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Pesquisa : D08.811.682.047.210 [Categoria DeCS]
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[PMID]:28741462
[Au] Autor:Weissenborn MJ; Debecker DP; Golten S; Linclau B; Turner NJ; Flitsch SL
[Ad] Endereço:School of Chemistry & Manchester Interdisciplinary Biocentre, The University of Manchester, 131 Princess Street, Manchester, M17DN. United Kingdom.
[Ti] Título:Development of a Solid Phase Array Assay for the Screening of Galactose Oxidase Activity and for Fast Identification of Inhibitors.
[So] Source:Protein Pept Lett;24(8):742-746, 2017.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Galactose oxidase (GOase) catalyses the highly selective oxidation of terminal galactosides on a wide range of natural glycoconjugates and has found wide applications in biotechnology - particularly in biocatalysis. GOase is copper dependent and uses oxygen to oxidise the C6-primary alcohol of galactose and produces hydrogen peroxide. The enzyme activity can be conveniently assessed by a colorimetric assay. OBJECTIVES: The objective of the present study was to develop an assay system, which is independent of the hydrogen peroxide formation to identify possible fluorinated GOase inhibitors. In case that the inhibitor bears a primary or secondary alcohol, it could also be oxidised by the enzyme. In such case, the colorimetric assay is not able to distinguish between substrate and inhibitor, since oxidation of both molecules would result in the formation of hydrogen peroxide. METHODS: D-galactose (D-Gal) was immobilised onto a gold surface functionalised by selfassembled monolayers (SAMs,). A GOase solution was then added to the surface in a droplet for a certain period of time and thereafter washed away. The activity of GOase on the immobilised D-Gal can then be quantified by MALDI-ToF MS. RESULTS: For inhibition studies, GOase was incubated together with 62.5 mM of deoxy-fluorinated monosaccharides on the D-Gal displaying platform. Five deoxy-fluorinated D-Gal showed a >50% inhibition of its activity. The array system has been moreover utilised to determine the apparent IC50 value of 3-F-Gal 15 as a proof of principle. CONCLUSION: The developed array platform allows the fast identification of GOase substrates and inhibitors from a library of deoxy-fluorinated sugars using MALDI-ToF MS as a label-free readout method. In addition, the enzymatic reaction enables for the in situ activation of sugar-coated surfaces to bioorthogonal aldehydes, which can be utilised for subsequent chemical modifications.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/química
Galactose Oxidase/química
Galactose/química
Ensaios de Triagem em Larga Escala
[Mh] Termos MeSH secundário: Adsorção
Biocatálise
Galactose Oxidase/antagonistas & inibidores
Ouro/química
Halogenação
Peróxido de Hidrogênio/química
Monossacarídeos/química
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Monosaccharides); 7440-57-5 (Gold); BBX060AN9V (Hydrogen Peroxide); EC 1.1.3.9 (Galactose Oxidase); X2RN3Q8DNE (Galactose)
[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:10.2174/0929866524666170724114348


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[PMID]:28093470
[Au] Autor:Chaplin AK; Svistunenko DA; Hough MA; Wilson MT; Vijgenboom E; Worrall JA
[Ad] Endereço:School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, U.K.
[Ti] Título:Active-site maturation and activity of the copper-radical oxidase GlxA are governed by a tryptophan residue.
