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Pesquisa : D08.811.682.047.150.700.156 [Categoria DeCS]
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[PMID]:28922901
[Au] Autor:Yamamoto K; Ozakiya Y; Uno T
[Ad] Endereço:Department of Bioscience and Biotechnology, Kyushu University Graduate School, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan.
[Ti] Título:Localization of an Aldo-Keto Reductase (AKR2E4) in the Silkworm Bombyx mori (Lepidoptera: Bombycidae).
[So] Source:J Insect Sci;17(5), 2017 Sep 01.
[Is] ISSN:1536-2442
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The aldo-keto reductase AKR2E4 reduces 3-dehydroecdysone to ecdysone in the silkworm Bombyx mori L. In this study, a quantitative polymerase chain reaction analysis revealed that the level of AKR2E4 mRNA was higher in the testes than in other tissues, and a western immunoblot analysis revealed that the AKR2E4 content in the testes was stage-specific from the fifth larval instar to the pupal stage. Immunohistochemical analysis showed that the AKR2E4 protein was present in cyst cells associated with sperm cells and spermatocytes. These results indicate that AKR2E4 plays an important role in 3-dehydroecdysone conversion to ecdysone and spermatogenesis in silkworm testes.
[Mh] Termos MeSH primário: Aldeído Redutase/genética
Bombyx/enzimologia
Bombyx/genética
Proteínas de Insetos/genética
[Mh] Termos MeSH secundário: Aldeído Redutase/metabolismo
Aldo-Ceto Redutases
Animais
Bombyx/crescimento & desenvolvimento
Proteínas de Insetos/metabolismo
Larva/enzimologia
Larva/crescimento & desenvolvimento
Masculino
Especificidade de Órgãos
Pupa/enzimologia
Pupa/crescimento & desenvolvimento
Reação em Cadeia da Polimerase em Tempo Real
Testículo/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insect Proteins); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE
[do] DOI:10.1093/jisesa/iex071


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[PMID]:28699078
[Au] Autor:Auiyawong B; Narawongsanont R; Tantitadapitak C
[Ad] Endereço:Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok, 10900, Thailand.
[Ti] Título:Characterization of AKR4C15, a Novel Member of Aldo-Keto Reductase, in Comparison with Other Rice AKR(s).
[So] Source:Protein J;36(4):257-269, 2017 Aug.
[Is] ISSN:1875-8355
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Environmental stresses often cause a rapid and excessive accumulation of reactive oxygen species (ROS), the toxicity of which is further amplified by downstream aldehyde production. Aldo-keto reductase (AKR) is a group of enzymes metabolizing aldehyde/ketone to the corresponding alcohol using NADPH as the cofactor. In this study, OsI_20197 (AKR4C15), a novel member of AKR4 subfamily C, was isolated and biochemically characterized. Kinetic studies on bacterially-expressed recombinant AKR4C15 revealed that the enzyme was capable of metabolizing a wide variety of aldehydes but clearly exhibited a preference for three carbon compounds, i.e. methylglyoxal, malondialdehyde and glyceraldehyde. In comparison with His-tagged proteins of AKR4C9 from Arabidopsis and several other rice AKR(s): OsI_04426, OsI_04428, OsI_04429, and OsI_15387, AKR4C15 was the one capable of most efficiently metabolizing MDA and had the highest value of catalytic efficiency, which was higher than the value of AKR4C9, approximately, by 30-fold; while its capability of metabolizing MG was on par with AKR4C9, OsI_04426 and OsI_04428 (AKR4C14); and was considerably higher than the activity of OsI_04429 and OsI_15387. In vivo research on transgenic Arabidopsis seedlings ectopically-expressing AKR4C15 showed that the levels of both MDA and MG were also significantly lower than the levels in wild-type seedlings under both normal and stress conditions, emphasizing the role of AKR4C15 in MG and MDA metabolism. In conclusion, AKR4C15, together with OsI_04426 and AKR4C14, may play protective roles against small reactive aldehydes and medium-chain aldehydes.
