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Pesquisa : D08.811.682.047.150.900 [Categoria DeCS]
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[PMID]:28741460
[Au] Autor:Wei S; Zhang XY; Sun Y; Conway LP; Liu L
[Ad] Endereço:Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing. China.
[Ti] Título:Discovery and Biochemical Characterization of UDP-Glucose Dehydrogenase from Akkermansia muciniphila.
[So] Source:Protein Pept Lett;24(8):735-741, 2017.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The biocatalytic oxidation of UDP-glucose in the presence of NAD+ is catalyzed by UDP-glucose dehydrogenases. OBJECTIVES: The main objective of this study was the characterization of a UDP-glucose dehydrogenase (AmUGD) from Akkermansia muciniphila, a bacterium originally isolated from human faeces in an anaerobic medium containing gastric mucin as the sole carbon source. METHODS: The biochemical analysis of AmUGD was performed using a plate reader-based assay measuring the reaction by-product NADH. Furthermore, HPLC- and MALDI-ToF-MS- based methods were used for the enzyme characterization. RESULTS: The recombinant form of the protein was expressed in E. coli and the purified enzyme exhibited optimum levels of activity at 37°C and pH 9.0. While the enzyme is active in the absence of metal ions, the presence of Zn2+ ions results in markedly enhanced levels of catalysis. CONCLUSION: This study describes the first characterization of a nucleotide-processing enzyme from A. muciniphila. The ease of expression and purification of this enzyme make it ideal for biotechnological applications such as the enzymatic synthesis of nucleotide sugars, which may in turn be used for the synthesis of complex carbohydrates or glycoconjugates.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
NAD/metabolismo
Uridina Difosfato Glucose Desidrogenase/metabolismo
Uridina Difosfato Glucose/metabolismo
Verrucomicrobia/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Cátions Bivalentes
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Temperatura Alta
Concentração de Íons de Hidrogênio
Cinética
NAD/química
Plasmídeos/química
Plasmídeos/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Uridina Difosfato Glucose/química
Uridina Difosfato Glucose Desidrogenase/genética
Verrucomicrobia/enzimologia
Zinco/química
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cations, Divalent); 0 (Recombinant Proteins); 0U46U6E8UK (NAD); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase); J41CSQ7QDS (Zinc); V50K1D7P4Y (Uridine Diphosphate Glucose)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.2174/0929866524666170724111147


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[PMID]:28496038
[Au] Autor:Hirooka T; Yoshida E; Eto K; Kaji T
[Ad] Endereço:Department of Environmental Health, Faculty of Pharmaceutical Sciences, Tokyo University of Science.
[Ti] Título:Methylmercury induces hyaluronan synthesis in cultured human brain microvascular endothelial cells and pericytes via different mechanisms.
[So] Source:J Toxicol Sci;42(3):329-333, 2017.
[Is] ISSN:1880-3989
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:In a cerebrum damaged by methylmercury, where neuropathological lesions tend to localize along deep sulci and fissures, edematous changes in white matter have been proposed as the cause of such localization. Since hyaluronan has a high water-retention capability and can contribute to the progression of edematous changes, we hypothesize that methylmercury increases hyaluronan in brain microvascular cells. Our experimental results indicate that methylmercury induces the expression of hyaluronan in cultured human microvascular endothelial cells and pericytes through the induction of expressed UDP-glucose dehydrogenase and hyaluronan synthase 2, respectively. After exposure to methylmercury, hyaluronan largely accumulates in perivascular space, where it contributes to the progression of edematous changes.
[Mh] Termos MeSH primário: Encéfalo/irrigação sanguínea
Células Endoteliais/metabolismo
Ácido Hialurônico/biossíntese
Compostos de Metilmercúrio/toxicidade
Pericitos/metabolismo
[Mh] Termos MeSH secundário: Células Cultivadas
Edema
Células Endoteliais/enzimologia
Células Endoteliais/patologia
Indução Enzimática/efeitos dos fármacos
Glucuronosiltransferase/metabolismo
Seres Humanos
Hialuronan Sintases
Pericitos/enzimologia
Pericitos/patologia
Uridina Difosfato Glucose Desidrogenase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Methylmercury Compounds); 9004-61-9 (Hyaluronic Acid); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase); EC 2.4.1.17 (Glucuronosyltransferase); EC 2.4.1.212 (HAS2 protein, human); EC 2.4.1.212 (Hyaluronan Synthases)
[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:170513
[St] Status:MEDLINE
[do] DOI:10.2131/jts.42.329


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[PMID]:27966912
[Au] Autor:Beattie NR; Keul ND; Sidlo AM; Wood ZA
[Ad] Endereço:Department of Biochemistry & Molecular Biology, University of Georgia , Athens, Georgia 30602, United States.
