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[PMID]:28707464
[Au] Autor:Zou X; Lin J; Mao X; Zhao S; Ren Y
[Ad] Endereço:State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology , Shanghai 200237, China.
[Ti] Título:Biosynthesis of L-Erythrose by Assembly of Two Key Enzymes in Gluconobacter oxydans.
[So] Source:J Agric Food Chem;65(35):7721-7725, 2017 Sep 06.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:L-erythrose, a rare aldotetrose, possesses various pharmacological activities. However, efficient L-erythrose production is challenging. Currently, L-erythrose is produced by a two-step fermentation process from erythritol. Here, we describe a novel strategy for the production of L-erythrose in Gluconobacter oxydans (G. oxydans) by localizing the assembly of L-ribose isomerase (L-RI) to membrane-bound sorbitol dehydrogenase (SDH) via the protein-peptide interactions of the PDZ domain and PDZ ligand. To demonstrate this self-assembly, green fluorescent protein (GFP) replaced L-RI and its movement to membrane-bound SDH was observed by fluorescence microscopy. The final L-erythrose production was improved to 23.5 g/L with the stepwise metabolic engineering of G. oxydans, which was 1.4-fold higher than that obtained using coexpression of SDH and L-RI in G. oxydans. This self-assembly strategy shows remarkable potential for further improvement of L-erythrose production.
[Mh] Termos MeSH primário: Aldose-Cetose Isomerases/metabolismo
Proteínas de Bactérias/metabolismo
Gluconobacter oxydans/metabolismo
L-Iditol 2-Desidrogenase/metabolismo
Tetroses/metabolismo
[Mh] Termos MeSH secundário: Aldose-Cetose Isomerases/genética
Proteínas de Bactérias/genética
Gluconobacter oxydans/enzimologia
Gluconobacter oxydans/genética
L-Iditol 2-Desidrogenase/genética
Engenharia Metabólica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Tetroses); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase); EC 5.3.1.- (Aldose-Ketose Isomerases); EC 5.3.1.20 (ribose isomerase); X3EI0WE8Q4 (erythrose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02201


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Val, Adalberto Luis
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[PMID]:28707373
[Au] Autor:Duarte RM; Sadauskas-Henrique H; de Almeida-Val VMF; Val AL; Nice HE; Gagnon MM
[Ad] Endereço:São Paulo State University (UNESP), Institute of Bioscence, São Vicente, São Paulo, Brazil.
[Ti] Título:Biomarker responses and PAH ratios in fish inhabiting an estuarine urban waterway.
[So] Source:Environ Toxicol;32(10):2305-2315, 2017 Oct.
[Is] ISSN:1522-7278
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many cities worldwide are established adjacent to estuaries and their catchments resulting in estuarine contamination due to intense anthropogenic activities. The aim of this study was to evaluate if fish living in an estuarine urban waterway were affected by contamination, via the measurement of a suite of biomarkers of fish health. Black bream (Acanthopagrus butcheri) were sampled in a small urban embayment and a suite of biomarkers of fish health measured. These were condition factor (CF), liver somatic index (LSI), gonadosomatic index (GSI), hepatic EROD activity, polycyclic aromatic hydrocarbon (PAH) biliary metabolites, serum sorbitol dehydrogenase (s-SDH) and branchial enzymes cytochrome C oxidase (CCO), and lactate dehydrogenase (LDH) activities. The biomarkers of exposure EROD activity, and pyrene- and B(a)P-type biliary metabolites confirmed current or recent exposure of the fish and that fish were metabolizing contaminants. Relative to a reference site, LSI was higher in fish collected in the urban inlet as was the metabolic enzyme LDH activity. CF, GSI, s-SDH, CCO, and naphthalene-type metabolites were at similar levels in the urban inlet relative to the reference site. PAH biliary metabolite ratios of high-molecular-weight to low-molecular-weight suggest that fish from the urban inlet were exposed to pyrogenic PAHs, likely from legacy contamination and road runoff entering the embayment. Similarly, the sediment PAH ratios and the freshness indices suggested legacy contamination of a pyrogenic source, likely originating from the adjacent historic gasworks site and a degree of contamination of petrogenic nature entering the inlet via storm water discharge. Biomarkers of exposure and effect confirmed that black bream collected in the Claisebrook Cove inlet, Western Australia, are currently exposed to contamination and are experiencing metabolic perturbations not observed in fish collected at a nearby reference site.
