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  1 / 3846 MEDLINE  
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[PMID]:28862845
[Au] Autor:Xu Y; Wang L; Chen J; Zhao J; Fan S; Dong Y; Ha NC; Quan C
[Ad] Endereço:Department of Bioengineering, College of Life Science, Dalian Minzu University , Dalian 116600, Liaoning, China.
[Ti] Título:Structural and Functional Analyses of Periplasmic 5'-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase from Aeromonas hydrophila.
[So] Source:Biochemistry;56(40):5347-5355, 2017 Oct 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Gram-negative, rod-shaped bacterium Aeromonas hydrophila has two multifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTAN) enzymes, MtaN-1 and MtaN-2, that differ from those in other bacteria. These proteins are essential for several metabolic pathways, including biological methylation, polyamine biosynthesis, methionine recycling, and bacterial quorum sensing. To gain insight into how these two proteins function, we determined four high-resolution crystal structures of MtaN-1 in its apo form and in complex with the substrates S-adenosyl-l-homocysteine, 5'-methylthioadenosine, and 5'-deoxyadenosine. We found that the domain structures were generally similar, although slight differences were evident. The crystal structure demonstrates that AhMtaN-1 has an extension of the binding pocket and revealed that a tryptophan in the active site (Trp199) may play a major role in substrate binding, unlike in other MTAN proteins. Mutation of the Trp199 residue completely abolished the enzyme activity. Trp199 was identified as an active site residue that is essential for catalysis. Furthermore, biochemical characterization of AhMtaN-1 and AhMtaN-2 demonstrated that AhMtaN-1 exhibits inherent trypsin resistance that is higher than that of AhMtaN-2. Additionally, the thermally unfolded AhMtaN-2 protein is capable of refolding into active forms, whereas the thermally unfolded AhMtaN-1 protein does not have this ability. Examining the different biochemical characteristics related to the functional roles of AhMtaN-1 and AhMtaN-2 would be interesting. Indeed, the biochemical characterization of these structural features would provide a structural basis for the design of new antibiotics against A. hydrophila.
[Mh] Termos MeSH primário: Aeromonas hydrophila/citologia
Aeromonas hydrophila/enzimologia
Desoxiadenosinas/metabolismo
N-Glicosil Hidrolases/química
N-Glicosil Hidrolases/metabolismo
Periplasma/enzimologia
Tionucleosídeos/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Domínio Catalítico
Modelos Moleculares
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Deoxyadenosines); 0 (Thionucleosides); 634Z2VK3UQ (5'-methylthioadenosine); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 3.2.2.9 (adenosylhomocysteine nucleosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00691


  2 / 3846 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


  3 / 3846 MEDLINE  
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[PMID]:28763516
[Au] Autor:Kwon E; Pathak D; Chang HW; Kim DY
[Ad] Endereço:College of Pharmacy, Yeungnam University, Gyeongsan, Gyeongbuk, South Korea.
[Ti] Título:Crystal structure of mimivirus uracil-DNA glycosylase.
[So] Source:PLoS One;12(8):e0182382, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytosine deamination induced by stresses or enzymatic catalysis converts deoxycytidine into deoxyuridine, thereby introducing a G to A mutation after DNA replication. Base-excision repair to correct uracil to cytosine is initiated by uracil-DNA glycosylase (UDG), which recognizes and eliminates uracil from DNA. Mimivirus, one of the largest known viruses, also encodes a distinctive UDG gene containing a long N-terminal domain (N-domain; residues 1-130) and a motif-I (residues 327-343), in addition to the canonical catalytic domain of family I UDGs (also called UNGs). To understand the structural and functional features of the additional segments, we have determined the crystal structure of UNG from Acanthamoeba polyphaga mimivirus (mvUNG). In the crystal structure of mvUNG, residues 95-130 in the N-domain bind to a hydrophobic groove in the catalytic domain, and motif-I forms a short ß-sheet with a positively charged surface near the active site. Circular dichroism spectra showed that residues 1-94 are in a random coil conformation. Deletion of the three additional fragments reduced the activity and thermal stability, compared to full-length mvUNG. The results suggested that the mvUNG N-domain and motif-I are required for its structural and functional integrity.
