyoxal and pyruvate through enhanced activities of alcohol dehydrogenase and methylglyoxal-oxidizing enzymes in glutathione-depleted Candida albicans.
[So] Source:Biochim Biophys Acta;1862(1):18-39, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: High methylglyoxal content disrupts cell physiology, but mammals have scavengers to prevent glycolytic and mitochondrial dysfunctions. In yeast, methylglyoxal accumulation triggers methylglyoxal-oxidizing alcohol dehydrogenase (Adh1) activity. While methylglyoxal reductases and glyoxalases have been well studied in prokaryotes and eukaryotes, experimental evidence for methylglyoxal dehydrogenase (Mgd) and other catalytic activities of this enzyme affecting glycolysis and the tricarboxylic acid cycle is lacking. METHODS: A glycine-rich cytoplasmic Mgd protein, designated as Mgd1/Grp2, was isolated from glutathione-depleted Candida albicans. The effects of Mgd1/Grp2 activities on metabolic pathophysiology were investigated using knockout and overexpression mutants. We measured glutathione-(in)dependent metabolite contents and metabolic effects, including viability, oxygen consumption, ADH1 transcripts, and glutathione reductase and α-ketoglutarate dehydrogenase activities in the mutants. Based on the findings, methylglyoxal-oxidizing proteins were monitored to determine effects of MGD1/GRP2 disruption on methylglyoxal-scavenging traits during glutathione deprivation. RESULTS: Methylglyoxal-oxidizing NAD(H)-linked Mgd1/Grp2 was found solely in glutathione auxotrophs, and it catalyzed the reduction of both methylglyoxal and pyruvate. MGD1/GRP2 disruptants showed growth defects, cell-cycle arrest, and methylglyoxal and pyruvate accumulation with mitochondrial impairment, regardless of ADH1 compensation. Other methylglyoxal-oxidizing enzymes were identified as key glycolytic enzymes with enhanced activity and transcription in MGD1/GRP2 disruptants, irrespective of glutathione content. CONCLUSIONS: Failure of methylglyoxal and pyruvate dissimilation by Mgd1/Grp2 deficiency leads to poor glutathione-dependent redox regulation despite compensation by Adh1. GENERAL SIGNIFICANCE: This is the first report that multifunctional Mgd activities contribute to scavenging methylglyoxal and pyruvate to maintain metabolic homeostasis and the redox pool via glycolytic enzymes and Adh1 expression.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Oxirredutases do Álcool/metabolismo
Candida albicans/metabolismo
Proteínas Fúngicas/metabolismo
Glutationa/metabolismo
Aldeído Pirúvico/metabolismo
Ácido Pirúvico/metabolismo
[Mh] Termos MeSH secundário: Álcool Desidrogenase/genética
Oxirredutases do Álcool/genética
Candida albicans/genética
Proteínas Fúngicas/genética
Glutationa/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fungal Proteins); 722KLD7415 (Pyruvaldehyde); 8558G7RUTR (Pyruvic Acid); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.1.3.- (glyoxal oxidase); GAN16C9B8O (Glutathione)
[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:171012
[St] Status:MEDLINE


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[PMID]:28471114
[Au] Autor:Li Y; Pan Q; Gu YS
[Ad] Endereço:Department of Ophthalmology, the First Affiliated Hospital, College of Medicine, Zhejiang University, Hangzhou 310003, China.
[Ti] Título:Phenotype-genotype correlation with Sanger sequencing identified retinol dehydrogenase 12 (RDH12) compound heterozygous variants in a Chinese family with Leber congenital amaurosis.
[So] Source:J Zhejiang Univ Sci B;18(5):421-429, 2017 May.