[Mh] Termos MeSH primário: Aldeído Redutase/metabolismo
Arabidopsis/enzimologia
Oryza/enzimologia
Proteínas de Plantas/metabolismo
Plântulas/enzimologia
[Mh] Termos MeSH secundário: Aldeído Redutase/genética
Aldo-Ceto Redutases
Sequência de Aminoácidos
Arabidopsis/efeitos dos fármacos
Arabidopsis/genética
Clonagem Molecular
Coenzimas/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Gliceraldeído/metabolismo
Gliceraldeído/farmacologia
Isoenzimas/genética
Isoenzimas/metabolismo
Cinética
Malondialdeído/metabolismo
Malondialdeído/farmacologia
NADP/metabolismo
Oryza/classificação
Oryza/efeitos dos fármacos
Oryza/genética
Estresse Oxidativo
Paraquat/farmacologia
Filogenia
Proteínas de Plantas/genética
Plantas Geneticamente Modificadas
Aldeído Pirúvico/metabolismo
Aldeído Pirúvico/farmacologia
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Plântulas/efeitos dos fármacos
Plântulas/genética
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (Isoenzymes); 0 (Plant Proteins); 0 (Recombinant Proteins); 367-47-5 (Glyceraldehyde); 4Y8F71G49Q (Malondialdehyde); 53-59-8 (NADP); 722KLD7415 (Pyruvaldehyde); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase); PLG39H7695 (Paraquat)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1007/s10930-017-9732-z


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[PMID]:28524228
[Au] Autor:Li S; Teng X; Su L; Mao G; Xu Y; Li T; Liu R; Zhang Q; Wang Y; Bartlam M
[Ad] Endereço:State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.
[Ti] Título:Structure and characterization of a NAD(P)H-dependent carbonyl reductase from Pseudomonas aeruginosa PAO1.
[So] Source:FEBS Lett;591(12):1785-1797, 2017 Jun.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:To investigate the function of the pa4079 gene from the opportunistic pathogen Pseudomonas aeruginosa PAO1, we determined its crystal structure and confirmed it to be a NAD(P)-dependent short-chain dehydrogenase/reductase. Structural similarity and activity for a broad range of substrates indicate that PA4079 functions as a carbonyl reductase. Comparison of apo- and holo-PA4079 shows that NADP stabilizes the active site specificity loop, and small molecule binding induces rotation of the Tyr183 side chain by approximately 90° out of the active site. Quantitative real-time PCR results show that pa4079 maintains high expression levels during antibiotic exposure. This work provides a starting point for understanding substrate recognition and selectivity by PA4079, as well as its possible reduction of antimicrobial drugs. DATABASE: Structural data are available in the Protein Data Bank (PDB) under the following accession numbers: apo PA4079 (condition I), 5WQM; apo PA4079 (condition II), 5WQN; PA4079 + NADP (condition I), 5WQO; PA4079 + NADP (condition II), 5WQP.
[Mh] Termos MeSH primário: Aldeído Redutase/metabolismo
Proteínas de Bactérias/metabolismo
Butiril-CoA Desidrogenase/metabolismo
Modelos Moleculares
NADP/metabolismo
Pseudomonas aeruginosa/metabolismo
[Mh] Termos MeSH secundário: Aldeído Redutase/química
Aldeído Redutase/genética
Aldo-Ceto Redutases
Sequência de Aminoácidos
Substituição de Aminoácidos
Antibacterianos/farmacologia
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Sítios de Ligação
Butiril-CoA Desidrogenase/química
Butiril-CoA Desidrogenase/genética
Domínio Catalítico
Sequência Conservada
Cristalografia por Raios X
Estabilidade Enzimática
Regulação Bacteriana da Expressão Gênica/efeitos dos fármacos
Holoenzimas/química
Holoenzimas/genética
Holoenzimas/metabolismo
Ligantes
Mutação
NADP/química
Conformação Proteica
Pseudomonas aeruginosa/efeitos dos fármacos
Pseudomonas aeruginosa/crescimento & desenvolvimento
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia Estrutural de Proteína
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Apoenzymes); 0 (Bacterial Proteins); 0 (Holoenzymes); 0 (Ligands); 0 (Recombinant Proteins); 53-59-8 (NADP); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase); EC 1.3.8.1 (Butyryl-CoA Dehydrogenase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12683


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[PMID]:28278373
[Au] Autor:Huang M; Mesaros C; Hackfeld LC; Hodge RP; Zang T; Blair IA; Penning TM
[Ti] Título:Potential Metabolic Activation of a Representative C4-Alkylated Polycyclic Aromatic Hydrocarbon Retene (1-Methyl-7-isopropyl-phenanthrene) Associated with the Deepwater Horizon Oil Spill in Human Hepatoma (HepG2) Cells.