[Mh] Termos MeSH primário: Perciformes/metabolismo
Hidrocarbonetos Aromáticos Policíclicos/toxicidade
Poluentes Químicos da Água/toxicidade
[Mh] Termos MeSH secundário: Animais
Baías
Bile/metabolismo
Biomarcadores/metabolismo
Citocromo P-450 CYP1A1/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Monitoramento Ambiental
Estuários
L-Iditol 2-Desidrogenase/metabolismo
L-Lactato Desidrogenase/metabolismo
Fígado/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Polycyclic Aromatic Hydrocarbons); 0 (Water Pollutants, Chemical); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 1.14.14.1 (Cytochrome P-450 CYP1A1); EC 1.9.3.1 (Electron Transport Complex IV)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE
[do] DOI:10.1002/tox.22447


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[PMID]:28011130
[Au] Autor:Cui ZM; Zhang JD; Fan XJ; Zheng GW; Chang HH; Wei WL
[Ad] Endereço:Department of Biological and Pharmaceutical Engineering, College of Chemistry and Chemical Engineering, Taiyuan University of Technology, Taiyuan, Shanxi, 030024, PR China.
[Ti] Título:Highly efficient bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol by two substrate tolerance carbonyl reductases with cofactor regeneration.
[So] Source:J Biotechnol;243:1-9, 2017 Feb 10.
[Is] ISSN:1873-4863
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Optically pure 1-phenyl-1,2-ethanediol is a very important chiral building block and intermediate in fine chemical and pharmaceutical industries. Reduction of 2-hydroxyacetophenone provides a straightforward approach to access these important compounds. In this study, two enantiocomplementary carbonyl reductases, BDHA (2,3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR (polyol dehydrogenase from Gluconobacter oxydans) were discovered for the first time to convert 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) and (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity, respectively. The two enzymes were purified and characterized. In vitro bioreduction of 2-HAP catalyzed by BDHA and GoSCR coupled with glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration were demonstrated, affording both (R)-PED and (S)-PED in>99% ee and 99% conversion. Recombinant Escherichia coli whole cells co-expressing both GDH and BDHA or GoSCR genes were used to asymmetric reduction of 2-HAP to (R)-PED or (S)-PED. Under the optimized conditions, the bioreduction of 400mM (54g/L) substrate was proceeded smoothly without the external addition of cofactor, and the product (R)-PED and (S)-PED were obtained with 99% yield, >99% ee and 18.0g/L/h volumetric productivity. These results offer a practical biocatalytic method for the preparation of both (R)-PED and (S)-PED with high volumetric productivity.
[Mh] Termos MeSH primário: Acetofenonas/metabolismo
Oxirredutases do Álcool/metabolismo
Etilenoglicóis/metabolismo
[Mh] Termos MeSH secundário: Acetofenonas/química
Oxirredutases do Álcool/química
Bacillus subtilis/enzimologia
Biotransformação
Butileno Glicóis/metabolismo
Clonagem Molecular
Ativação Enzimática
Escherichia coli/enzimologia
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Etilenoglicóis/química
Gluconobacter oxydans/enzimologia
Gluconobacter oxydans/genética
Glucose 1-Desidrogenase/metabolismo
L-Iditol 2-Desidrogenase/metabolismo
Chaperonas Moleculares
Estereoisomerismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetophenones); 0 (Butylene Glycols); 0 (Escherichia coli Proteins); 0 (Ethylene Glycols); 0 (Molecular Chaperones); 2ZAC511UK8 (styrene glycol); 3E533Z76W0 (2'-hydroxyacetophenone); 45427ZB5IJ (2,3-butylene glycol); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase); EC 1.1.1.47 (Glucose 1-Dehydrogenase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170404
[Lr] Data última revisão:
170404
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE


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[PMID]:27692814
[Au] Autor:Tripathi M; Singh AP; Gupta G; Rajender S
[Ad] Endereço:Division of Endocrinology, Central Drug Research Institute, Lucknow, India.
[Ti] Título:Concomitant and discrete expressions of aldose reductase and sorbitol dehydrogenase in the male reproductive tract.
[So] Source:Acta Histochem;118(8):776-783, 2016 Oct.
