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Pesquisa : D08.811.682.047.150.250 [Categoria DeCS]
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[PMID]:26821257
[Au] Autor:Kianmehr A; Mahrooz A; Ansari J; Oladnabi M; Shahbazmohammadi H
[Ad] Endereço:Biochemistry and Metabolic Disorders Research Center, Golestan University of Medical Sciences, Gorgan, Iran.
[Ti] Título:The Rapid and Sensitive Quantitative Determination of Galactose by Combined Enzymatic and Colorimetric Method: Application in Neonatal Screening.
[So] Source:Appl Biochem Biotechnol;179(2):283-93, 2016 May.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The quantitative measurement of galactose in blood is essential for the early diagnosis, treatment, and dietary monitoring of galactosemia patients. In this communication, we aimed to develop a rapid, sensitive, and cost-effective combined method for galactose determination in dry blood spots. This procedure was based on the combination of enzymatic reactions of galactose dehydrogenase (GalDH), dihydrolipoyl dehydrogenase (DLD), and alkaline phosphates with a colorimetric system. The incubation time and the concentration of enzymes used in new method were also optimized. The analytical performance was studied by the precision, recovery, linearity, and sensitivity parameters. Statistical analysis was applied to method comparison experiment. The regression equation and correlation coefficient (R (2)) were Y = 0.0085x + 0.032 and R (2) = 0.998, respectively. This assay exhibited a recovery in the range of 91.7-114.3 % and had the limit detection of 0.5 mg/dl for galactose. The between-run coefficient of variation (CV) was between 2.6 and 11.1 %. The within-run CV was between 4.9 and 9.2 %. Our results indicated that the new and reference methods were in agreement because no significant biases exist between them. Briefly, a quick and reliable combined enzymatic and colorimetric assay was presented for application in newborn mass screening and monitoring of galactosemia patients.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Galactose/sangue
Galactosemias/sangue
Triagem Neonatal
[Mh] Termos MeSH secundário: Colorimetria/métodos
Enzimas Imobilizadas/química
Galactose Desidrogenases/química
Galactosemias/patologia
Seres Humanos
Recém-Nascido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); EC 1.1.1.- (Galactose Dehydrogenases); EC 1.1.1.48 (galactose dehydrogenase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170116
[Lr] Data última revisão:
170116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160129
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-016-1993-z


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[PMID]:26040113
[Au] Autor:Azar SR; Naiebi R; Homami A; Akbari Z; Kianmehr A; Mahdizadehdehosta R; Najafzadeh F
[Ti] Título:Expression and response surface optimization of the recovery and purification of recombinant D-galactose dehydrogenase from Pseudomonas fluorescens.
[So] Source:Indian J Biochem Biophys;52(1):68-74, 2015 Feb.
[Is] ISSN:0301-1208
[Cp] País de publicação:India
[La] Idioma:eng
[Ab] Resumo:The enzyme D-galactose dehydrogenase (GalDH) has been used in diagnostic kits to screen blood serum of neonates for galactosemia. It is also a significant tool for the measurement of ß-D-galactose, α-D-galactose and lactose as well. In this study, response surface methodology (RSM) was used to identify the suitable conditions for recovery of recombinant GalDH from Pseudomonas fluorescens in aqueous two-phase systems (ATPS). The identified GalDH gene was amplified by PCR and confirmed by further cloning and sequencing. E. coli BL-21 (DE3) containing the GalDH gene on a plasmid (pET28aGDH) was used to express and purify the recombinant enzyme. The polyethylene glycol (PEG) and ammonium sulfate concentrations and pH value were selected as variables to analyze purification of GalDH. To build mathematical models, RSM with a central composite design was applied based on the conditions for the highest separation. The recombinant GalDH enzyme was expressed after induction with IPTG. It showed NAD'-dependent dehydrogenase activity towards D-Galactose. According to the RSM modeling, an optimal ATPS was composed of PEG-2000 14.0% (w/w) and ammonium sulfate 12.0% (w/w) at pH 7.5. Under these conditions, GalDH preferentially concentrated in the top PEG-rich phase. The enzyme activity, purification factor (PF) and recovery (R) were 1400 U/ml, 60.0% and 270.0%, respectively. The PEG and salt concentrations were found to have significant effect on the recovery of enzyme. Briefly, our data showed that RSM could be an appropriate tool to define the best ATPS for recombinant P. fluorescens GalDH recovery.