[Is] ISSN:1862-1783
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Leber congenital amaurosis (LCA) is a group of clinically and genetically heterogeneous retinal dystrophy. To date, 22 genes are known to be responsible for LCA, and some specific phenotypic features could provide significant prognostic information for a potential genetic etiology. This study is to identify gene variants responsible for LCA in a Chinese family using direct Sanger sequencing, with the help of phenotype-genotype correlations. METHODS: A Chinese family with six members including two individuals affected with LCA was studied. All patients underwent a complete ophthalmic examination. Based on phenotype-genotype correlation, direct Sanger sequencing was performed to identify the candidate gene on all family members and normal controls. Targeted next-generation sequencing was used to exclude other known LCA genes. RESULTS: By Sanger sequencing, we identified two novel missense variants in the retinol dehydrogenase 12 (RDH12) gene: a c.164C>A transversion predicting a p.T55K substitution, and a c.535C>G transversion predicting a p.H179D substitution. The two affected subjects carried both RDH12 variants, while their parents and offspring carried only one of heterozygous variants, showing complete cosegregation of the variants. The compound heterozygous variants were not present in 600 normal controls. Besides, the RDH12 variants were confirmed by targeted next-generation sequencing. CONCLUSIONS: The RDH12 compound heterozygous variants might be the cause of the LCA family. Our study adds to the molecular spectrum of RDH12-related retinopathy and offers an effective example of the power of phenotype-genotype correlations in molecular diagnosis of LCA.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/genética
Predisposição Genética para Doença/genética
Amaurose Congênita de Leber/enzimologia
Amaurose Congênita de Leber/genética
Polimorfismo de Nucleotídeo Único/genética
Análise de Sequência de DNA/métodos
[Mh] Termos MeSH secundário: Adulto
China
Feminino
Genótipo
Seres Humanos
Lactente
Amaurose Congênita de Leber/diagnóstico
Masculino
Meia-Idade
Fenótipo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.105 (RDH12 protein, human)
[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:170505
[St] Status:MEDLINE
[do] DOI:10.1631/jzus.B1600156


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[PMID]:29182182
[Au] Autor:Haas J; Häckh M; Justus V; Müller M; Lüdeke S
[Ad] Endereço:Institute of Pharmaceutical Sciences, University of Freiburg, Albertstraße 25, 79104 Freiburg, Germany. steffen.luedeke@pharmazie.uni-freiburg.de.
[Ti] Título:Addition of a polyhistidine tag alters the regioselectivity of carbonyl reductase S1 from Candida magnoliae.
[So] Source:Org Biomol Chem;15(48):10256-10264, 2017 Dec 13.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Studying enzymatic reductions of substrates with more than a single keto group is challenging, as the carbonyl reduction can create a vast array of regio- and stereoisomers. If used as reference compounds, regio- and stereopure hydroxy ketides could facilitate the characterization of reductases with unclear regio- and stereoselectivity. We have combined nonenzymatic and enzymatic reduction and oxidation steps to obtain all four regio- and stereoisomers of tert-butyl hydroxyoxohexanoates in high optical purity (enantiomeric ratio (er) of 99 : 1 for the δ-hydroxy-ß-keto isomers; er of >97 : 3 for the ß-hydroxy-δ-keto isomers). Furthermore, we have prepared seven of the eight possible regioisomers and diastereomers of γ-methylated hydroxyoxohexanoates. These 11 compounds allowed unraveling the complex stereoselectivity of ß,δ-diketo ester reductions catalyzed by carbonyl reductase S1 from Candida magnoliae (CMCR-S1). Our analysis shows that the regio- and stereoselectivity of CMCR-S1-catalyzed reductions is highly sensitive toward modifications at the C-terminus of CMCR-S1: in addition to the expected δ-hydroxy product, the variant with a C-terminal His-tag also led to formation of ß-hydroxy by-products with high optical purity.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/metabolismo
Candida/enzimologia
Histidina/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Histidina/química
Estrutura Molecular
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
26062-48-6 (polyhistidine); 4QD397987E (Histidine); EC 1.1.- (Alcohol Oxidoreductases)
[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:171129
[St] Status:MEDLINE
[do] DOI:10.1039/c7ob02666h


  4 / 12371 MEDLINE  
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[PMID]:29381923
[Au] Autor:Yang Y; Chu FH; Xu WR; Sun JQ; Sun X; Ma XM; Yu MW; Yang GW; Wang XM
[Ad] Endereço:Department of Oncology, Beijing Hospital of Traditional Chinese Medicine Affiliated to Capital Medical University.
[Ti] Título:Identification of regulatory role of DNA methylation in colon cancer gene expression via systematic bioinformatics analysis.