[Mh] Termos MeSH primário: Mimiviridae/enzimologia
Uracila-DNA Glicosidase/química
[Mh] Termos MeSH secundário: Acanthamoeba/virologia
Motivos de Aminoácidos
Domínio Catalítico
Dicroísmo Circular
Cristalografia por Raios X
DNA/química
Reparo do DNA
Deleção de Genes
Mimiviridae/genética
N-Glicosil Hidrolases/química
Estrutura Secundária de Proteína
Coloração pela Prata
Especificidade por Substrato
Uracila/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
56HH86ZVCT (Uracil); 9007-49-2 (DNA); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 3.2.2.- (Uracil-DNA Glycosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182382


  4 / 3846 MEDLINE  
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[PMID]:28575236
[Au] Autor:Bj Rås KØ; Sousa MML; Sharma A; Fonseca DM; S Gaard CK; Bj Rås M; Otterlei M
[Ad] Endereço:Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
[Ti] Título:Monitoring of the spatial and temporal dynamics of BER/SSBR pathway proteins, including MYH, UNG2, MPG, NTH1 and NEIL1-3, during DNA replication.
[So] Source:Nucleic Acids Res;45(14):8291-8301, 2017 Aug 21.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Base lesions in DNA can stall the replication machinery or induce mutations if bypassed. Consequently, lesions must be repaired before replication or in a post-replicative process to maintain genomic stability. Base excision repair (BER) is the main pathway for repair of base lesions and is known to be associated with DNA replication, but how BER is organized during replication is unclear. Here we coupled the iPOND (isolation of proteins on nascent DNA) technique with targeted mass-spectrometry analysis, which enabled us to detect all proteins required for BER on nascent DNA and to monitor their spatiotemporal orchestration at replication forks. We demonstrate that XRCC1 and other BER/single-strand break repair (SSBR) proteins are enriched in replisomes in unstressed cells, supporting a cellular capacity of post-replicative BER/SSBR. Importantly, we identify for the first time the DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA. Our findings suggest that a broad spectrum of DNA base lesions are recognized and repaired by BER in a post-replicative process.
[Mh] Termos MeSH primário: Quebras de DNA de Cadeia Simples
Enzimas Reparadoras do DNA/metabolismo
Reparo do DNA
Replicação do DNA
DNA/genética
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
DNA/metabolismo
DNA Glicosilases/metabolismo
DNA Liase (Sítios Apurínicos ou Apirimidínicos)/metabolismo
Proteínas de Ligação a DNA/metabolismo
Desoxirribonuclease (Dímero de Pirimidina)/metabolismo
Células HEK293
Células HeLa
Seres Humanos
Immunoblotting
Espectrometria de Massas/métodos
N-Glicosil Hidrolases/metabolismo
Transdução de Sinais/genética
Fatores de Tempo
Proteína 1 Complementadora Cruzada de Reparo de Raio-X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (X-ray Repair Cross Complementing Protein 1); 0 (XRCC1 protein, human); 9007-49-2 (DNA); EC 3.1.25.1 (Deoxyribonuclease (Pyrimidine Dimer)); EC 3.1.25.1 (NTHL1 protein, human); EC 3.2.2.- (CCNO protein, human); EC 3.2.2.- (DNA Glycosylases); EC 3.2.2.- (FLJ10858 protein, human); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 3.2.2.- (NEIL1 protein, human); EC 3.2.2.- (mutY adenine glycosylase); EC 3.2.2.21 (DNA-3-methyladenine glycosidase II); EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase); EC 4.2.99.18 (NEIL2 protein, human); EC 6.5.1.- (DNA Repair Enzymes)
[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:170603
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx476


  5 / 3846 MEDLINE  
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[PMID]:28378638
[Au] Autor:de Sousa JF; Torrieri R; Serafim RB; Di Cristofaro LF; Escanfella FD; Ribeiro R; Zanette DL; Paçó-Larson ML; da Silva WA; Tirapelli DP; Neder L; Carlotti CG; Valente V
[Ad] Endereço:1 Department of Clinical Analysis, Faculty of Pharmaceutical Sciences of Araraquara, University of São Paulo State, Araraquara, Brazil.