[Mh] Termos MeSH primário: Galactose Desidrogenases/isolamento & purificação
Pseudomonas fluorescens/enzimologia
[Mh] Termos MeSH secundário: Sequência de Bases
Primers do DNA
Galactose Desidrogenases/metabolismo
Reação em Cadeia da Polimerase
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); 0 (Recombinant Proteins); EC 1.1.1.- (Galactose Dehydrogenases); EC 1.1.1.48 (galactose dehydrogenase)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:150604
[Lr] Data última revisão:
150604
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150605
[St] Status:MEDLINE


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[PMID]:25591389
[Au] Autor:Shahbaz Mohammadi H; Mostafavi SS; Soleimani S; Bozorgian S; Pooraskari M; Kianmehr A
[Ad] Endereço:Department of Biochemistry, Genetic and Metabolism Research Group, Pasteur Institute of Iran, Tehran 13164, Iran; Department of Marine Biology, Islamic Azad University, Bandar Abbas Branch, Bandar Abbas, Iran.
[Ti] Título:Response surface methodology to optimize partition and purification of two recombinant oxidoreductase enzymes, glucose dehydrogenase and d-galactose dehydrogenase in aqueous two-phase systems.
[So] Source:Protein Expr Purif;108:41-47, 2015 Apr.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oxidoreductases are an important family of enzymes that are used in many biotechnological processes. An experimental design was applied to optimize partition and purification of two recombinant oxidoreductases, glucose dehydrogenase (GDH) from Bacillus subtilis and d-galactose dehydrogenase (GalDH) from Pseudomonas fluorescens AK92 in aqueous two-phase systems (ATPS). Response surface methodology (RSM) with a central composite rotatable design (CCRD) was performed to optimize critical factors like polyethylene glycol (PEG) concentration, concentration of salt and pH value. The best partitioning conditions was achieved in an ATPS composed of 12% PEG-6000, 15% K2HPO4 with pH 7.5 at 25°C, which ensured partition coefficient (KE) of 66.6 and 45.7 for GDH and GalDH, respectively. Under these experimental conditions, the activity of GDH and GalDH was 569.5U/ml and 673.7U/ml, respectively. It was found that these enzymes preferentially partitioned into the top PEG-rich phase and appeared as single bands on SDS-PAGE gel. Meanwhile the validity of the response model was confirmed by a good agreement between predicted and experimental results. Collectively, according to the obtained data it can be inferred that the ATPS optimization using RSM approach can be applied for recovery and purification of any enzyme from oxidoreductase family.
[Mh] Termos MeSH primário: Bacillus subtilis/enzimologia
Proteínas de Bactérias
Galactose Desidrogenases
Glucose 1-Desidrogenase
Pseudomonas fluorescens/enzimologia
[Mh] Termos MeSH secundário: Bacillus subtilis/genética
Proteínas de Bactérias/biossíntese
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/isolamento & purificação
Galactose Desidrogenases/biossíntese
Galactose Desidrogenases/química
Galactose Desidrogenases/genética
Galactose Desidrogenases/isolamento & purificação
Glucose 1-Desidrogenase/biossíntese
Glucose 1-Desidrogenase/química
Glucose 1-Desidrogenase/genética
Glucose 1-Desidrogenase/isolamento & purificação
Pseudomonas fluorescens/genética
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); EC 1.1.1.- (Galactose Dehydrogenases); EC 1.1.1.47 (Glucose 1-Dehydrogenase); EC 1.1.1.48 (galactose dehydrogenase)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150117
[St] Status:MEDLINE


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[PMID]:25387133
[Au] Autor:Geddes BA; González JE; Oresnik IJ
[Ti] Título:Exopolysaccharide production in response to medium acidification is correlated with an increase in competition for nodule occupancy.