[Is] ISSN:1618-0372
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:This study aimed at investigating the expression and localization of the polyol pathway enzymes; aldose reductase (AR) and sorbitol dehydrogenase (SDH), in the male reproductive tract of rat. Gene expression analysis showed maximum expression of AR and SDH in the coagulating glands. Western blot analysis showed a coordinated presence of the two enzymes in the coagulating glands, seminal vesicle and epididymis. Immunohistochemistry showed a concordant expression of the two enzymes in the coagulating gland, which goes well with its function of fructose production in rats. A less concordant expression of the two enzymes in the seminal vesicle was also seen. Discrete expression of AR was seen in the Sertoli cells without SDH. Germ cells including sperm in the seminiferous tubules lacked AR, but SDH was present in all stages of developing germ cells including sperm present in the seminiferous tubules. The epithelial layer of epididymis showed the presence of AR, but it was negligible in vas deferens and prostate. SDH was not seen in the epithelial layer of epididymis, vas deferens or prostate. Though sperm in the seminiferous tubules lacked AR, sperm extracted from cauda showed the presence of both AR and SDH. Immunofluorescence localization of AR and SDH on sperm showed the presence of both the enzymes all over sperm. Discrete expression of AR in the Sertoli cells may be linked to detoxification of a number of metabolism by-products. Similarly, the presence of polyol enzymes on sperm in epididymis and beyond may be to tackle toxic metabolites they may encounter during their journey along the male or female reproductive tract.
[Mh] Termos MeSH primário: Aldeído Redutase/metabolismo
Epididimo/metabolismo
L-Iditol 2-Desidrogenase/metabolismo
Próstata/metabolismo
Túbulos Seminíferos/metabolismo
Espermatozoides/metabolismo
[Mh] Termos MeSH secundário: Animais
Frutose/metabolismo
Masculino
Ratos Sprague-Dawley
Glândulas Seminais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
30237-26-4 (Fructose); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase); EC 1.1.1.21 (Aldehyde Reductase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170123
[Lr] Data última revisão:
170123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE


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[PMID]:27628063
[Au] Autor:Winges A; Garcia TB; Prager P; Wiedemann P; Kohen L; Bringmann A; Hollborn M
[Ad] Endereço:Department of Ophthalmology and Eye Hospital, Faculty of Medicine, University of Leipzig, Liebigstrasse 10-14, D-04103, Leipzig, Germany.
[Ti] Título:Osmotic expression of aldose reductase in retinal pigment epithelial cells: involvement of NFAT5.
[So] Source:Graefes Arch Clin Exp Ophthalmol;254(12):2387-2400, 2016 Dec.
[Is] ISSN:1435-702X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Diabetic retinopathy is associated with osmotic stress resulting from hyperglycemia and intracellular sorbitol accumulation. Systemic hypertension is a risk factor of diabetic retinopathy. High intake of dietary salt increases extracellular osmolarity resulting in systemic hypertension. We determined the effects of extracellular hyperosmolarity, chemical hypoxia, and oxidative stress on the gene expression of enzymes involved in sorbitol production and conversion in cultured human retinal pigment epithelial (RPE) cells. METHODS: Alterations in the expression of aldose reductase (AR) and sorbitol dehydrogenase (SDH) genes were examined with real-time RT-PCR. Protein levels were determined with Western blot analysis. Nuclear factor of activated T cell 5 (NFAT5) was knocked down with siRNA. RESULTS: AR gene expression in RPE cells was increased by high (25 mM) extracellular glucose, CoCl (150 µM)-induced chemical hypoxia, H O (20 µM)-induced oxidative stress, and extracellular hyperosmolarity induced by addition of NaCl or sucrose. Extracellular hyperosmolarity (but not hypoxia) also increased AR protein level. SDH gene expression was increased by hypoxia and oxidative stress, but not extracellular hyperosmolarity. Hyperosmolarity and hypoxia did not alter the SDH protein level. The hyperosmotic AR gene expression was dependent on activation of metalloproteinases, autocrine/paracrine TGF-ß signaling, activation of p38 MAPK, ERK1/2, and PI3K signal transduction pathways, and the transcriptional activity of NFAT5. Knockdown of NAFT5 or inhibition of AR decreased the cell viability under hyperosmotic (but not hypoxic) conditions and aggravated the hyperosmotic inhibition of cell proliferation. CONCLUSIONS: The data suggest that sorbitol accumulation in RPE cells occurs under hyperosmotic, but not hypoxic and oxidative stress conditions. NFAT5- and AR-mediated sorbitol accumulation may protect RPE cells under conditions of osmotic stress.