[Ti] Título:Allostery and Hysteresis Are Coupled in Human UDP-Glucose Dehydrogenase.
[So] Source:Biochemistry;56(1):202-211, 2017 Jan 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human UDP-glucose dehydrogenase (hUGDH) is regulated by an atypical allosteric mechanism in which the feedback inhibitor UDP-xylose (UDP-Xyl) competes with the substrate for the active site. Binding of UDP-Xyl triggers the T131-loop/α6 allosteric switch, which converts the hexameric structure of hUGDH into an inactive, horseshoe-shaped complex (E ). This allosteric transition buries residue A136 in the protein core to produce a subunit interface that favors the E structure. Here we use a methionine substitution to prevent the burial of A136 and trap the T131-loop/α6 switch in the active conformation. We show that hUGDH does not exhibit substrate cooperativity, which is strong evidence that the methionine substitution prevents the formation of the low-UDP-Glc-affinity E state. In addition, the inhibitor affinity of hUGDH is reduced 14-fold, which most likely represents the K for competitive inhibition in the absence of the allosteric transition to the higher-affinity E state. hUGDH also displays a lag in progress curves, which is caused by a slow, substrate-induced isomerization that activates the enzyme. Stopped-flow analysis shows that hUGDH does not exhibit hysteresis, which suggests that the T131-loop/α6 switch is the source of the slow isomerization. This interpretation is supported by the 2.05 Å resolution crystal structure of hUGDH , which shows that the A136M substitution has stabilized the active conformation of the T131-loop/α6 allosteric switch. This work shows that the T131-loop/α6 allosteric switch couples allostery and hysteresis in hUGDH.
[Mh] Termos MeSH primário: Regulação Alostérica
Domínio Catalítico
Uridina Difosfato Glucose Desidrogenase/metabolismo
Uridina Difosfato Xilose/metabolismo
[Mh] Termos MeSH secundário: Alanina/química
Alanina/genética
Alanina/metabolismo
Ligação Competitiva
Biocatálise
Cristalização
Cristalografia por Raios X
Seres Humanos
Cinética
Metionina/química
Metionina/genética
Metionina/metabolismo
Modelos Moleculares
Mutação de Sentido Incorreto
Conformação Proteica
Multimerização Proteica
Especificidade por Substrato
Fatores de Tempo
Uridina Difosfato Glucose Desidrogenase/química
Uridina Difosfato Glucose Desidrogenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
3616-06-6 (Uridine Diphosphate Xylose); AE28F7PNPL (Methionine); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161215
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01044


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[PMID]:27784229
[Au] Autor:Gu B; Laborda P; Wei S; Duan XC; Song HB; Liu L; Voglmeir J
[Ti] Título:Discovery and Biochemical Characterization of the UDP-Xylose Biosynthesis Pathway in Sphaerobacter thermophilus.
[So] Source:Protein Pept Lett;23(12):1103-1110, 2016.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The biosynthesis of UDP-xylose requires the stepwise oxidation/ decarboxylation of UDP-glucose, which is catalyzed by the enzymes UDPglucuronic acid dehydrogenase (UGD) and UDP-xylose synthase (UXS). UDPxylose biosynthesis is ubiquitous in animals and plants. However, only a few UGD and UXS isoforms of bacterial origin have thus far been biochemically characterized. Sphaerobacter thermophilus DSM 20745 is a bacterium isolated from heated sewage sludge, and therefore can be a valuable source of thermostable enzymes of biotechnological interest. However, no biochemical characterizations of any S. thermophilus enzymes have yet been reported. Herein, we describe the cloning and characterization of putative UGD (StUGD) and UXS (StUXS) isoforms from this organism. HPLC- and plate reader-based activity tests of the recombinantly expressed StUGD and StUXS showed that they are indeed active enzymes. Both StUGD and StUXS showed a temperature optimum of 70°C, and a reasonable thermal stability up to 60°C. No metal ions were required for enzymatic activities. StUGD had a higher pH optimum than StUXS. The simple purification procedures and the thermotolerance of StUGD and StUXS make them valuable biocatalysts for the synthesis of UDP-glucuronic acid and UDP-xylose at elevated temperatures. The biosynthetic potential of StUGD was further exemplified in a coupled enzymatic reaction with an UDP-glucuronosyltransferase, allowing the glucuronylation of the natural model substrate bilirubin.