[So] Source:Chem Res Toxicol;30(4):1093-1101, 2017 Apr 17.
[Is] ISSN:1520-5010
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Exposure to petrogenic polycyclic aromatic hydrocarbons (PPAHs) in the food chain is the major human health hazard associated with the Deepwater Horizon oil spill. C4-Phenanthrenes are representative PPAHs present in the crude oil and could contaminate the seafood. We describe the metabolism of a C4-phenanthrene regioisomer retene (1-methyl-7-isopropyl-phenanthrene) in human HepG2 cells as a model for metabolism in human hepatocytes. Retene because of its sites of alkylation cannot be metabolized to a diol-epoxide. The structures of the metabolites were identified by HPLC-UV-fluorescence detection and LC-MS/MS. O-Monosulfonated-retene-catechols were discovered as signature metabolites of the ortho-quinone pathway of PAH activation catalyzed by aldo-keto reductases. We also found evidence for the formation of bis-ortho-quinones where the two dicarbonyl groups were present on different rings of retene. The identification of O-monosulfonated-retene-catechol and O-bismethyl-O-monoglucuronosyl-retene-bis-catechol supports metabolic activation of retene by P450 and aldo-keto reductase isozymes followed by metabolic detoxification of the ortho-quinone through interception of redox cycling by catechol-O-methyltransferase, uridine 5'-diphospho-glucuronosyltransferase, and sulfotransferase isozymes. We propose that catechol conjugates could be used as biomarkers of human exposure to retene resulting from oil spills.
[Mh] Termos MeSH primário: Poluição por Petróleo
Fenantrenos/análise
Hidrocarbonetos Aromáticos Policíclicos/metabolismo
[Mh] Termos MeSH secundário: Aldeído Redutase/metabolismo
Aldo-Ceto Redutases
Alquilação
Catecol O-Metiltransferase/metabolismo
Catecóis/química
Cromatografia Líquida de Alta Pressão
Cadeia Alimentar
Células Hep G2
Seres Humanos
Fenantrenos/metabolismo
Hidrocarbonetos Aromáticos Policíclicos/química
Espectrofotometria Ultravioleta
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Catechols); 0 (Phenanthrenes); 0 (Polycyclic Aromatic Hydrocarbons); 0W2D2E1P9Q (retene); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase); EC 2.1.1.6 (Catechol O-Methyltransferase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE
[do] DOI:10.1021/acs.chemrestox.6b00457


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[PMID]:28222349
[Au] Autor:Vemanna RS; Babitha KC; Solanki JK; Amarnatha Reddy V; Sarangi SK; Udayakumar M
[Ad] Endereço:Department of Crop Physiology, University of Agricultural Sciences, GKVK, Bangalore 560065, India.
[Ti] Título:Aldo-keto reductase-1 (AKR1) protect cellular enzymes from salt stress by detoxifying reactive cytotoxic compounds.
[So] Source:Plant Physiol Biochem;113:177-186, 2017 Apr.