[So] Source:Mol Plant Microbe Interact;27(12):1307-17, 2014 Dec.
[Is] ISSN:0894-0282
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sinorhizobium meliloti strains unable to utilize galactose as a sole carbon source, due to mutations in the De-Ley Doudoroff pathway (dgoK), were previously shown to be more competitive for nodule occupancy. In this work, we show that strains carrying this mutation have galactose-dependent exopolysaccharide (EPS) phenotypes that were manifested as aberrant Calcofluor staining as well as decreased mucoidy when in an expR(+) genetic background. The aberrant Calcofluor staining was correlated with changes in the pH of the growth medium. Strains carrying dgoK mutations were subsequently demonstrated to show earlier acidification of their growth medium that was correlated with an increase expression of genes associated with succinoglycan biosynthesis as well as increased accumulation of high and low molecular weight EPS in the medium. In addition, it was shown that the acidification of the medium was dependent on the inability of S. meliloti strains to initiate the catabolism of galactose. To more fully understand why strains carrying the dgoK allele were more competitive for nodule occupancy, early nodulation phenotypes were investigated. It was found that strains carrying the dgoK allele had a faster rate of nodulation. In addition, nodule competition experiments using genetic backgrounds unable to synthesize either succinoglycan or EPSII were consistent with the hypothesis that the increased competition phenotype was dependent upon the synthesis of succinoglycan. Fluorescent microscopy experiments on infected root-hair cells, using the acidotropic dye Lysotracker Red DND-99, provide evidence that the colonized curled root hair is an acidic compartment.
[Mh] Termos MeSH primário: Medicago sativa/microbiologia
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Polissacarídeos Bacterianos/metabolismo
Nódulos Radiculares de Plantas/microbiologia
Sinorhizobium meliloti/fisiologia
[Mh] Termos MeSH secundário: Aminas
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Benzenossulfonatos
Corantes Fluorescentes
Galactose/genética
Galactose/metabolismo
Galactose Desidrogenases/genética
Galactose Desidrogenases/metabolismo
Genes Reporter
Concentração de Íons de Hidrogênio
Medicago sativa/citologia
Mutação
Fenótipo
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Raízes de Plantas/citologia
Raízes de Plantas/microbiologia
Nódulos Radiculares de Plantas/citologia
Plântulas/citologia
Plântulas/microbiologia
Sinorhizobium meliloti/citologia
Sinorhizobium meliloti/genética
Sinorhizobium meliloti/crescimento & desenvolvimento
Simbiose
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Amines); 0 (Bacterial Proteins); 0 (Benzenesulfonates); 0 (EPSI polysaccharide); 0 (Fluorescent Dyes); 0 (Polysaccharides, Bacterial); 0 (Red DND-99); 73667-50-2 (succinoglycan); 7S9P0Y4313 (C.I. Fluorescent Brightening Agent 28); EC 1.1.1.- (Galactose Dehydrogenases); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.58 (2-dehydro-3-deoxygalactonokinase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141112
[St] Status:MEDLINE
[do] DOI:10.1094/MPMI-06-14-0168-R


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[PMID]:25236800
[Au] Autor:Aro-Kärkkäinen N; Toivari M; Maaheimo H; Ylilauri M; Pentikäinen OT; Andberg M; Oja M; Penttilä M; Wiebe MG; Ruohonen L; Koivula A
[Ad] Endereço:VTT, Technical Research Centre of Finland, P.O. Box 1000, 02044, Espoo, Finland.
[Ti] Título:L-arabinose/D-galactose 1-dehydrogenase of Rhizobium leguminosarum bv. trifolii characterised and applied for bioconversion of L-arabinose to L-arabonate with Saccharomyces cerevisiae.