[So] Source:Medicine (Baltimore);96(47):e8487, 2017 Nov.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Colon cancer arises from the accumulations of genetic and epigenetic changes. Currently, profiles of DNA methylation and gene expression of colon cancer have not been elucidated clearly. This articles aims to characterize the profile of DNA methylation and gene expression of colon cancer systemically, and acquire candidate genes potentially regulated by altered methylation for this disease.Data were downloaded from The Cancer Genome Atlas database. Differentially methylated CpG sites (DMCs) and differentially methylated regions (DMRs) were calculated via COHCAP. Differentially expressed genes (DEGs) were identified by DESeq2. Weighted gene co-expression network analysis (WGCNA) package in R was applied for WGCNA.Data of 275 solid tumor tissues and 19 adjacent tumor tissues of colon cancer were obtained. A total of 1828 DMCs, including 1390 hypermethylated and 438 hypomethylated CpG sites, were identified between tumor and normal groups. A total of 789 DEGs, containing 435 upregulated genes and 354 downregulated genes were observed. It revealed that 8 DMRs-DEGs and 95 DMCs-DEGs pairs were significantly correlated. Furthermore, genes of yellow and brown modules from WGCNA were significantly correlated with tumor/normal status, and significantly enriched in peroxisome proliferator activated receptor signaling pathway, glutamatergic synapse, and neuroactive ligand-receptor interaction. Genes in the above 2 modules were also significantly enriched in DMCs or DMRs-associated genes. Specifically, ADHFE1, HAND2, and GNAO1 were hypermethylated and downregulated in colon cancer, suggesting that the low expression levels of these genes may be regulated by DNA hypermethylation. In addition, the 3 genes were involved in brown module of WGCNA, indicating their important roles in colon cancer.The investigation of the relationship between DNA methylation and gene expression may help to understand the effect of DNA methylation alteration on genes expression, especially gene co-expression network in the development of colon cancer. Genes such as ADHFE1, HAND2, and GNAO1 may be served as potential candidates for diagnosis and therapy targets in colon cancer.
[Mh] Termos MeSH primário: Neoplasias do Colo/genética
Neoplasias do Colo/fisiopatologia
Metilação de DNA/fisiologia
Expressão Gênica/fisiologia
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/metabolismo
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Ilhas de CpG/fisiologia
Bases de Dados Genéticas
Subunidades alfa Gi-Go de Proteínas de Ligação ao GTP/metabolismo
Redes Reguladoras de Genes/fisiologia
Seres Humanos
Proteínas Mitocondriais/metabolismo
Receptores Ativados por Proliferador de Peroxissomo/metabolismo
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (GNAO1 protein, human); 0 (HAND2 protein, human); 0 (Mitochondrial Proteins); 0 (Peroxisome Proliferator-Activated Receptors); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.99.24 (hydroxyacid-oxoacid transhydrogenase); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gi-Go)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180201
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000008487


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[PMID]:29337257
[Au] Autor:Dimopoulou M; Verhoef A; Gomes CA; van Dongen CW; Rietjens IMCM; Piersma AH; van Ravenzwaay B
[Ad] Endereço:Division of Toxicology, Wageningen University, The Netherlands; National Institute of Public Health and the Environment (RIVM), Bilthoven, The Netherlands. Electronic address: myrto.dimopoulou@wur.nl.
[Ti] Título:A comparison of the embryonic stem cell test and whole embryo culture assay combined with the BeWo placental passage model for predicting the embryotoxicity of azoles.
[So] Source:Toxicol Lett;286:10-21, 2018 Apr.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In the present study, we show the value of combining toxico-dynamic and -kinetic in vitro approaches for embryotoxicity testing of azoles. Both the whole embryo culture (WEC) and the embryonic stem cells test (EST) predicted the in vivo potency ranking of twelve tested azoles with moderate accuracy. Combining these results with relative placental transfer rates (Papp values) as determined in the BeWo cell culture model, increased the predictability of both WEC and EST, with R values increasing from 0.51 to 0.87 and from 0.35 to 0.60, respectively. The comparison of these in vitro systems correlated well (R = 0.67), correctly identifying the in vivo strong and weak embryotoxicants. Evaluating also specific gene responses related with the retinoic acid and sterol biosynthesis pathways, which represent the toxicological and fungicidal mode of action of azoles respectively in the WEC and EST, we observed that the differential regulation of Dhrs3 and Msmo1 reached higher magnitudes in both systems compared to Cyp26a1 and Cyp51. Establishing sensitive biomarkers across the in vitro systems for studying the underlying mechanism of action of chemicals, such as azoles, is valuable for comparing alternative in vitro models and for improving insight in the mechanism of developmental toxicity of chemicals.