[Is] ISSN:1873-2690
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Cytotoxic compounds like reactive carbonyl compounds such as methylglyoxal (MG), melandialdehyde (MDA), besides the ROS accumulate significantly at higher levels under salinity stress conditions and affect lipids and proteins that inhibit plant growth and productivity. The detoxification of these cytotoxic compounds by overexpression of NADPH-dependent Aldo-ketoreductase (AKR1) enzyme enhances the salinity stress tolerance in tobacco. The PsAKR1 overexpression plants showed higher survival and chlorophyll content and reduced MDA, H2O2, and MG levels under NaCl stress. The transgenic plants showed reduced levels of Na levels in both root and shoot due to reduced reactive carbonyl compounds (RCCs) and showed enhanced membrane stability resulted in higher root growth and biomass. The increased levels of antioxidant glutathione and enhanced activity of superoxide dismutase (SOD), ascorbate peroxidase (APX) and glutathione reductase (GR) suggest AKR1 could protect these enzymes from the RCC induced protein carbonylation by detoxification process. The transgenics also showed higher activity of delta 1-pyrroline-5- carboxylate synthase (P5CS) enzyme resulted in increasedproline levels to maintain osmotic homeostasis. The results demonstrates that the AKR1 protects proteins or enzymes that are involved in scavenging of cytotoxic compounds by detoxifying RCCs generated under salinity stress.
[Mh] Termos MeSH primário: Oxirredutases/metabolismo
Plantas Tolerantes a Sal/fisiologia
Tabaco/enzimologia
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/metabolismo
Aldeído Redutase/metabolismo
Aldo-Ceto Redutases
Antioxidantes/metabolismo
Ascorbato Peroxidases/metabolismo
Biomassa
Clorofila/metabolismo
Glutationa Redutase/metabolismo
Peróxido de Hidrogênio/metabolismo
Ornitina-Oxo-Ácido Transaminase/metabolismo
Pressão Osmótica
Oxirredutases/biossíntese
Oxirredutases/genética
Fotossíntese
Plantas Geneticamente Modificadas
Prolina/metabolismo
Aldeído Pirúvico/metabolismo
Salinidade
Estresse Fisiológico/fisiologia
Superóxido Dismutase/metabolismo
Tabaco/genética
Tabaco/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 1406-65-1 (Chlorophyll); 722KLD7415 (Pyruvaldehyde); 9DLQ4CIU6V (Proline); BBX060AN9V (Hydrogen Peroxide); EC 1.- (Oxidoreductases); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase); EC 1.11.1.11 (Ascorbate Peroxidases); EC 1.15.1.1 (Superoxide Dismutase); EC 1.2.1.3 (Aldehyde Dehydrogenase); EC 1.8.1.7 (Glutathione Reductase); EC 2.6.1.13 (Ornithine-Oxo-Acid Transaminase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170222
[St] Status:MEDLINE


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[PMID]:27854034
[Au] Autor:He M; Zhou S; Cui M; Jin X; Lai D; Zhang S; Wang Z; Chen Z
[Ad] Endereço:Lab of Biocatalysis, Hangzhou Normal University, Hangzhou, Zhejiang, 311121, China.
[Ti] Título:Efficient Preparation of (S)-N-Boc-3-Hydroxylpiperidine Through Bioreduction by a Thermostable Aldo-KetoReductase.
[So] Source:Appl Biochem Biotechnol;181(4):1304-1313, 2017 Apr.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:(S)-N-Boc-3-hydroxypiperidine ((S)-NBHP) is a key pharmaceutical intermediate and the chiral source in synthesizing Imbruvica, which is a newly approved drug in lymphoma therapy by targeting Bruton's tyrosine kinase (BTK). Current chemical synthesis of (S)-NBHP suffered from the need of noble metal catalyst and low yield. The single reported bioconversion of (S)-NBHP was achieved by using recombinant ketoreductase, but enzyme sequence was kept confidential and the catalytic process suffered from the thermodeactivation and substrate inhibition. In the current study, we presented a thermostable aldo-keto reductase (AKR)-AKR-43-which showed high activity toward N-Boc-3-piperidone (NBP) to produce (S)-NBHP, high enantioselectivity, and no substrate inhibition. The molecular simulations demonstrated the structural rationale for the enantioselectivity of AKR-43 toward NBP and supported the classic ordered two-step catalytic mechanism. The catalytic process was achieved by using glucose dehydrogenase (GDH) for cofactor recycling, and the optimal reaction conditions were determined to be 30 °C and pH 7.5. Within a reaction time of 16 h, the 16 % substrate concentration (w/w), over 99 % ee and under 3.5 % of enzyme loading (w/w) characterized a high efficiency process with promising industrial values.
