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Registro Completo |
Biblioteca(s): |
Embrapa Agricultura Digital. |
Data corrente: |
26/11/2009 |
Data da última atualização: |
15/01/2020 |
Tipo da produção científica: |
Resumo em Anais de Congresso |
Autoria: |
CAMINHA, I. P.; FALCÃO, P. K.; TEIXEIRA, K. R. |
Afiliação: |
ISABEL PEREIRA CAMINHA, Estagiária/CNPTIA; PAULA REGINA KUSER FALCAO, CNPTIA; KATIA REGINA DOS SANTOS TEIXEIRA, CNPAB. |
Título: |
Structural studies of Gluconate 5-dehydrogenase from gluconacetobacter diazotrophicus. |
Ano de publicação: |
2009 |
Fonte/Imprenta: |
In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. |
Páginas: |
Não paginado. |
Idioma: |
Inglês |
Notas: |
X-Meeting 2009. |
Conteúdo: |
The recent sequencing of the Gluconacetobacter diazotrophicus genome, developed by Projeto RioGene, permits a search by ORFs related to organic acid production. In this study, a putative Gluconate 5-dehydrogenase (Ga5DH) ORF, A9H995, was selected. Ga5DH is an enzyme that plays an important role in regulating the flux of carbon and energy source in bacteria, and in the production of organic acids, among them the 5-keto-D-Gluconate (5KGA). Due to the fundamental role of this acid in the chemical industry, like the precursor to tartaric acid production for example, there is a large interest in respect to the structure of this protein since there is little physical or structural information available about it. To this end, we herein report the theoretical structure of Ga5DH from Gluconacetobacter diazotrophicus. This structure was obtained through in silico studies if the three-dimensional structure generated by homology modelling. The sequence alignment program BLAST was used to search homologous sequences against the Protein Data Bank (PDB), and the best template was chosen according to the sequence identity (ID). The reference structure used was the crystal structure of Ga5DH from Streptococcus suis species (PDB 3cxr:A). This protein wich belongs to the family of short-chain dehydrogenases/reductases (SDR), presented 42% identity with Ga5DH from G. diazotrophicus. By using the programa MODELLER9v6, ten models were built and the best model was determined by the lowest value of objective function. LIGPLOT was used to identify the interactions with possible ligants of this enzyme. A comparative analysis shows that the residues from S. Suis which are involved in ligand binding (GKR D-glucarate and NAP NADP Nicotinamide-adenine-dinucleotide-phosphate) are conserved both sequentially and structurally. This may suggests that the target sequence has the same ligands. Molecular dynamics simulations were performed with GROMACS software package. The residues involved in the interaction with the substrate were replaced by alanine, and the model with mutated amino acids was further submitted to molecular dynamics simulations to gain insights into affinities, contacts and stability of the essencial amino acids for structure and function of this enzyme, as well as information on the binding profile. MenosThe recent sequencing of the Gluconacetobacter diazotrophicus genome, developed by Projeto RioGene, permits a search by ORFs related to organic acid production. In this study, a putative Gluconate 5-dehydrogenase (Ga5DH) ORF, A9H995, was selected. Ga5DH is an enzyme that plays an important role in regulating the flux of carbon and energy source in bacteria, and in the production of organic acids, among them the 5-keto-D-Gluconate (5KGA). Due to the fundamental role of this acid in the chemical industry, like the precursor to tartaric acid production for example, there is a large interest in respect to the structure of this protein since there is little physical or structural information available about it. To this end, we herein report the theoretical structure of Ga5DH from Gluconacetobacter diazotrophicus. This structure was obtained through in silico studies if the three-dimensional structure generated by homology modelling. The sequence alignment program BLAST was used to search homologous sequences against the Protein Data Bank (PDB), and the best template was chosen according to the sequence identity (ID). The reference structure used was the crystal structure of Ga5DH from Streptococcus suis species (PDB 3cxr:A). This protein wich belongs to the family of short-chain dehydrogenases/reductases (SDR), presented 42% identity with Ga5DH from G. diazotrophicus. By using the programa MODELLER9v6, ten models were built and the best model was determined by the lowest value of... Mostrar Tudo |
Palavras-Chave: |
Bioinformática; BLAST; GROMACS; Modelagem. |
Thesagro: |
Genoma; Proteína; Simulação. |
Thesaurus Nal: |
Bioinformatics; Models. |
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
Marc: |
LEADER 03173nam a2200265 a 4500 001 1576243 005 2020-01-15 008 2009 bl uuuu u00u1 u #d 100 1 $aCAMINHA, I. P. 245 $aStructural studies of Gluconate 5-dehydrogenase from gluconacetobacter diazotrophicus.$h[electronic resource] 260 $aIn: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB$c2009 300 $aNão paginado. 500 $aX-Meeting 2009. 520 $aThe recent sequencing of the Gluconacetobacter diazotrophicus genome, developed by Projeto RioGene, permits a search by ORFs related to organic acid production. In this study, a putative Gluconate 5-dehydrogenase (Ga5DH) ORF, A9H995, was selected. Ga5DH is an enzyme that plays an important role in regulating the flux of carbon and energy source in bacteria, and in the production of organic acids, among them the 5-keto-D-Gluconate (5KGA). Due to the fundamental role of this acid in the chemical industry, like the precursor to tartaric acid production for example, there is a large interest in respect to the structure of this protein since there is little physical or structural information available about it. To this end, we herein report the theoretical structure of Ga5DH from Gluconacetobacter diazotrophicus. This structure was obtained through in silico studies if the three-dimensional structure generated by homology modelling. The sequence alignment program BLAST was used to search homologous sequences against the Protein Data Bank (PDB), and the best template was chosen according to the sequence identity (ID). The reference structure used was the crystal structure of Ga5DH from Streptococcus suis species (PDB 3cxr:A). This protein wich belongs to the family of short-chain dehydrogenases/reductases (SDR), presented 42% identity with Ga5DH from G. diazotrophicus. By using the programa MODELLER9v6, ten models were built and the best model was determined by the lowest value of objective function. LIGPLOT was used to identify the interactions with possible ligants of this enzyme. A comparative analysis shows that the residues from S. Suis which are involved in ligand binding (GKR D-glucarate and NAP NADP Nicotinamide-adenine-dinucleotide-phosphate) are conserved both sequentially and structurally. This may suggests that the target sequence has the same ligands. Molecular dynamics simulations were performed with GROMACS software package. The residues involved in the interaction with the substrate were replaced by alanine, and the model with mutated amino acids was further submitted to molecular dynamics simulations to gain insights into affinities, contacts and stability of the essencial amino acids for structure and function of this enzyme, as well as information on the binding profile. 650 $aBioinformatics 650 $aModels 650 $aGenoma 650 $aProteína 650 $aSimulação 653 $aBioinformática 653 $aBLAST 653 $aGROMACS 653 $aModelagem 700 1 $aFALCÃO, P. K. 700 1 $aTEIXEIRA, K. R.