[Mh] Termos MeSH primário: Azóis/toxicidade
Bioensaio
Embrião de Mamíferos/efeitos dos fármacos
Células-Tronco Embrionárias Murinas/efeitos dos fármacos
Placenta/efeitos dos fármacos
Teratogênios/toxicidade
Testes de Toxicidade/métodos
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/genética
Oxirredutases do Álcool/metabolismo
Animais
Transporte Biológico
Diferenciação Celular/efeitos dos fármacos
Linhagem Celular
Relação Dose-Resposta a Droga
Técnicas de Cultura Embrionária
Embrião de Mamíferos/metabolismo
Embrião de Mamíferos/patologia
Feminino
Regulação da Expressão Gênica no Desenvolvimento/efeitos dos fármacos
Seres Humanos
Cinética
Camundongos
Oxigenases de Função Mista/genética
Oxigenases de Função Mista/metabolismo
Células-Tronco Embrionárias Murinas/metabolismo
Células-Tronco Embrionárias Murinas/patologia
Miócitos Cardíacos/efeitos dos fármacos
Miócitos Cardíacos/metabolismo
Miócitos Cardíacos/patologia
Placenta/metabolismo
Placenta/patologia
Gravidez
Reprodutibilidade dos Testes
Ácido Retinoico 4 Hidroxilase/genética
Ácido Retinoico 4 Hidroxilase/metabolismo
Medição de Risco
Esterol 14-Desmetilase/genética
Esterol 14-Desmetilase/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azoles); 0 (Teratogens); EC 1.- (Mixed Function Oxygenases); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.71 (DHRS3 protein, mouse); EC 1.14.13.70 (Cyp51 protein, mouse); EC 1.14.13.70 (Sterol 14-Demethylase); EC 1.14.13.72 (methylsterol monooxygenase); EC 1.14.14.1 (Cyp26a1 protein, mouse); EC 1.14.14.1 (Retinoic Acid 4-Hydroxylase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE


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[PMID]:29188674
[Au] Autor:Ding BF; Shao L; Zhang RS; Liang C; Zhang YR
[Ad] Endereço:College of Life and Environmental Sciences, Shanghai Normal University, Shanghai 200234, China.
[Ti] Título:[Research Progress on Abused Drugs Metabolic in vivo].
[So] Source:Fa Yi Xue Za Zhi;32(4):290-295, 2016 Aug.
[Is] ISSN:1004-5619
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Under the catalysis of a variety of metabolic enzymes , such as UDP-glucuronyl transferases, cytochrome P450, carboxylesterase, sulfotransferase, butyrylcholinesterase, catechol- -methyl transferase and 6-morphine dehydrogenase, the drugs perform glucuronidation, hydrolysis, oxidation, sulfonation and other reactions, then translate into active or inactive metabolites, which are excreted through urination, bile or the other pathways at last. Different drugs own their different metabolic pathways. This paper introduces the studies about the metabolism of drugs in human and animal in recent years, such as morphine-like drugs, amphetamine, ketamine, cannabis and cocaine, and reviews the research progress about the sites of metabolism, metabolic enzymes, metabolites and physiological activity of those drugs metabolic .
[Mh] Termos MeSH primário: Colinesterases/metabolismo
Sistema Enzimático do Citocromo P-450/metabolismo
Glucuronosiltransferase/metabolismo
Drogas Ilícitas/metabolismo
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/metabolismo
Animais
Carboxilesterase/metabolismo
Catecol O-Metiltransferase/metabolismo
Seres Humanos
Oxirredução
Sulfotransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Street Drugs); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.218 (morphine 6-dehydrogenase); EC 2.1.1.6 (Catechol O-Methyltransferase); EC 2.4.1.17 (Glucuronosyltransferase); EC 2.8.2.- (Sulfotransferases); EC 3.1.1.1 (Carboxylesterase); EC 3.1.1.8 (Cholinesterases)
[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:171201
[St] Status:MEDLINE
[do] DOI:10.3969/j.issn.1004-5619.2016.04.013


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[PMID]:28745425
[Au] Autor:Filipov Y; Domanskyi S; Wood ML; Gamella M; Privman V; Katz E
[Ad] Endereço:Department of Chemistry and Biomolecular Science, Clarkson University, Potsdam, NY, 13699, USA.