[Mh] Termos MeSH primário: Aldeído Redutase/metabolismo
Piperidinas/metabolismo
Temperatura Ambiente
[Mh] Termos MeSH secundário: Aldeído Redutase/química
Aldo-Ceto Redutases
Bacillus subtilis/enzimologia
Biocatálise
Estabilidade Enzimática
Simulação de Dinâmica Molecular
Oxirredução
Piperidinas/química
Conformação Proteica
Estereoisomerismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (N-tert-butoxycarbonyl-3-hydroxypiperidine); 0 (Piperidines); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161118
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-016-2285-3


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[PMID]:27806574
[Au] Autor:Penning TM
[Ad] Endereço:Center of Excellence in Environmental Toxicology, Department of Systems Pharmacology and Translational Therapeutics, Perelman School of Medicine, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
[Ti] Título:Aldo-Keto Reductase Regulation by the Nrf2 System: Implications for Stress Response, Chemotherapy Drug Resistance, and Carcinogenesis.
[So] Source:Chem Res Toxicol;30(1):162-176, 2017 01 17.
[Is] ISSN:1520-5010
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human aldo-keto reductases (AKRs) are NAD(P)H-dependent oxidoreductases that convert aldehydes and ketones to primary and secondary alcohols for subsequent conjugation reactions and can be referred to as "phase 1" enzymes. Among all the human genes regulated by the Keap1/Nrf2 pathway, they are consistently the most overexpressed in response to Nrf2 activators. Although these enzymes play clear cytoprotective roles and deal effectively with carbonyl stress, their upregulation by the Keap1/Nrf2 pathway also has a potential dark-side, which can lead to chemotherapeutic drug resistance and the metabolic activation of lung carcinogens (e.g., polycyclic aromatic hydrocarbons). They also play determinant roles in 4-(methylnitrosoamino)-1-(3-pyridyl)-1-butanone metabolism to R- and S-4-(methylnitrosoamino)-1-(3-pyridyl)-1-butanol. The overexpression of AKR genes as components of the "smoking gene" battery raises the issue as to whether this is part of a smoking stress response or acquired susceptibility to lung cancer. Human AKR genes also regulate retinoid, prostaglandin, and steroid hormone metabolism and can regulate the local concentrations of ligands available for nuclear receptors (NRs). The prospect exists that signaling through the Keap1/Nrf2 system can also effect NR signaling, but this has remained largely unexplored. We present the case that chemoprevention through the Keap1/Nrf2 system may be context dependent and that the Nrf2 "dose-response curve" for electrophilic and redox balance may not be monotonic.
[Mh] Termos MeSH primário: Aldeído Redutase/metabolismo
Proteína 1 Associada a ECH Semelhante a Kelch/metabolismo
Fator 2 Relacionado a NF-E2/metabolismo
Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Aldeído Redutase/genética
Aldeídos/metabolismo
Aldo-Ceto Redutases
Animais
Antineoplásicos/farmacologia
Carcinogênese/genética
Carcinogênese/metabolismo
Resistência a Medicamentos Antineoplásicos
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Peróxidos Lipídicos/metabolismo
Neoplasias/genética
Estresse Oxidativo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Aldehydes); 0 (Antineoplastic Agents); 0 (Kelch-Like ECH-Associated Protein 1); 0 (Lipid Peroxides); 0 (NF-E2-Related Factor 2); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161104
[St] Status:MEDLINE
[do] DOI:10.1021/acs.chemrestox.6b00319


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[PMID]:27835967
[Au] Autor:Chen K; Li K; Deng J; Zhang B; Lin J; Wei D
[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:Carbonyl reductase identification and development of whole-cell biotransformation for highly efficient synthesis of (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol.