[Mh] Termos MeSH primário: Carboxiliases/metabolismo
Chloroflexi/enzimologia
Chloroflexi/metabolismo
Uridina Difosfato Glucose Desidrogenase/metabolismo
Uridina Difosfato Xilose/biossíntese
[Mh] Termos MeSH secundário: Oxirredução
Esgotos/microbiologia
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sewage); 3616-06-6 (Uridine Diphosphate Xylose); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.35 (UDPglucuronate decarboxylase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170327
[Lr] Data última revisão:
170327
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161028
[St] Status:MEDLINE


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[PMID]:27307252
[Au] Autor:Zimmer BM; Howell ME; Wei Q; Ma L; Romsdahl T; Loughman EG; Markham JE; Seravalli J; Barycki JJ; Simpson MA
[Ad] Endereço:Department of Biochemistry, University of Nebraska, 1901 Vine Street, Lincoln, NE, 68588-0664, USA.
[Ti] Título:Loss of exogenous androgen dependence by prostate tumor cells is associated with elevated glucuronidation potential.
[So] Source:Horm Cancer;7(4):260-71, 2016 Aug.
[Is] ISSN:1868-8500
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prostate epithelial cells control the potency and availability of androgen hormones in part by inactivation and elimination. UDP-glucose dehydrogenase (UGDH) catalyzes the NAD(+)-dependent oxidation of UDP-glucose to UDP-glucuronate, an essential precursor for androgen inactivation by the prostate glucuronidation enzymes UGT2B15 and UGT2B17. UGDH expression is androgen stimulated, which increases the production of UDP-glucuronate and fuels UGT-catalyzed glucuronidation. In this study, we compared the glucuronidation potential and its impact on androgen-mediated gene expression in an isogenic LNCaP model for androgen-dependent versus castration-resistant prostate cancer. Despite significantly lower androgen-glucuronide output, LNCaP 81 castration-resistant tumor cells expressed higher levels of UGDH, UGT2B15, and UGT2B17. However, the magnitude of androgen-activated UGDH and prostate-specific antigen (PSA) expression, as well as the androgen receptor (AR)-dependent repression of UGT2B15 and UGT2B17, was blunted several-fold in these cells. Consistent with these results, the ligand-activated binding of AR to the PSA promoter and subsequent transcriptional activation were also significantly reduced in castration-resistant cells. Analysis of the UDP-sugar pools and flux through pathways downstream of UDP-glucuronate production revealed that these glucuronidation precursor metabolites were channeled through proteoglycan and glycosaminoglycan biosynthetic pathways, leading to increased surface expression of Notch1. Knockdown of UGDH diminished Notch1 and increased glucuronide output. Overall, these results support a model in which the aberrant partitioning of UDP-glucuronate and other UDP-sugars into alternative pathways during androgen deprivation contributes to the loss of prostate tumor cell androgen sensitivity by promoting altered cell surface proteoglycan expression.
[Mh] Termos MeSH primário: Androgênios/farmacologia
Glucuronídeos/metabolismo
Glucuronosiltransferase/metabolismo
Antígenos de Histocompatibilidade Menor/metabolismo
Neoplasias da Próstata/metabolismo
Uridina Difosfato Glucose Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Calicreínas/genética
Calicreínas/metabolismo
Masculino
Modelos Biológicos
Regiões Promotoras Genéticas
Antígeno Prostático Específico/genética
Antígeno Prostático Específico/metabolismo
Neoplasias da Próstata/genética
Neoplasias de Próstata Resistentes à Castração/genética
Neoplasias de Próstata Resistentes à Castração/metabolismo
Receptores Androgênicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AR protein, human); 0 (Androgens); 0 (Glucuronides); 0 (Minor Histocompatibility Antigens); 0 (Receptors, Androgen); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase); EC 2.4.1.17 (Glucuronosyltransferase); EC 2.4.1.17 (UDP-glucuronosyltransferase 2B15, human); EC 2.4.1.17 (UGT2B17 protein, human); EC 3.4.21.- (Kallikreins); EC 3.4.21.- (kallikrein-related peptidase 3, human); EC 3.4.21.77 (Prostate-Specific Antigen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160617
[St] Status:MEDLINE
[do] DOI:10.1007/s12672-016-0268-z


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[PMID]:27198584
[Au] Autor:Grady G; Thelen A; Albers J; Ju T; Guo J; Barycki JJ; Simpson MA
[Ad] Endereço:Department of Biochemistry, University of Nebraska , Lincoln, Nebraska 68588-0664, United States.