[Ti] Título:Expression signatures of DNA repair genes correlate with survival prognosis of astrocytoma patients.
[So] Source:Tumour Biol;39(4):1010428317694552, 2017 Apr.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Astrocytomas are the most common primary brain tumors. They are very resistant to therapies and usually progress rapidly to high-grade lesions. Here, we investigated the potential role of DNA repair genes in astrocytoma progression and resistance. To this aim, we performed a polymerase chain reaction array-based analysis focused on DNA repair genes and searched for correlations between expression patters and survival prognoses. We found 19 genes significantly altered. Combining these genes in all possible arrangements, we found 421 expression signatures strongly associated with poor survival. Importantly, five genes (DDB2, EXO1, NEIL3, BRCA2, and BRIP1) were independently correlated with worse prognoses, revealing single-gene signatures. Moreover, silencing of EXO1, which is remarkably overexpressed, promoted faster restoration of double-strand breaks, while NEIL3 knockdown, also highly overexpressed, caused an increment in DNA damage and cell death after irradiation of glioblastoma cells. These results disclose the importance of DNA repair pathways for the maintenance of genomic stability of high-grade astrocytomas and suggest that EXO1 and NEIL3 overexpression confers more efficiency for double-strand break repair and resistance to reactive oxygen species, respectively. Thereby, we highlight these two genes as potentially related with tumor aggressiveness and promising candidates as novel therapeutic targets.
[Mh] Termos MeSH primário: Astrocitoma/mortalidade
Neoplasias Encefálicas/mortalidade
Reparo do DNA
[Mh] Termos MeSH secundário: Apoptose
Astrocitoma/genética
Astrocitoma/metabolismo
Neoplasias Encefálicas/genética
Neoplasias Encefálicas/metabolismo
Ciclo Celular
Linhagem Celular Tumoral
Enzimas Reparadoras do DNA/genética
Enzimas Reparadoras do DNA/metabolismo
Exodesoxirribonucleases/genética
Exodesoxirribonucleases/metabolismo
Expressão Gênica
Seres Humanos
Estimativa de Kaplan-Meier
N-Glicosil Hidrolases/genética
N-Glicosil Hidrolases/metabolismo
Prognóstico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.- (EXO1 protein, human); EC 3.1.- (Exodeoxyribonucleases); EC 3.2.2.- (FLJ10858 protein, human); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 6.5.1.- (DNA Repair Enzymes)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170410
[Lr] Data última revisão:
170410
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317694552


  6 / 3846 MEDLINE  
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[PMID]:28262582
[Au] Autor:Yang Z; Nejad MI; Varela JG; Price NE; Wang Y; Gates KS
[Ad] Endereço:University of Missouri Department of Chemistry, 125 Chemistry Building Columbia, MO 65211, United States.
[Ti] Título:A role for the base excision repair enzyme NEIL3 in replication-dependent repair of interstrand DNA cross-links derived from psoralen and abasic sites.
[So] Source:DNA Repair (Amst);52:1-11, 2017 Apr.