[So] Source:Biochem J;474(5):809-825, 2017 Feb 20.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:GlxA from is a mononuclear copper-radical oxidase and a member of the auxiliary activity family 5 (AA5). Its domain organisation and low sequence homology make it a distinct member of the AA5 family in which the fungal galactose 6-oxidase (Gox) is the best characterised. GlxA is a key cuproenzyme in the copper-dependent morphological development of with a function that is linked to the processing of an extracytoplasmic glycan. The catalytic sites in GlxA and Gox contain two distinct one-electron acceptors comprising the copper ion and a 3'-( -cysteinyl) tyrosine. The latter is formed post-translationally through a covalent bond between a cysteine and a copper-co-ordinating tyrosine ligand and houses a radical. In GlxA and Gox, a second co-ordination sphere tryptophan residue (Trp288 in GlxA) is present, but the orientation of the indole ring differs between the two enzymes, creating a marked difference in the π-π stacking interaction of the benzyl ring with the 3'-( -cysteinyl) tyrosine. Differences in the spectroscopic and enzymatic activity have been reported between GlxA and Gox with the indole orientation suggested as a reason. Here, we report a series of and studies using the W288F and W288A variants of GlxA to assess the role of Trp288 on the morphology, maturation, spectroscopic and enzymatic properties. Our findings point towards a salient role for Trp288 in the kinetics of copper loading and maturation of GlxA, with its presence essential for stabilising the metalloradical site required for coupling catalytic activity and morphological development.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Cobre/química
Galactose Oxidase/química
Oxirredutases/química
Streptomyces lividans/química
Triptofano/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Substituição de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Domínio Catalítico
Cátions Bivalentes
Clonagem Molecular
Cobre/metabolismo
Cristalografia por Raios X
Cisteína/química
Cisteína/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Fusarium/química
Fusarium/enzimologia
Fusarium/crescimento & desenvolvimento
Galactose Oxidase/genética
Galactose Oxidase/metabolismo
Expressão Gênica
Cinética
Ligantes
Mutação
Oxirredutases/genética
Oxirredutases/metabolismo
Ligação Proteica
Domínios Proteicos
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Streptomyces lividans/enzimologia
Streptomyces lividans/crescimento & desenvolvimento
Homologia Estrutural de Proteína
Especificidade por Substrato
Triptofano/metabolismo
Tirosina/química
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cations, Divalent); 0 (Ligands); 0 (Recombinant Proteins); 42HK56048U (Tyrosine); 789U1901C5 (Copper); 8DUH1N11BX (Tryptophan); EC 1.- (Oxidoreductases); EC 1.1.3.9 (Galactose Oxidase); EC 1.16.- (copper oxidase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170614
[Lr] Data última revisão:
170614
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170118
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160968


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[PMID]:27074906
[Au] Autor:Weissenborn MJ; Notonier S; Lang SL; Otte KB; Herter S; Turner NJ; Flitsch SL; Hauer B
[Ad] Endereço:Institute of Technical Biochemistry, Universitaet Stuttgart, Allmandring 31, 70569 Stuttgart, Germany. bernhard.hauer@itb.uni-stuttgart.de.
[Ti] Título:Whole-cell microtiter plate screening assay for terminal hydroxylation of fatty acids by P450s.
[So] Source:Chem Commun (Camb);52(36):6158-61, 2016 05 04.
[Is] ISSN:1364-548X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A readily available galactose oxidase (GOase) variant was used to develop a whole cell screening assay. This endpoint detection system was applied in a proof-of-concept approach by screening a focussed mutant library. This led to the discovery of the thus far most active P450 Marinobacter aquaeolei mutant catalysing the terminal hydroxylation of fatty acids.
[Mh] Termos MeSH primário: Sistema Enzimático do Citocromo P-450/metabolismo
Ácidos Graxos/metabolismo
Análise Serial de Tecidos
[Mh] Termos MeSH secundário: Sistema Enzimático do Citocromo P-450/genética
Ácidos Graxos/química
Galactose Oxidase/química
Galactose Oxidase/metabolismo
Hidroxilação
Ácidos Láuricos/química
Marinobacter/enzimologia
Mutagênese
NADP/química
NADP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Lauric Acids); 1160N9NU9U (lauric acid); 53-59-8 (NADP); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.1.3.9 (Galactose Oxidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160415
[St] Status:MEDLINE
[do] DOI:10.1039/c6cc01749e


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[PMID]:26518347
[Au] Autor:Mollerup F; Parikka K; Vuong TV; Tenkanen M; Master E
[Ad] Endereço:Department of Biotechnology and Chemical Technology, Aalto University, 00076 Aalto, Finland.