[So] Source:Appl Microbiol Biotechnol;98(23):9653-65, 2014 Dec.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Four potential dehydrogenases identified through literature and bioinformatic searches were tested for L-arabonate production from L-arabinose in the yeast Saccharomyces cerevisiae. The most efficient enzyme, annotated as a D-galactose 1-dehydrogenase from the pea root nodule bacterium Rhizobium leguminosarum bv. trifolii, was purified from S. cerevisiae as a homodimeric protein and characterised. We named the enzyme as a L-arabinose/D-galactose 1-dehydrogenase (EC 1.1.1.-), Rl AraDH. It belongs to the Gfo/Idh/MocA protein family, prefers NADP(+) but uses also NAD(+) as a cofactor, and showed highest catalytic efficiency (k cat/K m) towards L-arabinose, D-galactose and D-fucose. Based on nuclear magnetic resonance (NMR) and modelling studies, the enzyme prefers the α-pyranose form of L-arabinose, and the stable oxidation product detected is L-arabino-1,4-lactone which can, however, open slowly at neutral pH to a linear L-arabonate form. The pH optimum for the enzyme was pH 9, but use of a yeast-in-vivo-like buffer at pH 6.8 indicated that good catalytic efficiency could still be expected in vivo. Expression of the Rl AraDH dehydrogenase in S. cerevisiae, together with the galactose permease Gal2 for L-arabinose uptake, resulted in production of 18 g of L-arabonate per litre, at a rate of 248 mg of L-arabonate per litre per hour, with 86 % of the provided L-arabinose converted to L-arabonate. Expression of a lactonase-encoding gene from Caulobacter crescentus was not necessary for L-arabonate production in yeast.
[Mh] Termos MeSH primário: Arabinose/metabolismo
Galactose Desidrogenases/metabolismo
Rhizobium leguminosarum/enzimologia
Saccharomyces cerevisiae/metabolismo
Açúcares Ácidos/metabolismo
[Mh] Termos MeSH secundário: Clonagem Molecular
Coenzimas/metabolismo
Estabilidade Enzimática
Galactose Desidrogenases/química
Galactose Desidrogenases/genética
Galactose Desidrogenases/isolamento & purificação
Expressão Gênica
Concentração de Íons de Hidrogênio
Cinética
Dados de Sequência Molecular
NAD/metabolismo
NADP/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Rhizobium leguminosarum/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Coenzymes); 0 (Recombinant Proteins); 0 (Sugar Acids); 0U46U6E8UK (NAD); 53-59-8 (NADP); B40ROO395Z (Arabinose); EC 1.1.1.- (Galactose Dehydrogenases); EC 1.1.1.48 (galactose dehydrogenase)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:141114
[Lr] Data última revisão:
141114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140920
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-014-6039-2


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[PMID]:24963813
[Au] Autor:Hobbs ME; Williams HJ; Hillerich B; Almo SC; Raushel FM
[Ad] Endereço:Department of Biochemistry and Biophysics, §Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.
[Ti] Título:l-Galactose metabolism in Bacteroides vulgatus from the human gut microbiota.
[So] Source:Biochemistry;53(28):4661-70, 2014 Jul 22.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A previously unknown metabolic pathway for the utilization of l-galactose was discovered in a prevalent gut bacterium, Bacteroides vulgatus. The new pathway consists of three previously uncharacterized enzymes that were found to be responsible for the conversion of l-galactose to d-tagaturonate. Bvu0219 (l-galactose dehydrogenase) was determined to oxidize l-galactose to l-galactono-1,5-lactone with kcat and kcat/Km values of 21 s(-1) and 2.0 × 10(5) M(-1) s(-1), respectively. The kinetic product of Bvu0219 is rapidly converted nonenzymatically to the thermodynamically more stable l-galactono-1,4-lactone. Bvu0220 (l-galactono-1,5-lactonase) hydrolyzes both the kinetic and thermodynamic products of Bvu0219 to l-galactonate. However, l-galactono-1,5-lactone is estimated to be hydrolyzed 300-fold faster than its thermodynamically more stable counterpart, l-galactono-1,4-lactone. In the final step of this pathway, Bvu0222 (l-galactonate dehydrogenase) oxidizes l-galactonate to d-tagaturonate with kcat and kcat/Km values of 0.6 s(-1) and 1.7 × 10(4) M(-1) s(-1), respectively. In the reverse direction, d-tagaturonate is reduced to l-galactonate with values of kcat and kcat/Km of 90 s(-1) and 1.6 × 10(5) M(-1) s(-1), respectively. d-Tagaturonate is subsequently converted to d-glyceraldehyde and pyruvate through enzymes encoded within the degradation pathway for d-glucuronate and d-galacturonate.