[So] Source:Microb Cell Fact;15(1):191, 2016 Nov 11.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol [(R)-3,5-BTPE] is a valuable chiral intermediate for Aprepitant (Emend) and Fosaprepitant (Ivemend). Biocatalyzed asymmetric reduction is a preferred approach to synthesize highly optically active (R)-3,5-BTPE. However, the product concentration and productivity of reported (R)-3,5-BTPE synthetic processes remain unsatisfied. RESULTS: A NADPH-dependent carbonyl reductase from Lactobacillus kefir (LkCR) was discovered by genome mining for reduction of 3,5-bis(trifluoromethyl) acetophenone (3,5-BTAP) into (R)-3,5-BTPE with excellent enantioselectivity. In order to synthesize (R)-3,5-BTPE efficiently, LkCR was coexpressed with glucose dehydrogenase from Bacillus subtilis (BsGDH) for NADPH regeneration in Escherichia coli BL21 (DE3) cells, and the optimal recombinant strain produced 250.3 g/L (R)-3,5-BTPE with 99.9% ee but an unsatisfied productivity of 5.21 g/(L h). Then, four different linker peptides were used for the fusion expression of LkCR and BsGDH in E. coli to regulate catalytic efficiency of the enzymes and improved NADPH-recycling efficiency. Using the best strain (E. coli/pET-BsGDH-ER/K(10 nm)-LkCR), up to 297.3 g/L (R)-3,5-BTPE with enantiopurity >99.9% ee was produced via reduction of as much as 1.2 M of substrate with a 96.7% yield and productivity of 29.7 g/(L h). CONCLUSIONS: Recombinant E. coli/pET-BsGDH-ER/K(10 nm)-LkCR was developed for the bioreduction of 3,5-BTAP to (R)-3,5-BTPE, offered the best results in terms of high product concentration and productivity, demonstrating its great potential in industrial manufacturing of (R)-3,5-BTPE.
[Mh] Termos MeSH primário: Aldeído Redutase/metabolismo
Glucose 1-Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Aldeído Redutase/genética
Aldo-Ceto Redutases
Biotransformação
Eletroforese em Gel de Poliacrilamida/métodos
Glucose 1-Desidrogenase/genética
Técnicas de Patch-Clamp
Álcool Feniletílico/análogos & derivados
Álcool Feniletílico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (1-(3,5-bis(trifluoromethyl)phenyl)ethanol); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase); EC 1.1.1.47 (Glucose 1-Dehydrogenase); ML9LGA7468 (Phenylethyl Alcohol)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161113
[St] Status:MEDLINE


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[PMID]:27824809
[Au] Autor:MacLeod AK; Acosta-Jimenez L; Coates PJ; McMahon M; Carey FA; Honda T; Henderson CJ; Wolf CR
[Ad] Endereço:Division of Cancer Research, School of Medicine, University of Dundee, Ninewells Hospital, Dundee DD1 9SY, UK.
[Ti] Título:Aldo-keto reductases are biomarkers of NRF2 activity and are co-ordinately overexpressed in non-small cell lung cancer.
[So] Source:Br J Cancer;115(12):1530-1539, 2016 Dec 06.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Although the nuclear factor-erythroid 2-related factor 2 (NRF2) pathway is one of the most frequently dysregulated in cancer, it is not clear whether mutational status is a good predictor of NRF2 activity. Here we utilise four members of the aldo-keto reductase (AKR) superfamily as biomarkers to address this question. METHODS: Twenty-three cell lines of diverse origin and NRF2-pathway mutational status were used to determine the relationship between AKR expression and NRF2 activity. AKR expression was evaluated in lung cancer biopsies and Cancer Genome Atlas (TCGA) and Oncomine data sets. RESULTS: AKRs were expressed at a high basal level in cell lines carrying mutations in the NRF2 pathway. In non-mutant cell lines, co-ordinate induction of AKRs was consistently observed following activation of NRF2. Immunohistochemical analysis of lung tumour biopsies and interrogation of TCGA data revealed that AKRs are enriched in both squamous cell carcinomas (SCCs) and adenocarcinomas that contain somatic alterations in the NRF2 pathway but, in the case of SCC, AKRs were also enriched in most other tumours. CONCLUSIONS: An AKR biomarker panel can be used to determine NRF2 status in tumours. Hyperactivation of the NRF2 pathway is far more prevalent in lung SCC than previously predicted by genomic analyses.