[Ti] Título:Influence of a family 29 carbohydrate binding module on the activity of galactose oxidase from Fusarium graminearum.
[So] Source:Biochim Biophys Acta;1860(2):354-62, 2016 Feb.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Galactose oxidase (GaO) selectively oxidizes the primary hydroxyl of galactose to a carbonyl, facilitating targeted chemical derivatization of galactose-containing polysaccharides, leading to renewable polymers with tailored physical and chemical properties. Here we investigate the impact of a family 29 glucomannan binding module on the activity and binding of GaO towards various polysaccharides. Specifically, CBM29-1-2 from Piromyces equi was separately linked to the N- and C-termini of GaO. RESULTS: Both GaO-CBM29 and CBM29-GaO were successfully expressed in Pichia pastoris, and demonstrated enhanced binding to galactomannan, galactoglucomannan and galactoxyloglucan. The position of the CBM29 fusion affected the enzyme function. Particularly, C-terminal fusion led to greatest increases in galactomannan binding and catalytic efficiency, where relative to wild-type GaO, kcat/Km values increased by 7.5 and 19.8 times on guar galactomannan and locust bean galactomannan, respectively. The fusion of CBM29 also induced oligomerization of GaO-CBM29. MAJOR CONCLUSIONS: Similar to impacts of cellulose-binding modules associated with cellulolytic enzymes, increased substrate binding impeded the action of GaO fusions on more concentrated preparations of galactomannan, galactoglucomannan and galactoxyloglucan; this was especially true for GaO-CBM29. Given the N-terminal positioning of the native galactose-binding CBM32 in GaO, the varying impacts of N-terminal versus C-terminal fusion of CBM29-1-2 may reflect competing action of neighboring CBMs. GENERAL SIGNIFICANCE: This study thoroughly examines and discusses the effects of CBM fusion to non-lignocellulytic enzymes on soluble polysaccharides. Herein kinetics of GaO on galactose containing polysaccharides is presented for the first time.
[Mh] Termos MeSH primário: Fusarium/enzimologia
Galactose Oxidase/metabolismo
Mananas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Estabilidade Enzimática
Galactose/química
Galactose Oxidase/química
Dados de Sequência Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mannans); 0 (galactoglucomannan); 11078-30-1 (galactomannan); 36W3E5TAMG ((1-6)-alpha-glucomannan); EC 1.1.3.9 (Galactose Oxidase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151101
[St] Status:MEDLINE


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[PMID]:26680532
[Au] Autor:Yin DT; Urresti S; Lafond M; Johnston EM; Derikvand F; Ciano L; Berrin JG; Henrissat B; Walton PH; Davies GJ; Brumer H
[Ad] Endereço:Michael Smith Laboratories and Department of Chemistry, University of British Columbia, 2185 East Mall, Vancouver, British Columbia, Canada V6T 1Z4.
[Ti] Título:Structure-function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family.