[Mh] Termos MeSH primário: Bacteroides/metabolismo
Galactose/metabolismo
Intestinos/microbiologia
Microbiota
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Bacteroides/genética
Galactose/genética
Galactose Desidrogenases/genética
Galactose Desidrogenases/metabolismo
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 1.1.1.- (Galactose Dehydrogenases); EC 1.1.1.48 (galactose dehydrogenase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140626
[St] Status:MEDLINE
[do] DOI:10.1021/bi500656m


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[PMID]:23820824
[Au] Autor:Liu H; Ramos KR; Valdehuesa KN; Nisola GM; Malihan LB; Lee WK; Park SJ; Chung WJ
[Ad] Endereço:Department of Energy and Biotechnology, Energy and Environment Fusion Technology Center (E2FTC), Myongji University, 116 Myongji-ro, Cheoin-gu, Yongin-si, Gyeonggi-do, 449-728, Republic of Korea.
[Ti] Título:Metabolic engineering of Escherichia coli for biosynthesis of D-galactonate.
[So] Source:Bioprocess Biosyst Eng;37(3):383-91, 2014 Mar.
[Is] ISSN:1615-7605
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:D-galactose is an attractive substrate for bioconversion. Herein, Escherichia coli was metabolically engineered to convert D-galactose into D-galactonate, a valuable compound in the polymer and cosmetic industries. D-galactonate productions by engineered E. coli strains were observed in shake flask cultivations containing 2 g L(-1) D-galactose. Engineered E. coli expressing gld coding for galactose dehydrogenase from Pseudomonas syringae was able to produce 0.17 g L(-1) D-galactonate. Inherent metabolic pathways for assimilating both D-galactose and D-galactonate were blocked to enhance the production of D-galactonate. This approach finally led to a 7.3-fold increase with D-galactonate concentration of 1.24 g L(-1) and yield of 62.0 %. Batch fermentation in 20 g L(-1) D-galactose of E. coli ∆galK∆dgoK mutant expressing the gld resulted in 17.6 g L(-1) of D-galactonate accumulation and highest yield of 88.1 %. Metabolic engineering strategy developed in this study could be useful for industrial production of D-galactonate.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Açúcares Ácidos/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Clonagem Molecular
Meios de Cultura
Primers do DNA
Escherichia coli/genética
Galactose Desidrogenases/genética
Concentração de Íons de Hidrogênio
Espectroscopia de Ressonância Magnética
Estrutura Molecular
Pseudomonas syringae/enzimologia
Açúcares Ácidos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Culture Media); 0 (DNA Primers); 0 (Sugar Acids); 13382-27-9 (galactonic acid); EC 1.1.1.- (Galactose Dehydrogenases); EC 1.1.1.48 (galactose dehydrogenase)
[Em] Mês de entrada:1412
[Cu] Atualização por classe:140327
[Lr] Data última revisão:
140327
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130704
[St] Status:MEDLINE
[do] DOI:10.1007/s00449-013-1003-6


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[PMID]:23832214
[Au] Autor:Momma M; Fujimoto Z
[Ad] Endereço:Biomolecular Research Unit, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba 305-8602, Japan. momma@affrc.go.jp
[Ti] Título:Expression, crystallization and preliminary X-ray analysis of rice L-galactose dehydrogenase.
[So] Source:Acta Crystallogr Sect F Struct Biol Cryst Commun;69(Pt 7):809-11, 2013 Jul.
