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  1 / 2243 MEDLINE  
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[PMID]:29267382
[Au] Autor:Zhang Z; Gu Q; de Manuel Montero M; Bravo IG; Marques-Bonet T; Häussinger D; Münk C
[Ad] Endereço:Clinic for Gastroenterology, Hepatology, and Infectiology, Medical Faculty, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
[Ti] Título:Stably expressed APOBEC3H forms a barrier for cross-species transmission of simian immunodeficiency virus of chimpanzee to humans.
[So] Source:PLoS Pathog;13(12):e1006746, 2017 12.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:APOBEC3s (A3s) are potent restriction factors of human immunodeficiency virus type 1/simian immunodeficiency viruses (HIV-1/SIV), and can repress cross-species transmissions of lentiviruses. HIV-1 originated from a zoonotic infection of SIV of chimpanzee (SIVcpz) to humans. However, the impact of human A3s on the replication of SIVcpz remains unclear. By using novel SIVcpz reporter viruses, we identified that human APOBEC3B (A3B) and APOBEC3H (A3H) haplotype II strongly reduced the infectivity of SIVcpz, because both of them are resistant to SIVcpz Vifs. We further demonstrated that human A3H inhibited SIVcpz by deaminase dependent as well independent mechanisms. In addition, other stably expressed human A3H haplotypes and splice variants showed strong antiviral activity against SIVcpz. Moreover, most SIV and HIV lineage Vif proteins could degrade chimpanzee A3H, but no Vifs from SIVcpz and SIV of gorilla (SIVgor) lineages antagonized human A3H haplotype II. Expression of human A3H hapII in human T cells efficiently blocked the spreading replication of SIVcpz. The spreading replication of SIVcpz was also restricted by stable A3H in human PBMCs. Thus, we speculate that stably expressed human A3H protects humans against the cross-species transmission of SIVcpz and that SIVcpz spillover to humans may have started in individuals that harbor haplotypes of unstable A3H proteins.
[Mh] Termos MeSH primário: Aminoidrolases/metabolismo
Transmissão de Doença Infecciosa
Síndrome de Imunodeficiência Adquirida dos Símios/transmissão
Vírus da Imunodeficiência Símia
Zoonoses
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Pan troglodytes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.5.4.- (APOBEC3H protein, human); EC 3.5.4.- (Aminohydrolases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180111
[Lr] Data última revisão:
180111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006746


  2 / 2243 MEDLINE  
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[PMID]:28957411
[Au] Autor:Hodge-Hanson KM; Downs DM
[Ad] Endereço:Department of Microbiology, University of Georgia, Athens, Georgia, United States of America.
[Ti] Título:Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro.
[So] Source:PLoS One;12(9):e0185544, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Rid (YjgF/YER057c/UK114) protein family is a group of small, sequence diverse proteins that consists of eight subfamilies. The archetypal RidA subfamily is found in all domains, while the Rid1-7 subfamilies are present only in prokaryotes. Bacterial genomes often encode multiple members of the Rid superfamily. The best characterized member of this protein family, RidA from Salmonella enterica, is a deaminase that quenches the reactive metabolite 2-aminoacrylate generated by pyridoxal 5'-phosphate-dependent enzymes and ultimately spares certain enzymes from damage. The accumulation of 2-aminoacrylate can damage enzymes and lead to growth defects in bacteria, plants, and yeast. While all subfamily members have been annotated as imine deaminases based on the RidA characterization, experimental evidence to support this annotation exists for a single protein outside the RidA subfamily. Here we report that six proteins, spanning Rid subfamilies 1-3, deaminate a variety of imine/enamine substrates with differing specific activities. Proteins from the Rid2 and Rid3 subfamilies, but not from the RidA and Rid1 subfamilies deaminated iminoarginine, generated in situ by the Pseudomonas aeruginosa D-arginine dehydrogenase DauA. These data biochemically distinguished the subfamilies and showed Rid proteins have activity on a metabolite that is physiologically relevant in Pseudomonas and other bacteria.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/metabolismo
Aminoidrolases/metabolismo
Proteínas de Bactérias/metabolismo
Pseudomonas aeruginosa/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aminoidrolases/química
Aminoidrolases/genética
Mutação
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (arginine oxidase); EC 3.5.4.- (Aminohydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185544


  3 / 2243 MEDLINE  
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[PMID]:28873512
[Au] Autor:Dong TT; Gong JS; Gu BC; Zhang Q; Li H; Lu ZM; Lu ML; Shi JS; Xu ZH
[Ad] Endereço:School of Pharmaceutical Science, Jiangnan University, Wuxi 214122, PR China; National Engineering Laboratory for Cereal Fermentation Technology, School of Biotechnology, Jiangnan University, Wuxi 214122, PR China.