[Ti] Título:Experimental Realization of a High-Quality Biochemical XOR Gate.
[So] Source:Chemphyschem;18(20):2908-2915, 2017 Oct 19.
[Is] ISSN:1439-7641
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:We report an experimental realization of a biochemical XOR gate function that avoids many of the pitfalls of earlier realizations based on biocatalytic cascades. Inputs-represented by pairs of chemicals-cross-react to largely cancel out when both are nearly equal. The cross-reaction can be designed to also optimize gate functioning for noise handling. When not equal, the residual inputs are further processed to result in the output of the XOR type, by biocatalytic steps that allow for further gate-function optimization. The quality of the realized XOR gate is theoretically analyzed.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Oxirredutases do Álcool/metabolismo
Biocatálise
Glucose Oxidase/metabolismo
Hexoquinase/metabolismo
NAD/metabolismo
Peroxidase/metabolismo
[Mh] Termos MeSH secundário: Armoracia/enzimologia
Aspergillus niger/enzimologia
Modelos Moleculares
Pichia/enzimologia
Saccharomyces cerevisiae/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0U46U6E8UK (NAD); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.1.3.13 (alcohol oxidase); EC 1.1.3.4 (Glucose Oxidase); EC 1.11.1.7 (Peroxidase); EC 2.7.1.1 (Hexokinase)
[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:170727
[St] Status:MEDLINE
[do] DOI:10.1002/cphc.201700705


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[PMID]:29225171
[Au] Autor:Bi C; Meng F; Yang L; Cheng L; Wang P; Chen M; Fang M; Xie H
[Ad] Endereço:Institute of Life Sciences, MOE Key Laboratory of Developmental Genes and Human Diseases, Southeast University, Nanjing 210096, China.
[Ti] Título:CtBP represses Dpp signaling as a dimer.
[So] Source:Biochem Biophys Res Commun;495(2):1980-1985, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:C-terminal binding protein (CtBP) is a highly conserved transcriptional co-repressor in animal development and human diseases. In Drosophila, CtBP is critical for fly development and is thought to exert its repressive roles in many signaling pathways including Dpp/BMP pathway. Here we provide evidence that although wild type CtBP negatively and dominantly influences Dpp signaling in fly presumptive wings, mutant CtBP unable to form dimer does not, indicating that dimerization is required for the repression role of CtBP in Dpp signaling in vivo.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/metabolismo
Proteínas de Ligação a DNA/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila/crescimento & desenvolvimento
Drosophila/metabolismo
Morfogênese/fisiologia
Asas de Animais/crescimento & desenvolvimento
Asas de Animais/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
Multimerização Proteica/fisiologia
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Drosophila Proteins); 0 (dpp protein, Drosophila); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.- (C-terminal binding protein)
[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:171212
[St] Status:MEDLINE


  9 / 12371 MEDLINE  
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[PMID]:29363372
[Au] Autor:Díaz-Quiroz DC; Cardona-Félix CS; Viveros-Ceballos JL; Reyes-González MA; Bolívar F; Ordoñez M; Escalante A
[Ad] Endereço:a Departamento de Ingeniería Celular y Biocatálisis , Instituto de Biotecnología, Universidad Nacional Autónoma de México , Cuernavaca , México.
[Ti] Título:Synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli.
[So] Source:J Enzyme Inhib Med Chem;33(1):397-404, 2018 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Shikimic acid (SA) pathway is the common route used by bacteria, plants, fungi, algae, and certain Apicomplexa parasites for the biosynthesis of aromatic amino acids and other secondary metabolites. As this essential pathway is absent in mammals designing inhibitors against implied enzymes may lead to the development of antimicrobial and herbicidal agents harmless to humans. Shikimate dehydrogenase (SDH) is the fourth enzyme of the SA pathway. In this contribution, a series of SA amide derivatives were synthesised and evaluated for in vitro SDH inhibition and antibacterial activity against Escherichia coli. All tested compounds showed to be mixed type inhibitors; diamide derivatives displayed more inhibitory activity than synthesised monoamides. Among the evaluated compounds, molecules called 4a and 4b were the most active derivatives with IC 588 and 589 µM, respectively. Molecular modelling studies suggested two different binding modes of monoamide and diamide derivatives to the SDH enzyme of E. coli.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/antagonistas & inibidores
Escherichia coli/enzimologia
Ácido Chiquímico/farmacologia
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/metabolismo
Relação Dose-Resposta a Droga
Modelos Moleculares
Conformação Molecular
Ácido Chiquímico/síntese química
Ácido Chiquímico/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
29MS2WI2NU (Shikimic Acid); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.25 (Shikimate dehydrogenase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2017.1422125


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[PMID]:28450226
[Au] Autor:Hara A; Endo S; Matsunaga T; El-Kabbani O; Miura T; Nishinaka T; Terada T
[Ad] Endereço:Faculty of Engineering, Gifu University, Gifu 501-1193, Japan.