[Mh] Termos MeSH primário: Aldeído Redutase/genética
Retinopatia Diabética/genética
Regulação da Expressão Gênica
L-Iditol 2-Desidrogenase/genética
RNA/genética
Epitélio Pigmentado da Retina/metabolismo
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Aldeído Redutase/biossíntese
Western Blotting
Proliferação Celular
Sobrevivência Celular
Células Cultivadas
Retinopatia Diabética/metabolismo
Retinopatia Diabética/patologia
Seres Humanos
L-Iditol 2-Desidrogenase/biossíntese
Fatores de Transcrição NFATC
Concentração Osmolar
Estresse Oxidativo
Reação em Cadeia da Polimerase em Tempo Real
Epitélio Pigmentado da Retina/patologia
Fatores de Transcrição/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NFAT5 protein, human); 0 (NFATC Transcription Factors); 0 (Transcription Factors); 63231-63-0 (RNA); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase); EC 1.1.1.21 (Aldehyde Reductase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160916
[St] Status:MEDLINE


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[PMID]:27535960
[Au] Autor:Steinhauser CB; Landers M; Myatt L; Burghardt RC; Vallet JL; Bazer FW; Johnson GA
[Ad] Endereço:Department of Veterinary Integrative Biosciences, Texas A&M University, College Station, Texas.
[Ti] Título:Fructose Synthesis and Transport at the Uterine-Placental Interface of Pigs: Cell-Specific Localization of SLC2A5, SLC2A8, and Components of the Polyol Pathway.
[So] Source:Biol Reprod;95(5):108, 2016 Nov.
[Is] ISSN:1529-7268
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The fetal fluids and uterine flushings of pigs contain higher concentrations of fructose than glucose, but fructose is not detected in maternal blood. Fructose can be synthesized from glucose via enzymes of the polyol pathway, aldose reductase (AKR1B1) and sorbitol dehydrogenase (SORD), transported across cell membranes by solute carriers SLC2A5 and SLC2A8, and converted to fructose-1-phosphate by ketohexokinase (KHK). SLC2A8, SLC2A5, AKR1B1, SORD, and KHK mRNAs and proteins were analyzed using quantitative PCR and immunohistochemistry or in situ hybridization in endometria and placentae of cyclic and pregnant gilts, cyclic gilts injected with estrogen, and ovariectomized gilts injected with progesterone. Progesterone up-regulated SLC2A8 protein in uterine luminal (LE) and glandular epithelia during the peri-implantation period, and expression became exclusively placental, chorion and blood vessels, after Day 30. P4 up-regulated SLC2A5 mRNA in uterine LE and glandular epithelia after implantation, and the chorion expressed SLC2A5 between Days 30 and 85. AKR1B1 and SORD proteins localized to uterine LE during the peri-implantation period, but expression switched to chorion by Day 20 and was maintained through Day 85. Uterine expression of AKR1B1 mRNA was down-regulated by estrogen. KHK protein localized to trophectoderm/chorion throughout gestation. These results provide evidence that components for the conversion of glucose to fructose and for fructose transport are present at the uterine-placental interface of pigs. The shift in expression from LE to chorion during pregnancy suggests free-floating conceptuses are supported by fructose synthesized by the uterus, but after implantation, the chorion becomes self-sufficient for fructose synthesis and transport.
[Mh] Termos MeSH primário: Frutose/metabolismo
Proteínas Facilitadoras de Transporte de Glucose/metabolismo
Transportador de Glucose Tipo 5/metabolismo
Placenta/metabolismo
Útero/metabolismo
[Mh] Termos MeSH secundário: Aldeído Redutase/metabolismo
Animais
Implantação do Embrião/efeitos dos fármacos
Implantação do Embrião/fisiologia
Estradiol/farmacologia
Ciclo Estral/metabolismo
Feminino
Frutose/biossíntese
L-Iditol 2-Desidrogenase/metabolismo
Ovariectomia
Placenta/efeitos dos fármacos
Gravidez
Progesterona/farmacologia
Suínos
Útero/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucose Transport Proteins, Facilitative); 0 (Glucose Transporter Type 5); 30237-26-4 (Fructose); 4G7DS2Q64Y (Progesterone); 4TI98Z838E (Estradiol); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase); EC 1.1.1.21 (Aldehyde Reductase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160819
[St] Status:MEDLINE


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[PMID]:27411537
[Au] Autor:Sadauskas-Henrique H; Braz-Mota S; Duarte RM; de Almeida-Val VM
[Ad] Endereço:Laboratory of Ecophysiology and Molecular Evolution, Brazilian National Institute for Research in the Amazon, Ave André Araújo 2936, Manaus, AM, 69083-000, Brazil. helensadauskas@gmail.com.