[Ti] Título:Significantly enhanced substrate tolerance of Pseudomonas putida nitrilase via atmospheric and room temperature plasma and cell immobilization.
[So] Source:Bioresour Technol;244(Pt 1):1104-1110, 2017 Nov.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The objective of the study was to enhance the substrate tolerance of Pseudomonas putida nitrilase via atmospheric and room temperature plasma (ARTP) and cell immobilization. The mutant library was constructed by ARTP and rapidly screened by an OPA-TCA microscale reaction. A mutant strain of mut-D3 was obtained and its optimum substrate concentration was improved to 150mM from 100mM. It could accumulate 189g/L nicotinic acid (NA) from 3-cyanopyridine (3-CP), which was increased by 42% compared with that of wild type (WT). Additionally, composite immobilization of mut-D3 was performed and SA-PVA immobilized cells could catalyze 250mM 3-CP each batch with finally accumulating 346g/L NA, while free cells accumulated 175g/L NA. These results indicated that the free or immobilized catalysts of mut-D3 could serve as a good choice for NA production. This is the first report on mutation breeding of nitrilase-producing microorganisms by ARTP.
[Mh] Termos MeSH primário: Aminoidrolases
Pseudomonas putida
[Mh] Termos MeSH secundário: Piridinas
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyridines); EC 3.5.4.- (Aminohydrolases); EC 3.5.5.1 (nitrilase); X64V0K6260 (3-cyanopyridine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE


  4 / 2243 MEDLINE  
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[PMID]:28808129
[Au] Autor:Toussaint JP; Farrell-Sherman A; Feldman TP; Smalley NE; Schaefer AL; Greenberg EP; Dandekar AA
[Ad] Endereço:Department of Medicine, University of Washington, Seattle, Washington, USA.
[Ti] Título:Gene Duplication in Pseudomonas aeruginosa Improves Growth on Adenosine.
[So] Source:J Bacteriol;199(21), 2017 Nov 01.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The laboratory strain of , PAO1, activates genes for catabolism of adenosine using quorum sensing (QS). However, this strain is not well-adapted for growth on adenosine, with doubling times greater than 40 h. We previously showed that when PAO1 is grown on adenosine and casein, variants emerge that grow rapidly on adenosine. To understand the mechanism by which this adaptation occurs, we performed whole-genome sequencing of five isolates evolved for rapid growth on adenosine. All five genomes had a gene duplication-amplification (GDA) event covering several genes, including the quorum-regulated nucleoside hydrolase gene, , and PA0148, encoding an adenine deaminase. In addition, two of the growth variants also exhibited a promoter mutation. We recapitulated the rapid growth phenotype with a plasmid containing six genes common to all the GDA events. We also showed that and PA0148, the two genes at either end of the common GDA, were sufficient to confer rapid growth on adenosine. Additionally, we demonstrated that the variant promoter increased basal expression of but maintained its QS regulation. Therefore, GDA in confers the ability to grow efficiently on adenosine while maintaining QS regulation of nucleoside catabolism. thrives in many habitats and is an opportunistic pathogen of humans. In these diverse environments, must adapt to use myriad potential carbon sources. PAO1 cannot grow efficiently on nucleosides, including adenosine; however, it can acquire this ability through genetic adaptation. We show that the mechanism of adaptation is by amplification of a specific region of the genome and that the amplification preserves the regulation of the adenosine catabolic pathway by quorum sensing. These results demonstrate an underexplored mechanism of adaptation by , with implications for phenotypes such as development of antibiotic resistance.