[Is] ISSN:1568-7856
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Interstrand DNA-DNA cross-links are highly toxic lesions that are important in medicinal chemistry, toxicology, and endogenous biology. In current models of replication-dependent repair, stalling of a replication fork activates the Fanconi anemia pathway and cross-links are "unhooked" by the action of structure-specific endonucleases such as XPF-ERCC1 that make incisions flanking the cross-link. This process generates a double-strand break, which must be subsequently repaired by homologous recombination. Recent work provided evidence for a new, incision-independent unhooking mechanism involving intrusion of a base excision repair (BER) enzyme, NEIL3, into the world of cross-link repair. The evidence suggests that the glycosylase action of NEIL3 unhooks interstrand cross-links derived from an abasic site or the psoralen derivative trioxsalen. If the incision-independent NEIL3 pathway is blocked, repair reverts to the incision-dependent route. In light of the new model invoking participation of NEIL3 in cross-link repair, we consider the possibility that various BER glycosylases or other DNA-processing enzymes might participate in the unhooking of chemically diverse interstrand DNA cross-links.
[Mh] Termos MeSH primário: Adutos de DNA/metabolismo
Dano ao DNA
Reparo do DNA
Furocumarinas/metabolismo
N-Glicosil Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Animais
Reagentes para Ligações Cruzadas/toxicidade
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (DNA Adducts); 0 (Furocoumarins); 0 (psoralen-DNA adduct); EC 3.2.2.- (FLJ10858 protein, human); EC 3.2.2.- (N-Glycosyl Hydrolases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170916
[Lr] Data última revisão:
170916
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170307
[St] Status:MEDLINE


  7 / 3846 MEDLINE  
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[PMID]:28225907
[Au] Autor:Villela AD; Rodrigues VD; Pinto AF; Wink PL; Sánchez-Quitian ZA; Petersen GO; Campos MM; Basso LA; Santos DS
[Ad] Endereço:Pontifícia Universidade Católica do Rio Grande do Sul, Centro de Pesquisas em Biologia Molecular e Funcional, Instituto Nacional de Ciência e Tecnologia em Tuberculose, Porto Alegre, RS, Brasil.
[Ti] Título:Characterisation of iunH gene knockout strain from Mycobacterium tuberculosis.
[So] Source:Mem Inst Oswaldo Cruz;112(3):203-208, 2017 Mar.
[Is] ISSN:1678-8060
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Tuberculosis (TB) is an infectious disease caused mainly by the bacillus Mycobacterium tuberculosis. The better understanding of important metabolic pathways from M. tuberculosis can contribute to the development of novel therapeutic and prophylactic strategies to combat TB. Nucleoside hydrolase (MtIAGU-NH), encoded by iunH gene (Rv3393), is an enzyme from purine salvage pathway in M. tuberculosis. MtIAGU-NH accepts inosine, adenosine, guanosine, and uridine as substrates, which may point to a pivotal metabolic role. OBJECTIVES: Our aim was to construct a M. tuberculosis knockout strain for iunH gene, to evaluate in vitro growth and the effect of iunH deletion in M. tuberculosis in non-activated and activated macrophages models of infection. METHODS: A M. tuberculosis knockout strain for iunH gene was obtained by allelic replacement, using pPR27xylE plasmid. The complemented strain was constructed by the transformation of the knockout strain with pNIP40::iunH. MtIAGU-NH expression was analysed by Western blot and LC-MS/MS. In vitro growth was evaluated in Sauton's medium. Bacterial load of non-activated and interferon-γ activated RAW 264.7 cells infected with knockout strain was compared with wild-type and complemented strains. FINDINGS: Western blot and LC-MS/MS validated iunH deletion at protein level. The iunH knockout led to a delay in M. tuberculosis growth kinetics in Sauton's medium during log phase, but did not affect bases and nucleosides pool in vitro. No significant difference in bacterial load of knockout strain was observed when compared with both wild-type and complemented strains after infection of non-activated and interferon-γ activated RAW 264.7 cells. MAIN CONCLUSION: The disruption of iunH gene does not influence M. tuberculosis growth in both non-activated and activated RAW 264.7 cells, which show that iunH gene is not important for macrophage invasion and virulence. Our results indicated that MtIAGU-NH is not a target for drug development.