[Ti] Título:Influence of the natural Rio Negro water on the toxicological effects of a crude oil and its chemical dispersion to the Amazonian fish Colossoma macropomum.
[So] Source:Environ Sci Pollut Res Int;23(19):19764-75, 2016 Oct.
[Is] ISSN:1614-7499
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The increment in crude oil exploitation over the last decades has considerably increased the risk of polycyclic aromatic hydrocarbon (PAH) contamination to Amazonian aquatic environments, especially for the black water environments such as the Rio Negro. The present work was designed to evaluate the acute toxicity of the Urucu crude oil (CO), the chemically dispersed Urucu crude oil (CO + D), and the dispersant alone (D) to the Amazonian fish Colossoma macropomum. Acute toxicity tests were performed, using a more realistic approach, where fish were acclimated to both groundwater (GW), used as internal control, and natural Rio Negro water (RNW) and exposed to CO, CO + D and D. Then, biomarkers such as ethoxyresorufin-O-deethylase (EROD), superoxide dismutase (SOD), lipid peroxidation (LPO), serum sorbitol dehydrogenase (s-SDH) in liver, DNA damage in blood cells, and the presence of the benzo[a]pyrene-type, pyrene-type, and naphthalene-type metabolites in fish bile were assessed. Fish exposed to CO and CO + D, at both water types tested, presented increased biomarker responses and higher PAH-type metabolites in the bile. However, fish exposed to these treatments after the acclimation to RNW increased the levels of LPO, s-SDH (hepatotoxicity), DNA damage in blood cells (genotoxicity), and benzo[a]pyrene-type metabolites when compared to fish in GW. Our data suggests that some physicochemical properties of Rio Negro water (i.e., presence of natural organic matter (NOM)) might cause mild chemical stress responses in fish, which can make it more susceptible to oxidative stress following exposure to crude oil, particularly to those chemically dispersed.
[Mh] Termos MeSH primário: Peixes/metabolismo
Petróleo/toxicidade
Rios/química
Poluentes Químicos da Água/toxicidade
[Mh] Termos MeSH secundário: Animais
Bile/química
Biomarcadores/metabolismo
Citocromo P-450 CYP1A1/metabolismo
Dano ao DNA
Proteínas de Peixes/metabolismo
L-Iditol 2-Desidrogenase/metabolismo
Peroxidação de Lipídeos
Fígado/metabolismo
Superóxido Dismutase/metabolismo
Testes de Toxicidade Aguda
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Fish Proteins); 0 (Petroleum); 0 (Water Pollutants, Chemical); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase); EC 1.14.14.1 (Cytochrome P-450 CYP1A1); EC 1.15.1.1 (Superoxide Dismutase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160715
[St] Status:MEDLINE
[do] DOI:10.1007/s11356-016-7190-3


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[PMID]:27373435
[Au] Autor:Naidu PB; Sathibabu Uddandrao VV; Naik RR; Pothani S; Munipally PK; Meriga B; Begum MS; Varatharaju C; Pandiyan R; Saravanan G
[Ad] Endereço:Animal Physiology and Biochemistry Laboratory, Department of Biochemistry, Sri Venkateswara University, Tirupati, India.
[Ti] Título:Effects of S-Allylcysteine on Biomarkers of the Polyol Pathway in Rats with Type 2 Diabetes.
[So] Source:Can J Diabetes;40(5):442-448, 2016 Oct.