[Mh] Termos MeSH primário: Adenosina/metabolismo
Aminoidrolases/genética
Duplicação Gênica
N-Glicosil Hidrolases/genética
Pseudomonas aeruginosa/crescimento & desenvolvimento
Pseudomonas aeruginosa/fisiologia
[Mh] Termos MeSH secundário: Adaptação Biológica
Aminoidrolases/metabolismo
Meios de Cultura/química
Análise Mutacional de DNA
Genoma Bacteriano
N-Glicosil Hidrolases/metabolismo
Plasmídeos
Regiões Promotoras Genéticas
Pseudomonas aeruginosa/enzimologia
Pseudomonas aeruginosa/genética
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 3.5.4.- (Aminohydrolases); EC 3.5.4.2 (adenine deaminase); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171118
[Lr] Data última revisão:
171118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE


  5 / 2243 MEDLINE  
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[PMID]:28662040
[Au] Autor:Song Y; Li J; Shin HD; Liu L; Du G; Chen J
[Ad] Endereço:Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, Wuxi, China.
[Ti] Título:Tuning the transcription and translation of L-amino acid deaminase in Escherichia coli improves α-ketoisocaproate production from L-leucine.
[So] Source:PLoS One;12(6):e0179229, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:α-Ketoisocaproate (KIC) is used widely in the pharmaceutical and nutraceutical industries. In previous studies, we achieved a one-step biosynthesis of KIC from l-leucine, using an Escherichia coli whole-cell biocatalyst expressing an l-amino acid deaminase (l-AAD) from Proteus vulgaris. Herein, we report the fine-tuning of l-AAD gene expression in E. coli BL21 (DE3) at the transcriptional and translational levels to improve the KIC titer. By optimizing the plasmid origin with different copy numbers, modulating messenger RNA structure downstream of the initiation codon, and designing the sequences at the ribosome binding site, we increased biocatalyst activity to 31.77%, 24.89%, and 30.20%, respectively, above that achieved with BL21/pet28a-lad. The highest KIC titers reached 76.47 g·L-1, 80.29 g·L-1, and 81.41 g·L-1, respectively. Additionally, the integration of these three engineering strategies achieved an even higher KIC production of 86.55 g·L-1 and a higher l-leucine conversion rate of 94.25%. The enzyme-engineering strategies proposed herein may be generally applicable to the construction of other biocatalysts.
[Mh] Termos MeSH primário: Aminoidrolases/genética
Caproatos/metabolismo
Escherichia coli/genética
Leucina/metabolismo
Biossíntese de Proteínas
Transcrição Genética
[Mh] Termos MeSH secundário: Biocatálise
Cromatografia Líquida de Alta Pressão
Códon
Plasmídeos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caproates); 0 (Codon); 2492-75-3 (alpha-ketocaproic acid); EC 3.5.4.- (Aminohydrolases); GMW67QNF9C (Leucine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179229


  6 / 2243 MEDLINE  
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[PMID]:28475648
[Au] Autor:Nakano Y; Misawa N; Juarez-Fernandez G; Moriwaki M; Nakaoka S; Funo T; Yamada E; Soper A; Yoshikawa R; Ebrahimi D; Tachiki Y; Iwami S; Harris RS; Koyanagi Y; Sato K
[Ad] Endereço:Laboratory of Systems Virology, Department of Biosystems Science, Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, Japan.
[Ti] Título:HIV-1 competition experiments in humanized mice show that APOBEC3H imposes selective pressure and promotes virus adaptation.
[So] Source:PLoS Pathog;13(5):e1006348, 2017 May.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:APOBEC3 (A3) family proteins are DNA cytosine deaminases recognized for contributing to HIV-1 restriction and mutation. Prior studies have demonstrated that A3D, A3F, and A3G enzymes elicit a robust anti-HIV-1 effect in cell cultures and in humanized mouse models. Human A3H is polymorphic and can be categorized into three phenotypes: stable, intermediate, and unstable. However, the anti-viral effect of endogenous A3H in vivo has yet to be examined. Here we utilize a hematopoietic stem cell-transplanted humanized mouse model and demonstrate that stable A3H robustly affects HIV-1 fitness in vivo. In contrast, the selection pressure mediated by intermediate A3H is relaxed. Intriguingly, viral genomic RNA sequencing reveled that HIV-1 frequently adapts to better counteract stable A3H during replication in humanized mice. Molecular phylogenetic analyses and mathematical modeling suggest that stable A3H may be a critical factor in human-to-human viral transmission. Taken together, this study provides evidence that stable variants of A3H impose selective pressure on HIV-1.