[So] Source:Nat Commun;6:10197, 2015 Dec 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Alcohol oxidases, including carbohydrate oxidases, have a long history of research that has generated fundamental biological understanding and biotechnological applications. Despite a long history of study, the galactose 6-oxidase/glyoxal oxidase family of mononuclear copper-radical oxidases, Auxiliary Activity Family 5 (AA5), is currently represented by only very few characterized members. Here we report the recombinant production and detailed structure-function analyses of two homologues from the phytopathogenic fungi Colletotrichum graminicola and C. gloeosporioides, CgrAlcOx and CglAlcOx, respectively, to explore the wider biocatalytic potential in AA5. EPR spectroscopy and crystallographic analysis confirm a common active-site structure vis-à-vis the archetypal galactose 6-oxidase from Fusarium graminearum. Strikingly, however, CgrAlcOx and CglAlcOx are essentially incapable of oxidizing galactose and galactosides, but instead efficiently catalyse the oxidation of diverse aliphatic alcohols. The results highlight the significant potential of prospecting the evolutionary diversity of AA5 to reveal novel enzyme specificities, thereby informing both biology and applications.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/metabolismo
Proteínas Fúngicas/metabolismo
Galactose Oxidase/metabolismo
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/química
Álcoois/metabolismo
Domínio Catalítico
Colletotrichum
Cristalização
Cristalografia por Raios X
Espectroscopia de Ressonância de Spin Eletrônica
Proteínas Fúngicas/química
Fusarium
Galactose Oxidase/química
Mutagênese Sítio-Dirigida
Filogenia
Pichia
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Espectroscopia de Prótons por Ressonância Magnética
Proteínas Recombinantes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Alcohols); 0 (Fungal Proteins); 0 (Recombinant Proteins); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.3.- (glyoxal oxidase); EC 1.1.3.13 (alcohol oxidase); EC 1.1.3.9 (Galactose Oxidase)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151219
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms10197


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[PMID]:25543085
[Au] Autor:Paukner R; Staudigl P; Choosri W; Haltrich D; Leitner C
[Ad] Endereço:Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Vienna, Austria.
[Ti] Título:Expression, purification, and characterization of galactose oxidase of Fusarium sambucinum in E. coli.
[So] Source:Protein Expr Purif;108:73-79, 2015 Apr.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A gene encoding a galactose oxidase (GalOx) was isolated from Fusarium sambucinum cultures and overexpressed in Escherichia coli yielding 4.4mg enzyme per L of growth culture with a specific activity of 159Umg(-1). By adding a C-terminal His-tag the enzyme could be easily purified with a single affinity chromatography step with high recovery rate (90%). The enzyme showed a single band on SDS-PAGE with an apparent molecular mass of 68.5kDa. The pH optimum for the oxidation of galactose was in the range of pH 6-7.5. Optimum temperature for the enzyme activity was 35°C, with a half-life of 11.2min, 5.3min, and 2.7min for incubation at 40°C, 50°C, and 60°C, respectively. From all tested substrates, the highest relative activity was found for 1-methyl-ß-galactopyranoside (226Umg(-1)) and the highest catalytic efficiency (kcat/Km) for melibiose (2700mM(-1)s(-1)). The enzyme was highly specific for molecular oxygen as an electron acceptor, and showed no appreciable activity with a range of alternative acceptors investigated. Different chemicals were tested for their effect on GalOx activity. The activity was significantly reduced by EDTA, NaN3, and KCN.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Proteínas Fúngicas
Fusarium/enzimologia
Galactose Oxidase
Expressão Gênica
[Mh] Termos MeSH secundário: Escherichia coli/genética
Proteínas Fúngicas/biossíntese
Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Proteínas Fúngicas/isolamento & purificação
Fusarium/genética
Galactose Oxidase/biossíntese
Galactose Oxidase/química
Galactose Oxidase/genética
Galactose Oxidase/isolamento & purificação
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Recombinant Fusion Proteins); EC 1.1.3.9 (Galactose Oxidase)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141228
[St] Status:MEDLINE


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[PMID]:25472443
[Au] Autor:Phillips MR; Turco SJ
[Ad] Endereço:Department of Biochemistry, University of Kentucky Medical Center, Lexington, KY 40536, USA.
[Ti] Título:Characterization of a ricin-resistant mutant of Leishmania donovani that expresses lipophosphoglycan.
[So] Source:Glycobiology;25(4):428-37, 2015 Apr.