[Is] ISSN:2352-3840
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: We evaluated the effects of S-allylcysteine (SAC) on biomarkers of the polyol pathway in streptozotocin-nicotinamide (STZ-NA)-induced diabetes in rats. METHODS: Diabetes was induced in male albino Wistar rats by intraperitoneal administration of STZ (55 mg kg bw ) and NA (110 mg kg bw ). SAC (150 mg kg bw ) was orally administered to the rats with diabetes for 45 days to assess its effects on blood glucose, insulin, insulin resistance, glycated hemoglobin, aldose reductase (AR), sorbitol dehydrogenase (SDH), sorbitol, fructose, thiobarbituric acid-reactive substances (TBARS), hydroperoxide, hemoglobin and glutathione (GSH). RESULTS: On SAC administration in the rats with diabetes, the levels of blood glucose, insulin resistance, glycated hemoglobin, AR, SDH, sorbitol, fructose, TBARS and hydroperoxide increased significantly (p<0.05), whereas those of insulin, hemoglobin and GSH decreased. SAC showed therapeutic effects similar to those of gliclazide in decreasing blood glucose, AR, SDH, sorbitol, fructose, glycosylated hemoglobin, TBARS and hydroperoxides levels and significant increases in insulin, hemoglobin and GSH activity in rats with diabetes. Moreover, histopathologic studies also revealed the protective effect of SAC on pancreatic beta cells. CONCLUSIONS: The results indicate that SAC prevents complications of diabetes by reducing the influx of glucose in the polyol pathway, thereby elevating the GSH level and reducing the activities of AR and SDH. Therefore, SAC may have imperative implications for the deterrence and early treatment of type 2 diabetes.
[Mh] Termos MeSH primário: Cisteína/análogos & derivados
Diabetes Mellitus Experimental/tratamento farmacológico
Hipoglicemiantes/farmacologia
Redes e Vias Metabólicas/efeitos dos fármacos
Polímeros/metabolismo
[Mh] Termos MeSH secundário: Aldeído Redutase/sangue
Animais
Biomarcadores/sangue
Glicemia/efeitos dos fármacos
Cisteína/farmacologia
Cisteína/uso terapêutico
Frutose/sangue
Glutationa/sangue
Hemoglobina A Glicada/metabolismo
Hemoglobinas/metabolismo
Peróxido de Hidrogênio/sangue
Hipoglicemiantes/uso terapêutico
Resistência à Insulina
L-Iditol 2-Desidrogenase/sangue
Ratos Wistar
Sorbitol/sangue
Substâncias Reativas com Ácido Tiobarbitúrico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Blood Glucose); 0 (Glycated Hemoglobin A); 0 (Hemoglobins); 0 (Hypoglycemic Agents); 0 (Polymers); 0 (Thiobarbituric Acid Reactive Substances); 0 (polyol); 30237-26-4 (Fructose); 506T60A25R (Sorbitol); 81R3X99M15 (S-allylcysteine); BBX060AN9V (Hydrogen Peroxide); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase); EC 1.1.1.21 (Aldehyde Reductase); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160705
[St] Status:MEDLINE


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[PMID]:27347931
[Au] Autor:Xi W; Zheng H; Zhang Q; Li W
[Ad] Endereço:College of Horticulture and Landscape Architecture, Southwest University, Chongqing 400716, China. xwp1999@zju.edu.cn.
[Ti] Título:Profiling Taste and Aroma Compound Metabolism during Apricot Fruit Development and Ripening.
[So] Source:Int J Mol Sci;17(7), 2016 Jun 24.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Sugars, organic acids and volatiles of apricot were determined by HPLC and GC-MS during fruit development and ripening, and the key taste and aroma components were identified by integrating flavor compound contents with consumers' evaluation. Sucrose and glucose were the major sugars in apricot fruit. The contents of all sugars increased rapidly, and the accumulation pattern of sugars converted from glucose-predominated to sucrose-predominated during fruit development and ripening. Sucrose synthase (SS), sorbitol oxidase (SO) and sorbitol dehydrogenase (SDH) are under tight developmental control and they might play important roles in sugar accumulation. Almost all organic acids identified increased during early development and then decrease rapidly. During early development, fruit mainly accumulated quinate and malate, with the increase of citrate after maturation, and quinate, malate and citrate were the predominant organic acids at the ripening stage. The odor activity values (OAV) of aroma volatiles showed that 18 aroma compounds were the characteristic components of apricot fruit. Aldehydes and terpenes decreased significantly during the whole development period, whereas lactones and apocarotenoids significantly increased with fruit ripening. The partial least squares regression (PLSR) results revealed that ß-ionone, γ-decalactone, sucrose and citrate are the key characteristic flavor factors contributing to consumer acceptance. Carotenoid cleavage dioxygenases (CCD) may be involved in ß-ionone formation in apricot fruit.