[Mh] Termos MeSH primário: Aminoidrolases/genética
Citosina Desaminase/genética
Infecções por HIV/virologia
HIV-1/fisiologia
Produtos do Gene vif do Vírus da Imunodeficiência Humana/genética
[Mh] Termos MeSH secundário: Aminoidrolases/metabolismo
Animais
Citosina Desaminase/metabolismo
Modelos Animais de Doenças
Células HEK293
Infecções por HIV/transmissão
HIV-1/genética
Seres Humanos
Camundongos
Camundongos Knockout
Modelos Genéticos
Mutação
Filogenia
RNA Viral/química
RNA Viral/genética
Análise de Sequência de RNA
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral); 0 (vif Gene Products, Human Immunodeficiency Virus); 0 (vif protein, Human immunodeficiency virus 1); EC 3.5.4.- (APOBEC3H protein, human); EC 3.5.4.- (Aminohydrolases); EC 3.5.4.1 (APOBEC3 protein, human); EC 3.5.4.1 (Cytosine Deaminase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006348


  7 / 2243 MEDLINE  
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[PMID]:28394261
[Au] Autor:Lee D; Xu IM; Chiu DK; Lai RK; Tse AP; Lan Li L; Law CT; Tsang FH; Wei LL; Chan CY; Wong CM; Ng IO; Wong CC
[Ti] Título:Folate cycle enzyme MTHFD1L confers metabolic advantages in hepatocellular carcinoma.
[So] Source:J Clin Invest;127(5):1856-1872, 2017 May 01.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cancer cells preferentially utilize glucose and glutamine, which provide macromolecules and antioxidants that sustain rapid cell division. Metabolic reprogramming in cancer drives an increased glycolytic rate that supports maximal production of these nutrients. The folate cycle, through transfer of a carbon unit between tetrahydrofolate and its derivatives in the cytoplasmic and mitochondrial compartments, produces other metabolites that are essential for cell growth, including nucleotides, methionine, and the antioxidant NADPH. Here, using hepatocellular carcinoma (HCC) as a cancer model, we have observed a reduction in growth rate upon withdrawal of folate. We found that an enzyme in the folate cycle, methylenetetrahydrofolate dehydrogenase 1-like (MTHFD1L), plays an essential role in support of cancer growth. We determined that MTHFD1L is transcriptionally activated by NRF2, a master regulator of redox homeostasis. Our observations further suggest that MTHFD1L contributes to the production and accumulation of NADPH to levels that are sufficient to combat oxidative stress in cancer cells. The elevation of oxidative stress through MTHFD1L knockdown or the use of methotrexate, an antifolate drug, sensitizes cancer cells to sorafenib, a targeted therapy for HCC. Taken together, our study identifies MTHFD1L in the folate cycle as an important metabolic pathway in cancer cells with the potential for therapeutic targeting.
[Mh] Termos MeSH primário: Aminoidrolases/metabolismo
Carcinoma Hepatocelular/enzimologia
Ácido Fólico/metabolismo
Formiato-Tetra-Hidrofolato Ligase/metabolismo
Neoplasias Hepáticas/enzimologia
Metilenotetra-Hidrofolato Desidrogenase (NADP)/metabolismo
Complexos Multienzimáticos/metabolismo
Proteínas de Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Aminoidrolases/genética
Carcinoma Hepatocelular/genética
Carcinoma Hepatocelular/patologia
Ácido Fólico/genética
Formiato-Tetra-Hidrofolato Ligase/genética
Células Hep G2
Seres Humanos
Neoplasias Hepáticas/genética
Neoplasias Hepáticas/patologia
Metilenotetra-Hidrofolato Desidrogenase (NADP)/genética
Complexos Multienzimáticos/genética
Fator 2 Relacionado a NF-E2/genética
Fator 2 Relacionado a NF-E2/metabolismo
Proteínas de Neoplasias/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Multienzyme Complexes); 0 (NF-E2-Related Factor 2); 0 (NFE2L2 protein, human); 0 (Neoplasm Proteins); 73699-18-0 (formyl-methenyl-methylenetetrahydrofolate synthetase); 935E97BOY8 (Folic Acid); EC 1.5.1.5 (Methylenetetrahydrofolate Dehydrogenase (NADP)); EC 3.5.4.- (Aminohydrolases); EC 6.3.4.3 (Formate-Tetrahydrofolate Ligase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE


  8 / 2243 MEDLINE  
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[PMID]:28336404
[Au] Autor:Nakashima M; Tsuzuki S; Awazu H; Hamano A; Okada A; Ode H; Maejima M; Hachiya A; Yokomaku Y; Watanabe N; Akari H; Iwatani Y
[Ad] Endereço:Clinical Research Center, National Hospital Organization Nagoya Medical Center, Nagoya, Aichi 460-0001, Japan.