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Embrapa Agricultura Digital (CNPTIA) |
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Biblioteca(s): |
Embrapa Amapá. |
Data corrente: |
20/03/2023 |
Data da última atualização: |
20/03/2023 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 2 |
Autoria: |
TAVARES-DIAS, M.; OLIVEIRA, M. S. B. |
Afiliação: |
MARCOS TAVARES DIAS, CPAF-AP; MARCOS S. B. OLIVEIRA, UNIVERSIDADE FEDERAL DO AMAPÁ. |
Título: |
Global distribution patterns of Caligus Müller, 1785 (Copepoda: Caligidae) associated to teleost fishes, with physiological and histopathological data and description of treatment strategies. |
Ano de publicação: |
2023 |
Fonte/Imprenta: |
Anais da Academia Brasileira de Ciências, v. 95, n. 1, e20220281, 2023. |
DOI: |
10.1590/0001-3765202320220281 |
Idioma: |
Inglês |
Conteúdo: |
This review surveyed information on Caligus Müller, 1785 to identify global infestation patterns and geographic distribution in teleost fishes, as well as physiological and histopathological data and description of treatment strategies. A total 990 samples of Caligus spp. (N = 212 species) obtained of 233 scientific papers on farmed and wild teleost species from 99 families and 30 orders were used, and the highest number of occurrences was on Carangidae. Caligus spp. was predominantly found in marine environments, and only Caligus lacustris and Caligus epidemicus were found in teleost fish of freshwater environments. There was a high prevalence of Caligus spp. on hosts and infestation occurred predominantly in both the tegument and the gills. Caligus species are distributed across different countries and some particularities were identified and discussed. Caligus elongatus and Caligus bonito bonito had the broadest geographic distribution. Histomorphological and hematological disorders caused by infestation by Caligus spp. were reported and discussed, as well as chemotherapeutic products used for controlling and treating the infestations. Variation in the distribution and geographic patterns of Caligus spp. were little evident in many ecosystems and due to the limited data on the infestation of these sea lice on teleost populations in different regions. |
Palavras-Chave: |
Infestation; Parasita. |
Thesagro: |
Crustáceo; Infestação. |
Thesaurus NAL: |
Caligus; Crustacean culture; Ectoparasites. |
Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1152511/1/CPAF-AP-2023-Global-distribution-patterns-of-Caligus-Muller.pdf
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Marc: |
LEADER 02174naa a2200229 a 4500 001 2152511 005 2023-03-20 008 2023 bl uuuu u00u1 u #d 024 7 $a10.1590/0001-3765202320220281$2DOI 100 1 $aTAVARES-DIAS, M. 245 $aGlobal distribution patterns of Caligus Müller, 1785 (Copepoda$bCaligidae) associated to teleost fishes, with physiological and histopathological data and description of treatment strategies.$h[electronic resource] 260 $c2023 520 $aThis review surveyed information on Caligus Müller, 1785 to identify global infestation patterns and geographic distribution in teleost fishes, as well as physiological and histopathological data and description of treatment strategies. A total 990 samples of Caligus spp. (N = 212 species) obtained of 233 scientific papers on farmed and wild teleost species from 99 families and 30 orders were used, and the highest number of occurrences was on Carangidae. Caligus spp. was predominantly found in marine environments, and only Caligus lacustris and Caligus epidemicus were found in teleost fish of freshwater environments. There was a high prevalence of Caligus spp. on hosts and infestation occurred predominantly in both the tegument and the gills. Caligus species are distributed across different countries and some particularities were identified and discussed. Caligus elongatus and Caligus bonito bonito had the broadest geographic distribution. Histomorphological and hematological disorders caused by infestation by Caligus spp. were reported and discussed, as well as chemotherapeutic products used for controlling and treating the infestations. Variation in the distribution and geographic patterns of Caligus spp. were little evident in many ecosystems and due to the limited data on the infestation of these sea lice on teleost populations in different regions. 650 $aCaligus 650 $aCrustacean culture 650 $aEctoparasites 650 $aCrustáceo 650 $aInfestação 653 $aInfestation 653 $aParasita 700 1 $aOLIVEIRA, M. S. B. 773 $tAnais da Academia Brasileira de Ciências$gv. 95, n. 1, e20220281, 2023.
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