[Mh] Termos MeSH primário: Qualidade dos Alimentos
Frutas/metabolismo
Odorantes
Óleos Voláteis/metabolismo
Prunus armeniaca/metabolismo
[Mh] Termos MeSH secundário: Citratos/metabolismo
Frutas/crescimento & desenvolvimento
Glucosiltransferases/metabolismo
L-Iditol 2-Desidrogenase/metabolismo
Malatos/metabolismo
Oxirredutases/metabolismo
Prunus armeniaca/crescimento & desenvolvimento
Ácido Quínico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Citrates); 0 (Malates); 0 (Oils, Volatile); 058C04BGYI (Quinic Acid); EC 1.- (Oxidoreductases); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase); EC 1.1.99.- (sorbitol oxidase); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.13 (sucrose synthase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160628
[St] Status:MEDLINE


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[PMID]:27189063
[Au] Autor:Yuan J; Wu M; Lin J; Yang L
[Ad] Endereço:Key Laboratory of Biomass Chemical Engineering of the Ministry of Education,College of Chemical and Biological Engineering, Zhejiang University, Hangzhou, 310027, China.
[Ti] Título:Combinatorial metabolic engineering of industrial Gluconobacter oxydans DSM2343 for boosting 5-keto-D-gluconic acid accumulation.
[So] Source:BMC Biotechnol;16(1):42, 2016 May 17.
[Is] ISSN:1472-6750
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: L-(+)-tartaric acid (L-TA) is an important organic acid, which is produced from the cream of tartar or stereospecific hydrolysis of the cis-epoxysuccinate. The former method is limited by the availability of raw material and the latter is dependent on the petrochemical material. Thus, new processes for the economical preparation of L-TA from carbohydrate or renewable resource would be much more attractive. Production of 5-keto-D-gluconate (5-KGA) from glucose by Gluconobacter oxydans is the first step to produce L-TA. The aim of this work is to enhance 5-KGA accumulation using combinatorial metabolic engineering strategies in G. oxydans. The sldAB gene, encoding sorbitol dehydrogenase, was overexpressed in an industrial strain G. oxydans ZJU2 under a carefully selected promoter, P0169. To enhance the efficiency of the oxidation by sldAB, the coenzyme pyrroloquinoline quinone (PQQ) and respiratory chain were engineered. Besides, the role in sldAB overexpression, coenzyme and respiratory chain engineering and their subsequent effects on 5-KGA production were investigated. RESULTS: An efficient, stable recombinant strain was constructed, whereas the 5-KGA production could be enhanced. By self-overexpressing the sldAB gene in G. oxydans ZJU2 under the constitutive promoter P0169, the resulting strain, G. oxydans ZJU3, produced 122.48 ± 0.41 g/L of 5-KGA. Furthermore, through the coenzyme and respiratory chain engineering, the titer and productivity of 5-KGA reached 144.52 ± 2.94 g/L and 2.26 g/(L · h), respectively, in a 15 L fermenter. It could be further improved the 5-KGA titer by 12.10 % through the fed-batch fermentation under the pH shift and dissolved oxygen tension (DOT) control condition, obtained 162 ± 2.12 g/L with the productivity of 2.53 g/(L · h) within 64 h. CONCLUSIONS: The 5-KGA production could be significantly enhanced with the combinatorial metabolic engineering strategy in Gluconobacter strain, including sldAB overexpression, coenzyme and respiratory chain engineering. Fed-batch fermentation could further enlarge the positive effect and increase the 5-KGA production. All of these demonstrated that the robust recombinant strain can efficiently produce 5-KGA in larger scale to fulfill the industrial production of L-TA from 5-KGA.
[Mh] Termos MeSH primário: Melhoramento Genético/métodos
Gluconatos/metabolismo
Gluconobacter oxydans/enzimologia
Gluconobacter oxydans/genética
L-Iditol 2-Desidrogenase/genética
Engenharia Metabólica/métodos
[Mh] Termos MeSH secundário: Técnicas de Química Combinatória/métodos
Gluconatos/isolamento & purificação
Gluconobacter oxydans/classificação
Microbiologia Industrial/métodos
Regiões Promotoras Genéticas/genética
Proteínas Recombinantes/metabolismo
Especificidade da Espécie
Regulação para Cima/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5-keto-d-gluconate); 0 (Gluconates); 0 (Recombinant Proteins); EC 1.1.1.14 (L-Iditol 2-Dehydrogenase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160519
[St] Status:MEDLINE
[do] DOI:10.1186/s12896-016-0272-y



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