[Is] ISSN:1460-2423
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The abundant cell-surface lipophosphoglycan (LPG) of Leishmania parasites plays a central role throughout the eukaryote's life cycle. A number of LPG-defective mutants and their complementing genes have been isolated and have proven invaluable in assessing the importance of LPG and related glycoconjugates in parasite virulence. While ricin agglutination selection protocols frequently result in lpg- mutants, one  Leishmania donovani variant we isolated, named JABBA, was found to be lpg+. Procyclic (logarithmic) JABBA expresses significant amounts of a large-sized LPG, larger than observed from procyclic wild type but similar in size to LPG from wild type from metacyclic (stationary) phase. Structural analysis of the LPG from logarithmically grown JABBA by capillary electrophoresis protocols revealed that it averaged 30 repeat units composed of the unsubstituted Gal(ß1,4)Man(α1)-PO4 typical of wild-type L. donovani. Analysis of JABBA LPG caps indicated that 20% is branched trisaccharide Gal(ß1,4)[Glc(ß1,2)]Man and tetrasaccharide Gal(ß1,4)[Glc(ß1,2)Man(α1,2)]Man instead of the usual Gal(ß1,4)Man and Man(α1,2)Man terminating caps. Consistent with these structural observations, analyses of the relevant glycosyltransferases in JABBA microsomes involved in LPG biosynthesis showed a 2-fold increase in elongating mannosylphosphoryltransferase activity and up-regulation of a ß-glucosyltransferase activity. Furthermore, the caps of JABBA LPG are cryptic in presentation as shown by the loss of binding by the lectins, ricin, peanut agglutinin and concanavalin A and reduced accessibility of the terminal galactose residues to oxidation by galactose oxidase. These results indicate that LPG from JABBA is intriguingly similar to the larger LPG in wild-type parasites that arises following the differentiation of the non-infectious procyclic promastigotes to infectious, metacyclic forms.
[Mh] Termos MeSH primário: Aglutininas/farmacologia
Glicoesfingolipídeos/metabolismo
Leishmania donovani/efeitos dos fármacos
Ricina/farmacologia
[Mh] Termos MeSH secundário: Configuração de Carboidratos
Sequência de Carboidratos
Resistência a Medicamentos
Galactose/química
Galactose Oxidase/química
Glicoesfingolipídeos/química
Glicosilação
Leishmania donovani/metabolismo
Dados de Sequência Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Agglutinins); 0 (Glycosphingolipids); 0 (lipophosphonoglycan); 9009-86-3 (Ricin); EC 1.1.3.9 (Galactose Oxidase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141205
[St] Status:MEDLINE
[do] DOI:10.1093/glycob/cwu130


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[PMID]:25442945
[Au] Autor:Nishiyama H; Watanabe T; Inoue Y
[Ad] Endereço:Department of Materials Science and Technology, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka 940-2188, Niigata, Japan.
[Ti] Título:Activation of immobilized enzymes by acoustic wave resonance oscillation.
[So] Source:Enzyme Microb Technol;67:27-31, 2014 Dec.
[Is] ISSN:1879-0909
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acoustic wave resonance oscillation has been used successfully in the development of methods to activate immobilized enzyme catalysts. In this study, resonance oscillation effects were demonstrated for enzyme reactions on galactose oxidase (GAD), D-amino acid oxidase (DAAO), and L-amino acid oxidase (LAAO), all of which were immobilized covalently on a ferroelectric lead zirconate titanate (PZT) device that could generate thickness-extensional resonance oscillations (TERO) of acoustic waves. For galactose oxidation on immobilized GAD in a microreactor, TERO generation immediately increased enzyme activity 2- to 3-fold. Eliminating TERO caused a slight decrease in the activity, with ∼90% of the enhanced activity retained while the reaction proceeded. Contact of the enhanced enzyme with a galactose-free solution caused almost complete reversion of the activity to the original low level before TERO generation, indicating that, not only TERO-induced GAD activation, but also preservation of the increased activity, required a galactose substrate. Similar activity changes with TERO were observed for enzyme reactions on DAAO and LAAO. Kinetic analysis demonstrated that TERO helped strengthen the interactions of the immobilized enzyme with the reactant substrate and promoted formation of an activation complex.