[Mh] Termos MeSH primário: Técnicas de Inativação de Genes
Genes Bacterianos
Mycobacterium tuberculosis/genética
N-Glicosil Hidrolases/genética
[Mh] Termos MeSH secundário: Seres Humanos
Macrófagos/microbiologia
Mycobacterium tuberculosis/enzimologia
Mycobacterium tuberculosis/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.2.- (N-Glycosyl Hydrolases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE


  8 / 3846 MEDLINE  
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[PMID]:28218438
[Au] Autor:Singh RK; Steyaert J; Versées W
[Ad] Endereço:Structural Biology Brussels, Vrije Universiteit Brussel (VUB), Pleinlaan 2, Brussels, 1050, Belgium.
[Ti] Título:Structural and biochemical characterization of the nucleoside hydrolase from C. elegans reveals the role of two active site cysteine residues in catalysis.
[So] Source:Protein Sci;26(5):985-996, 2017 May.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nucleoside hydrolases (NHs) catalyze the hydrolysis of the N-glycoside bond in ribonucleosides and are found in all three domains of life. Although in parasitic protozoa a role in purine salvage has been well established, their precise function in bacteria and higher eukaryotes is still largely unknown. NHs have been classified into three homology groups based on the conservation of active site residues. While many structures are available of representatives of group I and II, structural information for group III NHs is lacking. Here, we report the first crystal structure of a purine-specific nucleoside hydrolase belonging to homology group III from the nematode Caenorhabditis elegans (CeNH) to 1.65Å resolution. In contrast to dimeric purine-specific NHs from group II, CeNH is a homotetramer. A cysteine residue that characterizes group III NHs (Cys253) structurally aligns with the catalytic histidine and tryptophan residues of group I and group II enzymes, respectively. Moreover, a second cysteine (Cys42) points into the active site of CeNH. Substrate docking shows that both cysteine residues are appropriately positioned to interact with the purine ring. Site-directed mutagenesis and kinetic analysis proposes a catalytic role for both cysteines residues, with Cys253 playing the most prominent role in leaving group activation.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/química
Caenorhabditis elegans/enzimologia
N-Glicosil Hidrolases/química
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Domínio Catalítico
Cristalografia por Raios X
Cisteína
N-Glicosil Hidrolases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); EC 3.2.2.- (N-Glycosyl Hydrolases); K848JZ4886 (Cysteine)
[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:170221
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3141


  9 / 3846 MEDLINE  
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[PMID]:28010187
[Au] Autor:Klink VP; Sharma K; Pant SR; McNeece B; Niraula P; Lawrence GW
[Ad] Endereço:a Department of Biological Sciences , Mississippi State University , Mississippi State , MS , USA.
[Ti] Título:Components of the SNARE-containing regulon are co-regulated in root cells undergoing defense.
[So] Source:Plant Signal Behav;12(2):e1274481, 2017 Feb.
[Is] ISSN:1559-2324
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The term regulon has been coined in the genetic model plant Arabidopsis thaliana, denoting a structural and physiological defense apparatus defined genetically through the identification of the penetration (pen) mutants. The regulon is composed partially by the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) syntaxin PEN1. PEN1 has homology to a Saccharomyces cerevisae gene that regulates a Secretion (Sec) protein, Suppressor of Sec 1 (Sso1p). The regulon is also composed of the ß-glucosidase (PEN2) and an ATP binding cassette (ABC) transporter (PEN3). While important in inhibiting pathogen infection, limited observations have been made regarding the transcriptional regulation of regulon genes until now. Experiments made using the model agricultural Glycine max (soybean) have identified co-regulated gene expression of regulon components. The results explain the observation of hundreds of genes expressed specifically in the root cells undergoing the natural process of defense. Data regarding additional G. max genes functioning within