[Is] ISSN:1744-3091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In plants, L-galactose dehydrogenase (L-GalDH) is a key enzyme in the biosynthesis of ascorbic acid (AsA), which is well known as a unique antioxidant compound and a cofactor for many enzymes. L-GalDH catalyses the oxidation of L-galactose to L-galactono-1,4-lactone. Rice L-GalDH was overexpressed in Escherichia coli, purified and crystallized. Diffraction-quality rod-shaped crystals were grown using a sitting-drop vapour-diffusion method. The L-GalDH crystals exhibited the symmetry of space group P21 and diffracted to a resolution of 1.2 Å. The crystals had unit-cell parameters a = 46.8, b = 54.9, c = 56.9 Å, ß = 102.3°. On the basis of the Matthews coefficient (VM = 2.1 Å(3) Da(-1), solvent content of 42.3%), it was estimated that one peptide was present in the asymmetric unit.
[Mh] Termos MeSH primário: Galactose Desidrogenases/química
Oryza/enzimologia
Proteínas Recombinantes/química
[Mh] Termos MeSH secundário: Cristalização
Cristalografia por Raios X
Galactose Desidrogenases/genética
Galactose Desidrogenases/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 1.1.1.- (Galactose Dehydrogenases); EC 1.1.1.48 (galactose dehydrogenase)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130709
[St] Status:MEDLINE
[do] DOI:10.1107/S1744309113016692


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[PMID]:23800662
[Au] Autor:Xu Y; Zhu X; Chen Y; Gong Y; Liu L
[Ad] Endereço:National Key Laboratory of Crop Genetics and Germplasm Enhancement, Key Laboratory of Horticultural Crop Biology and Genetic Improvement (East China), Ministry of Agriculture, College of Horticulture, Nanjing Agricultural University, Nanjing 210095, PR China.
[Ti] Título:Expression profiling of genes involved in ascorbate biosynthesis and recycling during fleshy root development in radish.
[So] Source:Plant Physiol Biochem;70:269-77, 2013 Sep.
[Is] ISSN:1873-2690
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Ascorbate is a primary antioxidant and an essential enzyme cofactor in plants, which has an important effect on the development of plant root system. To investigate the molecular mechanisms of ascorbate accumulation during root development and reveal the key genes of the ascorbate biosynthesis and recycling pathways, the expression of 16 related genes together with ascorbate abundance were analyzed in the flesh and skin of radish (Raphanus sativus L.) fleshy root. The content of ascorbate decreased with root growth in both the flesh and skin. Expression of GDP-d-mannose pyrophosphorylase, GDP-d-mannose-3',5'-epimerase and d-galacturonate reductase were also decreased and correlated with ascorbate levels in the flesh. In the skin, the expression of GDP-d-mannose pyrophosphorylase and l-galactose dehydrogenase was correlated with ascorbate levels. These results suggested that ascorbate accumulation is affected mainly by biosynthesis rather than recycling in radish root, and the l-galactose pathway may be the major biosynthetic route of ascorbate, and moreover, the salvage pathway may also contribute to ascorbate accumulation. The data suggested that GDP-d-mannose pyrophosphorylase could play an important role in the regulation of ascorbate accumulation during radish fleshy taproot development.
[Mh] Termos MeSH primário: Ácido Ascórbico/genética
Expressão Gênica
Genes de Plantas
Desenvolvimento Vegetal/genética
Proteínas de Plantas/genética
Raízes de Plantas/metabolismo
Raphanus/genética
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/genética
Oxirredutases do Álcool/metabolismo
Antioxidantes/metabolismo
Ácido Ascórbico/biossíntese
Ácido Ascórbico/metabolismo
Galactose/genética
Galactose/metabolismo
Galactose Desidrogenases/genética
Galactose Desidrogenases/metabolismo
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)
Fosforilases/genética
Fosforilases/metabolismo
Proteínas de Plantas/metabolismo
Raízes de Plantas/crescimento & desenvolvimento
Raphanus/enzimologia
Raphanus/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antioxidants); 0 (Plant Proteins); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.- (Galactose Dehydrogenases); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 1.1.1.365 (D-galacturonate reductase); EC 1.1.1.48 (galactose dehydrogenase); EC 2.4.1.- (Phosphorylases); PQ6CK8PD0R (Ascorbic Acid); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:161020
[Lr] Data última revisão:
161020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130627
[St] Status:MEDLINE


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[PMID]:22153245
[Au] Autor:Mellado M; Contreras RA; González A; Dennett G; Moenne A
[Ad] Endereço:Departamento de Biología, Facultad de Química y Biología, Universidad de Santiago de Chile, Casilla 40 Correo 33, Santiago, Chile.