[Ti] Título:Inhibiting Hexamer Disassembly of Human UDP-Glucose Dehydrogenase by Photoactivated Amino Acid Cross-Linking.
[So] Source:Biochemistry;55(22):3157-64, 2016 Jun 07.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The enzyme UDP-glucose dehydrogenase (UGDH) catalyzes the reaction of UDP-glucose to UDP-glucuronate through two successive NAD(+)-dependent oxidation steps. Human UGDH apoprotein is purified as a mixture of dimeric and hexameric species. Addition of substrate and cofactor stabilizes the oligomeric state to primarily the hexameric form. To determine if the dynamic conformations of hUGDH are required for catalytic activity, we used site-specific unnatural amino acid incorporation to facilitate cross-linking of monomeric subunits into predominantly obligate oligomeric species. Optimal cross-linking was achieved by encoding p-benzoyl-l-phenylalanine at position 458, normally a glutamine located within the dimer-dimer interface, and exposing the enzyme to long wavelength ultraviolet (UV) radiation in the presence of substrate and cofactor. Hexameric complexes were purified by gel filtration chromatography and found to contain significant fractions of dimer and trimer (approximately 50%) along with another 10% higher-molecular mass species. The activity of the cross-linked enzyme was reduced by almost 60% relative to that of the un-cross-linked UGDH mutant, and UV exposure had no effect on the activity of the wild-type enzyme. These results support a model for catalysis in which the ability to dissociate the dimer-dimer interface is as important for maximal enzyme function as has been previously shown for the formation of the hexamer.
[Mh] Termos MeSH primário: Aminoácidos/química
Reagentes para Ligações Cruzadas
Luz
Multimerização Proteica/efeitos da radiação
Uridina Difosfato Glucose Desidrogenase/química
[Mh] Termos MeSH secundário: Aminoácidos/efeitos da radiação
Catálise
Seres Humanos
Cinética
Modelos Moleculares
Oxirredução
Processos Fotoquímicos
Conformação Proteica
Uridina Difosfato Glucose/metabolismo
Uridina Difosfato Glucose Desidrogenase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Cross-Linking Reagents); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase); V50K1D7P4Y (Uridine Diphosphate Glucose)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170520
[Lr] Data última revisão:
170520
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160521
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00259


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[PMID]:26920483
[Au] Autor:Chu X; Han J; Guo D; Fu Z; Liu W; Tao Y
[Ad] Endereço:Chinese Academy of Sciences Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China. Electronic address: chux@im.ac.cn.
[Ti] Título:Characterization of UDP-glucose dehydrogenase from Pasteurella multocida CVCC 408 and its application in hyaluronic acid biosynthesis.
[So] Source:Enzyme Microb Technol;85:64-70, 2016 Apr.