[Mh] Termos MeSH primário: Enzimas Imobilizadas/metabolismo
[Mh] Termos MeSH secundário: Animais
Reatores Biológicos
Catálise
D-Aminoácido Oxidase/metabolismo
Ativação Enzimática
Galactose/metabolismo
Galactose Oxidase/metabolismo
Cinética
L-Aminoácido Oxidase/metabolismo
Chumbo
Oxirredução
Som
Titânio
Zircônio
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 12626-81-2 (lead titanate zirconate); 2P299V784P (Lead); C6V6S92N3C (Zirconium); D1JT611TNE (Titanium); EC 1.1.3.9 (Galactose Oxidase); EC 1.4.3.2 (L-Amino Acid Oxidase); EC 1.4.3.3 (D-Amino-Acid Oxidase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:141202
[Lr] Data última revisão:
141202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141203
[St] Status:MEDLINE


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[PMID]:25371163
[Au] Autor:Thomas A; Shukla A; Sivakumar S; Verma S
[Ad] Endereço:Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur-208016, UP, India. sverma@iitk.ac.in.
[Ti] Título:Assembly, postsynthetic modification and hepatocyte targeting by multiantennary, galactosylated soft structures.
[So] Source:Chem Commun (Camb);50(99):15752-5, 2014 Dec 25.
[Is] ISSN:1364-548X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Enzyme modifiable, hollow self-assembled structures offer an excellent scope for multiantennary delivery vectors. Herein, we report synthesis and applications of bis-galactose lysine based supramolecular ensembles, which possess surface galactose moieties amenable to enzymatic modifications. This post-synthetic modification generates reactive aldehyde groups, which could possibly serve as dynamic anchors for crosslinking and cell adhesion.
[Mh] Termos MeSH primário: Galactose/metabolismo
Hepatócitos/metabolismo
[Mh] Termos MeSH secundário: Aminas/química
Adesão Celular
Galactose/química
Galactose Oxidase/metabolismo
Ouro/química
Células Hep G2
Hepatócitos/citologia
Seres Humanos
Nanopartículas Metálicas/química
Microscopia de Força Atômica
Microscopia Eletrônica de Varredura
Oxidiazóis/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amines); 0 (N-methyl-4-amino-7-nitrobenzofurazan); 0 (Oxadiazoles); 7440-57-5 (Gold); EC 1.1.3.9 (Galactose Oxidase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:141121
[Lr] Data última revisão:
141121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141106
[St] Status:MEDLINE
[do] DOI:10.1039/c4cc07074g


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[PMID]:25156181
[Au] Autor:Staniland S; Yuan B; Giménez-Agulló N; Marcelli T; Willies SC; Grainger DM; Turner NJ; Clayden J
[Ad] Endereço:School of Chemistry, University of Manchester, Oxford Road, Manchester M13 9PL (UK), Fax: (+44) 161-275-4939.
[Ti] Título:Enzymatic desymmetrising redox reactions for the asymmetric synthesis of biaryl atropisomers.
[So] Source:Chemistry;20(41):13084-8, 2014 Oct 06.
[Is] ISSN:1521-3765
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Atropisomeric biaryls carrying ortho-hydroxymethyl and formyl groups were made enantioselectively by desymmetrisation of dialdehyde or diol substrates. The oxidation of the symmetrical diol substrates was achieved using a variant of galactose oxidase (GOase), and the reduction of the dialdehydes using a panel of ketoreductases. Either M or P enantiomers of the products could be formed, with absolute configurations assigned by time-dependent DFT calculations of circular dichroism spectra. The differing selectivities observed with different biaryl structures offer an insight into the detailed structure of the active site of the GOase enzyme.
[Mh] Termos MeSH primário: Galactose Oxidase/metabolismo
Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Aldeídos/química
Aldeídos/metabolismo
Biocatálise
Domínio Catalítico
Dicroísmo Circular
Galactose Oxidase/química
Galactose Oxidase/genética
Modelos Moleculares
Mutação
Oxirredução
Oxirredutases/química
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aldehydes); EC 1.- (Oxidoreductases); EC 1.1.3.9 (Galactose Oxidase)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140827
[St] Status:MEDLINE
[do] DOI:10.1002/chem.201404509



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