[Mh] Termos MeSH primário: Aldeído Redutase/metabolismo
Biomarcadores/metabolismo
Carcinoma Pulmonar de Células não Pequenas/metabolismo
Neoplasias Pulmonares/metabolismo
Fator 2 Relacionado a NF-E2/metabolismo
[Mh] Termos MeSH secundário: Aldo-Ceto Redutases
Carcinoma Pulmonar de Células não Pequenas/patologia
Linhagem Celular Tumoral
Seres Humanos
Neoplasias Pulmonares/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (NF-E2-Related Factor 2); 0 (NFE2L2 protein, human); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161109
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2016.363


  10 / 466 MEDLINE  
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[PMID]:27629782
[Au] Autor:Matsunaga T; Saito H; Endo S; Iguchi K; Soda M; El-Kabbani O; Hara A; Ikari A
[Ad] Endereço:a Laboratory of Biochemistry, Gifu Pharmaceutical University , Gifu , Japan.
[Ti] Título:Roles of aldo-keto reductases 1B10 and 1C3 and ATP-binding cassette transporter in docetaxel tolerance.
[So] Source:Free Radic Res;50(12):1296-1308, 2016 Dec.
[Is] ISSN:1029-2470
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Docetaxel (DTX) is widely used for treatment of inveterate lung and prostate cancers, but its continuous administration elicits the hyposensitivity. Here, we established the DTX-resistant variants of human lung cancer A549 and androgen-independent prostate cancer Du145 cells and found that the resistance development provoked aberrant up-regulations of aldo-keto reductase (AKR) 1B10 and AKR1C3 in A549 and Du145 cells, respectively. In addition, the sensitivity to the DTX toxicity was significantly decreased and increased by overexpression and knockdown of the two AKR isoforms, respectively. Furthermore, the resistant cells exhibited a decreased level of reactive 4-hydroxy-2-nonenal formed during DTX treatment, and the decrease was alleviated by adding the AKR inhibitors, inferring that the two AKRs confer the chemoresistance through elevating the antioxidant properties. The development of DTX resistance was also associated with enhanced expression of an ATP-binding cassette (ABC) transporter ABCB1 among the ABC transporter isoforms. The combined treatment with inhibitors of the two AKRs and ABCB1 additively sensitized the resistant cells to DTX. Intriguingly, the AKR1B10 inhibitor also suppressed the lung cancer cross-resistance against cisplatin. The results suggest that combined treatment with AKRs (1B10 and 1C3) and ABCB1 inhibitors exerts overcoming effect against the cancer resistance to DTX and cisplatin, and can be used as the adjuvant therapy.
[Mh] Termos MeSH primário: Transportadores de Cassetes de Ligação de ATP/metabolismo
Aldeído Redutase/metabolismo
Antineoplásicos/uso terapêutico
Taxoides/uso terapêutico
[Mh] Termos MeSH secundário: Aldo-Ceto Redutases
Antineoplásicos/administração & dosagem
Antineoplásicos/farmacologia
Linhagem Celular Tumoral
Seres Humanos
Taxoides/administração & dosagem
Taxoides/farmacologia
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Taxoids); 15H5577CQD (docetaxel); EC 1.1.1.- (Aldo-Keto Reductases); EC 1.1.1.21 (Aldehyde Reductase)
[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:160916
[St] Status:MEDLINE



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