[Is] ISSN:1879-0909
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hyaluronic acid (HA), a vital acid mucopolysaccharide, has immense applied value in foodstuffs, medicaments, and cosmetics among others. UDP-glucose dehydrogenase (UGDH, EC 1.1.1.22) is an essential enzyme for HA synthesis. In this study, a UGDH (PmuHasB, 45.9 kDa) from Pasteurella multocida CVCC 408 was expressed in Escherichia coli BL21 (DE3). It was purified by two chromatographic columns with a specific activity of 6.58 IU/mg. The optimum pH and temperature were determined to be 10.0 and 37°C, respectively. The activity was stable across the pH range 6-10, and had a half-life of about 3 h at 45°C. The estimated apparent Km values for UDP-glucose and NAD(+) were 0.11 and 0.069 mM, respectively. The results indicated that PmuHasB was an alkaline and mesophilic UGDH. PmuHasB and PmuHasA (HA synthase, HAS) were co-expressed in E. coli BW25113 to obtain a HA high-producing strain pBPAB/BW25113. It produced about 2.39 g/L HA in shake flask by using the method of whole-cell catalysis. Investigation of the different UGDHs on HA synthesis revealed that intracellular UGDH activity and HA total yield of pBPAB/BW25113 (0.15 IU/mg and 5.4 g/L) were higher than from pBPASB/BW25113 (0.013 IU/mg and 2.8 g/L) and pBPAEB/BW25113 (0.010 IU/mg and 2.22 g/L). These results indicated that the activity and stability of UGDH plays a significant role in HA production, and should prove useful for further genetic engineering research with a view to construct other glucuronic acid polysaccharide synthesis pathways.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Ácido Hialurônico/biossíntese
Pasteurella multocida/enzimologia
Uridina Difosfato Glucose Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Estabilidade Enzimática
Escherichia coli/genética
Genes Bacterianos
Cinética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Uridina Difosfato Glucose Desidrogenase/química
Uridina Difosfato Glucose Desidrogenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); 9004-61-9 (Hyaluronic Acid); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160228
[St] Status:MEDLINE


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[PMID]:26903444
[Au] Autor:Scoglio S; Lo Curcio V; Catalani S; Palma F; Battistelli S; Benedetti S
[Ad] Endereço:a Nutritherapic Research Center , Urbino , Italy and.
[Ti] Título:Inhibitory effects of Aphanizomenon flos-aquae constituents on human UDP-glucose dehydrogenase activity.
[So] Source:J Enzyme Inhib Med Chem;31(6):1492-7, 2016 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: The purpose of this study was to investigate the in vitro inhibitory effects of the edible microalga Aphanizomenon flos-aquae (AFA) on human UDP-α-d-glucose 6-dehydrogenase (UGDH) activity, a cytosolic enzyme involved both in tumor progression and in phytochemical bioavailability. METHODS: Both the hydrophilic and ethanolic AFA extracts as well as the constitutive active principles phycocyanin (PC), phycocyanobilin (PCB) and mycosporine-like amino acids (MAAs) were tested. RESULTS: Among AFA components, PCB presented the strongest inhibitory effect on UGDH activity, acting as a competitive inhibitor with respect to UDP-glucose and a non-competitive inhibitor with respect to NAD(+). In preliminary experiments, AFA PCB was also effective in reducing the colony formation capacity of PC-3 prostate cancer cells and FTC-133 thyroid cancer cells. CONCLUSIONS: Overall, these findings confirmed that AFA and its active principles are natural compounds with high biological activity. Further studies evaluating the effects of AFA PCB in reducing tumor cell growth and phytochemical glucuronidation are encouraged.
[Mh] Termos MeSH primário: Aphanizomenon/química
Inibidores Enzimáticos/farmacologia
Uridina Difosfato Glucose Desidrogenase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Ensaios de Seleção de Medicamentos Antitumorais
Seres Humanos
Masculino
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170306
[Lr] Data última revisão:
170306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160224
[St] Status:MEDLINE
[do] DOI:10.3109/14756366.2016.1149478


  9 / 308 MEDLINE  
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[PMID]:26297818
[Au] Autor:Bubner P; Czabany T; Luley-Goedl C; Nidetzky B
[Ad] Endereço:Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, A-8010 Graz, Austria.
[Ti] Título:Comparison of broad-scope assays of nucleotide sugar-dependent glycosyltransferases.
[So] Source:Anal Biochem;490:46-51, 2015 Dec 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycosyltransferases (GTs) are abundant in nature and diverse in their range of substrates. Application of GTs is, however, often complicated by their narrow substrate specificity. GTs with tailored specificities are highly demanded for targeted glycosylation reactions. Engineering of such GTs is, however, restricted by lack of practical and broad-scope assays currently available. Here we present an improvement of an inexpensive and simple assay that relies on the enzymatic detection of inorganic phosphate cleaved from nucleoside phosphate products released in GT reactions. This phosphatase-coupled assay (PCA) is compared with other GT assays: a pH shift assay and a commercially available immunoassay in Escherichia coli cell-free extract (CE). Furthermore, we probe PCA with three GTs with different specificities. Our results demonstrate that PCA is a versatile and apparently general GT assay with a detection limit as low as 1 mU. The detection limit of the pH shift assay is roughly 4 times higher. The immunoassay, by contrast, detected only nucleoside diphosphates (NDPs) but had the lowest detection limit. Compared with these assays, PCA showed superior robustness and, therefore, appears to be a suitable general screening assay for nucleotide sugar-dependent GTs.