the context of the regulon are presented here, including Sec 14, Sec 4 and Sec 23. Other examined G. max homologs of membrane fusion genes include an endosomal bromo domain-containing protein1 (Bro1), syntaxin6 (SYP6), SYP131, SYP71, SYP8, Bet1, coatomer epsilon (ϵ-COP), a coatomer zeta (ζ-COP) paralog and an ER to Golgi component (ERGIC) protein. Furthermore, the effectiveness of biochemical pathways that would function within the context of the regulon ave been examined, including xyloglucan xylosyltransferase (XXT), reticuline oxidase (RO) and galactinol synthase (GS). The experiments have unveiled the importance of the regulon during defense in the root and show how the deposition of callose relates to the process.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/genética
Transportadores de Cassetes de Ligação de ATP/metabolismo
Arabidopsis/genética
Proteínas de Arabidopsis/genética
Galactosiltransferases/genética
Galactosiltransferases/metabolismo
Glucanos/metabolismo
N-Glicosil Hidrolases/genética
N-Glicosil Hidrolases/metabolismo
Oxirredutases N-Desmetilantes/genética
Oxirredutases N-Desmetilantes/metabolismo
Pentosiltransferases/genética
Pentosiltransferases/metabolismo
Raízes de Plantas/genética
Raízes de Plantas/metabolismo
Regulon/genética
Proteínas SNARE/genética
Proteínas SNARE/metabolismo
Feijão de Soja/genética
Feijão de Soja/metabolismo
beta-Glucosidase/genética
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Glucans); 0 (PDR8 protein, Arabidopsis); 0 (SNARE Proteins); 9064-51-1 (callose); EC 1.21.3.3 (reticuline oxidase); EC 1.5.- (Oxidoreductases, N-Demethylating); EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.123 (inositol 1-alpha-galactosyltransferase); EC 2.4.2.- (Pentosyltransferases); EC 2.4.2.- (xyloglucan xylosyltransferase); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.2.- (N-Glycosyl Hydrolases); EC 3.2.2.- (PEN2 protein, Arabidopsis)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE
[do] DOI:10.1080/15592324.2016.1274481


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[PMID]:27939867
[Au] Autor:Figueroa-Villar JD; Sales EM
[Ad] Endereço:Medicinal Chemistry Group, Department of Chemistry, Military Institute of Engineering, Praça General Tibúrcio 80, 22290-270 Rio de Janeiro, Brazil. Electronic address: jdfv2009@gmail.com.
[Ti] Título:The importance of nucleoside hydrolase enzyme (NH) in studies to treatment of Leishmania: A review.
[So] Source:Chem Biol Interact;263:18-27, 2017 Feb 01.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Leishmania is a genus of trypanosomes, which are responsible for leishmaniasis disease, a major trypanosome infection in humans. In recent years, published studies have shown that the search for new drugs for Leishmania treatments has intensified. Through technique modeling it has been possible to develop new compounds, which act as nucleoside hydrolase (NH) inhibitors. The effect of these enzymes is the hydrolysis of certain RNA nucleotides, which include uridine and inosine, necessary for the protozoa to transform certain nucleosides obtained from infected individuals into nucleobases for the preparation of their DNA. The obtention of NH inhibitors is very important to eliminate leishmaniasis disease in infected individuals. The aim of this study is to discuss the research and development of new agents for the treatment of Leishmania, and to stimulate the formulation of new NH inhibitors.
[Mh] Termos MeSH primário: Leishmania/enzimologia
N-Glicosil Hidrolases/metabolismo
Proteínas de Protozoários/metabolismo
[Mh] Termos MeSH secundário: Animais
Domínio Catalítico
Inibidores Enzimáticos/química
Inibidores Enzimáticos/metabolismo
Seres Humanos
Leishmaniose/tratamento farmacológico
Leishmaniose/parasitologia
Conformação Molecular
Simulação de Acoplamento Molecular
N-Glicosil Hidrolases/antagonistas & inibidores
Proteínas de Protozoários/antagonistas & inibidores
Ribitol/análogos & derivados
Ribitol/química
Ribitol/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Protozoan Proteins); 0 (phenyliminoribitol); 488-81-3 (Ribitol); EC 3.2.2.- (N-Glycosyl Hydrolases)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170201
[Lr] Data última revisão:
170201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE



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