[Ti] Título:Mapping Region of Human Restriction Factor APOBEC3H Critical for Interaction with HIV-1 Vif.
[So] Source:J Mol Biol;429(8):1262-1276, 2017 Apr 21.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The APOBEC3 (A3) family of cellular cytidine deaminases comprises seven members (A, B, C, D, F, G, and H) that potently inhibit retroviral replication. Human immunodeficiency virus type 1 (HIV-1) Vif is a small pleiotropic protein that specifically inactivates these enzymes, targeting them for ubiquitin-mediated proteasomal degradation. A3 Vif-interaction sites are presumed to fall into three distinct types: A3C/D/F, A3G, and A3H. To date, two types of A3G and A3C/D/F sites have been well characterized, whereas the A3H Vif-binding site remains poorly defined. Here, we explore the residues critical for the A3H-type Vif interaction. To avoid technical difficulties in performing experiments with human A3H haplotype II (hapII), which is relatively resistant to HIV-1 Vif, we employed its ortholog chimpanzee A3H (cA3H), which displays high Vif sensitivity, for a comparison of sensitivity with that of A3H hapII. The Vif susceptibility of A3H hapII-cA3H chimeras and their substitution mutants revealed a single residue at position 97 as a major determinant for the difference in their Vif sensitivities. We further surveyed critical residues by structure-guided mutagenesis using an A3H structural model and thus identified eight additional residues important for Vif sensitivity, which mapped to the α3 and α4 helices of A3H. Interestingly, this area is located on a surface adjacent to the A3G and A3C/D/F interfaces and is composed of negatively charged and hydrophobic patches. These findings suggest that HIV-1 Vif has evolved to utilize three dispersed surfaces for recognizing three types of interfaces on A3 proteins under certain structural constraints.
[Mh] Termos MeSH primário: Aminoidrolases/metabolismo
Produtos do Gene vif do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Aminoidrolases/química
Aminoidrolases/genética
Animais
Sítios de Ligação
Interações Hospedeiro-Patógeno
Seres Humanos
Mutagênese
Pan troglodytes
Conformação Proteica
Mapeamento de Interação de Proteínas/métodos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Produtos do Gene vif do Vírus da Imunodeficiência Humana/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 0 (vif Gene Products, Human Immunodeficiency Virus); 0 (vif protein, Human immunodeficiency virus 1); EC 3.5.4.- (APOBEC3H protein, human); EC 3.5.4.- (Aminohydrolases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170427
[Lr] Data última revisão:
170427
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE


  9 / 2243 MEDLINE  
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[PMID]:28265723
[Au] Autor:Park JM; Trevor Sewell B; Benedik MJ
[Ad] Endereço:Department of Biology, Texas A&M University, College Station, TX, 77843-3258, USA.
[Ti] Título:Cyanide bioremediation: the potential of engineered nitrilases.
[So] Source:Appl Microbiol Biotechnol;101(8):3029-3042, 2017 Apr.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The cyanide-degrading nitrilases are of notable interest for their potential to remediate cyanide contaminated waste streams, especially as generated in the gold mining, pharmaceutical, and electroplating industries. This review provides a brief overview of cyanide remediation in general but with a particular focus on the cyanide-degrading nitrilases. These are of special interest as the hydrolysis reaction does not require secondary substrates or cofactors, making these enzymes particularly good candidates for industrial remediation processes. The genetic approaches that have been used to date for engineering improved enzymes are described; however, recent structural insights provide a promising new approach.