[Ti] Título:Human carbonyl reductase 1 participating in intestinal first-pass drug metabolism is inhibited by fatty acids and acyl-CoAs.
[So] Source:Biochem Pharmacol;138:185-192, 2017 08 15.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human carbonyl reductase 1 (CBR1), a member of the short-chain dehydrogenase/reductase (SDR) superfamily, reduces a variety of carbonyl compounds including endogenous isatin, prostaglandin E and 4-oxo-2-nonenal. It is also a major non-cytochrome P450 enzyme in the phase I metabolism of carbonyl-containing drugs, and is highly expressed in the intestine. In this study, we found that long-chain fatty acids and their CoA ester derivatives inhibit CBR1. Among saturated fatty acids, myristic, palmitic and stearic acids were inhibitory, and stearic acid was the most potent (IC 9µM). Unsaturated fatty acids (oleic, elaidic, γ-linolenic and docosahexaenoic acids) and acyl-CoAs (palmitoyl-, stearoyl- and oleoyl-CoAs) were more potent inhibitors (IC 1.0-2.5µM), and showed high inhibitory selectivity to CBR1 over its isozyme CBR3 and other SDR superfamily enzymes (DCXR and DHRS4) with CBR activity. The inhibition by these fatty acids and acyl-CoAs was competitive with respect to the substrate, showing the K values of 0.49-1.2µM. Site-directed mutagenesis of the substrate-binding residues of CBR1 suggested that the interactions between the fatty acyl chain and the enzyme's Met141 and Trp229 are important for the inhibitory selectivity. We also examined CBR1 inhibition by oleic acid in cellular levels: The fatty acid effectively inhibited CBR1-mediated 4-oxo-2-nonenal metabolism in colon cancer DLD1 cells and increased sensitivity to doxorubicin in the drug-resistant gastric cancer MKN45 cells that highly express CBR1. The results suggest a possible new food-drug interaction through inhibition of CBR1-mediated intestinal first-pass drug metabolism by dietary fatty acids.
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Oxirredutases do Álcool/antagonistas & inibidores
Ácidos Graxos não Esterificados/metabolismo
Mucosa Intestinal/enzimologia
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/genética
Oxirredutases do Álcool/metabolismo
Sítios de Ligação
Ligação Competitiva
Linhagem Celular Tumoral
Resistência a Medicamentos Antineoplásicos
Interações Alimento-Droga
Seres Humanos
Mutação
Ácido Mirístico/metabolismo
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/metabolismo
Oxirredutases/antagonistas & inibidores
Oxirredutases/genética
Oxirredutases/metabolismo
Ácido Palmítico/metabolismo
Palmitoil Coenzima A/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Ácidos Esteáricos/metabolismo
Desidrogenase do Álcool de Açúcar/antagonistas & inibidores
Desidrogenase do Álcool de Açúcar/genética
Desidrogenase do Álcool de Açúcar/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Fatty Acids, Nonesterified); 0 (Neoplasm Proteins); 0 (Recombinant Proteins); 0 (Stearic Acids); 0I3V7S25AW (Myristic Acid); 1716-06-9 (oleoyl-coenzyme A); 1763-10-6 (Palmitoyl Coenzyme A); 2V16EO95H1 (Palmitic Acid); 362-66-3 (stearoyl-coenzyme A); 4ELV7Z65AP (stearic acid); EC 1.- (Oxidoreductases); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.- (Sugar Alcohol Dehydrogenases); EC 1.1.1.10 (L-xylulose reductase); EC 1.1.1.184 (CBR1 protein, human); EC 1.1.1.184 (CBR3 protein, human); EC 1.1.1.184 (DHRS4 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE



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