[Ti] Título:Copper-induced synthesis of ascorbate, glutathione and phytochelatins in the marine alga Ulva compressa (Chlorophyta).
[So] Source:Plant Physiol Biochem;51:102-8, 2012 Feb.
[Is] ISSN:1873-2690
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:In order to analyze the synthesis of antioxidant and heavy metal-chelating compounds in response to copper stress, the marine alga Ulva compressa (Chlorophyta) was exposed to 10 µM copper for 7 days and treated with inhibitors of ASC synthesis, lycorine, and GSH synthesis, buthionine sulfoximine (BSO). The levels of ascorbate, in its reduced (ASC) and oxidized (DHA) forms, glutathione, in its reduced (GSH) and oxidized (GSSG) forms, and phytochelatins (PCs) were determined as well as activities of enzymes involved in ASC synthesis, L-galactose dehydrogenase (GDH) and L-galactono 1,4 lactone dehydrogenase (GLDH), and in GSH synthesis, γ-glutamylcysteine synthase (γ-GCS) and glutathione synthase (GS). The level of ASC rapidly decreased to reach a minimum at day 1 that remained low until day 7, DHA decreased until day 1 but slowly increased up to day 7 and its accumulation was inhibited by lycorine. In addition, GSH level increased to reach a maximal level at day 5 and GSSG increased up to day 7 and their accumulation was inhibited by BSO. Activities of GDH and GLDH increased until day 7 and GLDH was inhibited by lycorine. Moreover, activities of γ-GCS and GS increased until day 7 and γ-GCS was inhibited by BSO. Furthermore, PC2, PC3 and PC4, increased until day 7 and their accumulation was inhibited by BSO. Thus, copper induced the synthesis of ascorbate, glutathione and PCs in U. compressa suggesting that these compounds are involved in copper tolerance. Interestingly, U. compressa is, until now, the only ulvophyte showing ASC, GSH and PCs synthesis in response to copper excess.
[Mh] Termos MeSH primário: Ácido Ascórbico/biossíntese
Cobre/farmacologia
Glutationa/biossíntese
Fitoquelatinas/biossíntese
Ulva/efeitos dos fármacos
[Mh] Termos MeSH secundário: Alcaloides de Amaryllidaceae/farmacologia
Ácido Ascórbico/antagonistas & inibidores
Butionina Sulfoximina/farmacologia
Ácido Desidroascórbico/metabolismo
Ativação Enzimática
Galactose Desidrogenases/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-CH/antagonistas & inibidores
Oxirredutases atuantes sobre Doadores de Grupo CH-CH/metabolismo
Fenantridinas/farmacologia
Fatores de Tempo
Ulva/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amaryllidaceae Alkaloids); 0 (Phenanthridines); 5072-26-4 (Buthionine Sulfoximine); 789U1901C5 (Copper); 98726-08-0 (Phytochelatins); EC 1.1.1.- (Galactose Dehydrogenases); EC 1.1.1.48 (galactose dehydrogenase); EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors); EC 1.3.2.3 (galactonolactone dehydrogenase); GAN16C9B8O (Glutathione); I9Q105R5BU (lycorine); PQ6CK8PD0R (Ascorbic Acid); Y2Z3ZTP9UM (Dehydroascorbic Acid)
[Em] Mês de entrada:1204
[Cu] Atualização por classe:161020
[Lr] Data última revisão:
161020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111214
[St] Status:MEDLINE
[do] DOI:10.1016/j.plaphy.2011.10.007



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