[Mh] Termos MeSH primário: Aminoidrolases/genética
Aminoidrolases/metabolismo
Biodegradação Ambiental
Cianetos/metabolismo
[Mh] Termos MeSH secundário: Bacillus/enzimologia
Bacillus/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Geobacillus/enzimologia
Geobacillus/genética
Hidroliases/metabolismo
Concentração de Íons de Hidrogênio
Hidrólise
Modelos Moleculares
Engenharia de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cyanides); EC 3.5.4.- (Aminohydrolases); EC 3.5.5.1 (nitrilase); EC 4.2.1.- (Hydro-Lyases); EC 4.2.1.- (nitrile hydratase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170425
[Lr] Data última revisão:
170425
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-017-8204-x


  10 / 2243 MEDLINE  
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[PMID]:28259896
[Au] Autor:Konno M; Asai A; Kawamoto K; Nishida N; Satoh T; Doki Y; Mori M; Ishii H
[Ad] Endereço:Department of Frontier Science for Cancer and Chemotherapy, Osaka University, Osaka 565-0871, Japan.
[Ti] Título:The one-carbon metabolism pathway highlights therapeutic targets for gastrointestinal cancer (Review).
[So] Source:Int J Oncol;50(4):1057-1063, 2017 Apr.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:After the initial use of anti-folates for treatment of malignancies, folate metabolism has emerged as a rational diagnostic and therapeutic target in gastrointestinal cancer. The one-carbon metabolic pathway, which comprises three critical reactions (i.e., folate and methionine cycles), underlies this effect in conjunction with the trans-sulfuration pathway. Understanding of the one-carbon metabolism pathway has served to unravel the link between the causes and effects of cancer phenotypes leading to several seminal discoveries such as that of diadenosine tri-phosphate hydrolase, microRNAs, 5-FU and, more recently, trifluridine. In the folate cycle, glycine and serine fuel the mitochondrial enzymes SHMT2, MTHFD2 and ALDH1L2, which play critical roles in the cancer survival and proliferation presumably through purine production. In the methionine cycle, S-adenocyl methionine serves hydrocarbons and polyamines that are critical for the epigenetic controls. The trans-sulfuration pathway is a critical component in the synthesis of glutathione, which is involved in the production of reactive oxygen species in cancer stem cells. Therefore, characterization of one-carbon metabolism is indispensable to the development of precision medicine in the context of cancer diagnostics and therapeutics. In the present study, we review the historical issues associated with one-carbon metabolism and highlight the recent advances in cancer research.
[Mh] Termos MeSH primário: Antineoplásicos/uso terapêutico
Ácido Fólico/metabolismo
Neoplasias Gastrointestinais/metabolismo
Redes e Vias Metabólicas/efeitos dos fármacos
Metionina/metabolismo
Mitocôndrias/metabolismo
Terapia de Alvo Molecular/métodos
[Mh] Termos MeSH secundário: Aminoidrolases/metabolismo
Fluoruracila/metabolismo
Antagonistas do Ácido Fólico/uso terapêutico
Neoplasias Gastrointestinais/tratamento farmacológico
Glicina Hidroximetiltransferase/metabolismo
Seres Humanos
Metaboloma
Metilenotetra-Hidrofolato Desidrogenase (NADP)/metabolismo
MicroRNAs/metabolismo
Mitocôndrias/enzimologia
Complexos Multienzimáticos/metabolismo
Nucleosídeos/uso terapêutico
Nucleotídeos/uso terapêutico
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Purinas/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Serina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Folic Acid Antagonists); 0 (MicroRNAs); 0 (Multienzyme Complexes); 0 (Nucleosides); 0 (Nucleotides); 0 (Purines); 0 (Reactive Oxygen Species); 0 (methylene tetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase); 452VLY9402 (Serine); 935E97BOY8 (Folic Acid); AE28F7PNPL (Methionine); EC 1.5.- (ALDH1L2 protein, human); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.1.5 (Methylenetetrahydrofolate Dehydrogenase (NADP)); EC 2.1.2.1 (Glycine Hydroxymethyltransferase); EC 2.1.2.1 (SHMT protein, human); EC 3.5.4.- (Aminohydrolases); U3P01618RT (Fluorouracil); W60KTZ3IZY (purine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170306
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2017.3885



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