[Mh] Termos MeSH primário: Fosfatase Alcalina/metabolismo
Glicosiltransferases/metabolismo
Nucleosídeos/metabolismo
Fosfatos/análise
[Mh] Termos MeSH secundário: Adsorção
Óxido de Alumínio/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sistema Livre de Células/enzimologia
Sistema Livre de Células/metabolismo
Centrifugação
Escherichia coli/enzimologia
Escherichia coli/metabolismo
Glicosiltransferases/genética
Seres Humanos
Hidrólise
Indicadores e Reagentes/química
Cinética
Limite de Detecção
Fosfatos/química
Fosfatos/isolamento & purificação
Fosfatos/metabolismo
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Recombinantes de Fusão/metabolismo
Sialiltransferases/genética
Sialiltransferases/metabolismo
Especificidade por Substrato
Uridina Difosfato Glucose Desidrogenase/genética
Uridina Difosfato Glucose Desidrogenase/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Indicators and Reagents); 0 (Nucleosides); 0 (Phosphates); 0 (Plant Proteins); 0 (Recombinant Fusion Proteins); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase); EC 2.4.- (Glycosyltransferases); EC 2.4.99.- (Sialyltransferases); EC 2.7.1.- (sucrose synthase kinase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.1.3.1 (Alkaline Phosphatase); LMI26O6933 (Aluminum Oxide)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151017
[Lr] Data última revisão:
151017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150823
[St] Status:MEDLINE


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Fotocópia
[PMID]:26008638
[Au] Autor:Wei S; Kulinich A; Duan XC; Liu L; Voglmeir J
[Ti] Título:Discovery and Biochemical Characterization of UDP-Glucose Dehydrogenase from Granulibacter bethesdensis.
[So] Source:Protein Pept Lett;22(7):628-34, 2015.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:UDP-glucose dehydrogenases (EC 1.1.1.22) are responsible for the conversion of UDP-glucose to UDP-glucuronic acid, a key precursor in the biosynthesis of glycoconjugates. Herein we report the discovery and characterization of a UDPglucose dehydrogenase (GbUGD) from Granulibacter bethesdensis, a bacterium originally isolated from the lymph nodes of patients with chronic granulomatous disease (CGD). The recombinant form of the protein was expressed in high yield and the purified enzyme showed highest activity at 37°C/pH 9.0 and was strongly inhibited by Zn(2+) ions, sodium dodecyl sulfate (SDS) and urea. UDP-xylose, an allosteric feedback inhibitor, reduced significantly the activity of the enzyme. High activities were observed using the co-substrates UDP-glucose and NAD+, whereas no activity could be detected using other nucleotide sugars or NADP(+) as potential alternative substrates. The high activity combined with the simple purification procedure used make GbUGD a valuable new alternative biocatalyst for the synthesis of UDP-glucuronic acid or the development of NAD+ regeneration systems.
[Mh] Termos MeSH primário: Acetobacteraceae/enzimologia
Uridina Difosfato Glucose Desidrogenase/química
Uridina Difosfato Glucose Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Acetobacteraceae/genética
Clonagem Molecular
Detergentes/farmacologia
Inibidores Enzimáticos/farmacologia
Seres Humanos
Concentração de Íons de Hidrogênio
Cinética
Metais/farmacologia
Desnaturação Proteica/efeitos dos fármacos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Temperatura Ambiente
Uridina Difosfato Glucose Desidrogenase/antagonistas & inibidores
Uridina Difosfato Glucose Desidrogenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Detergents); 0 (Enzyme Inhibitors); 0 (Metals); 0 (Recombinant Proteins); EC 1.1.1.22 (Uridine Diphosphate Glucose Dehydrogenase)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:150623
[Lr] Data última revisão:
150623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150527
[St] Status:MEDLINE



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