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[PMID]:27523732
[Au] Autor:Bombicino SS; Iglesias DE; Zaobornyj T; Boveris A; Valdez LB
[Ad] Endereço:Institute of Biochemistry and Molecular Medicine, Physical Chemistry Division, School of Pharmacy and Biochemistry, University of Buenos Aires (IBIMOL, UBA-CONICET), Junín 956, C1113AAD, Buenos Aires, Argentina. Electronic address: sbombicino@ffyb.uba.ar.
[Ti] Título:Mitochondrial nitric oxide production supported by reverse electron transfer.
[So] Source:Arch Biochem Biophys;607:8-19, 2016 Oct 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heart phosphorylating electron transfer particles (ETPH) produced NO at 1.2 ± 0.1 nmol NO. min(-1) mg protein(-1) by the mtNOS catalyzed reaction. These particles showed a NAD(+) reductase activity of 64 ± 3 nmol min(-1) mg protein(-1) sustained by reverse electron transfer (RET) at expenses of ATP and succinate. The same particles, without NADPH and in conditions of RET produced 0.97 ± 0.07 nmol NO. min(-1) mg protein(-1). Rotenone inhibited NO production supported by RET measured in ETPH and in coupled mitochondria, but did not reduce the activity of recombinant nNOS, indicating that the inhibitory effect of rotenone on NO production is due to an electron flow inhibition and not to a direct action on mtNOS structure. NO production sustained by RET corresponds to 20% of the total amount of NO released from heart coupled mitochondria. A mitochondrial fraction enriched in complex I produced 1.7 ± 0.2 nmol NO. min(-1) mg protein(-1) and reacted with anti-75 kDa complex I subunit and anti-nNOS antibodies, suggesting that complex I and mtNOS are located contiguously. These data show that mitochondrial NO production can be supported by RET, and suggest that mtNOS is next to complex I, reaffirming the idea of a functional association between these proteins.
[Mh] Termos MeSH primário: Mitocôndrias/metabolismo
Óxido Nítrico/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Animais
Catálise
Bovinos
Relação Dose-Resposta a Droga
Elétrons
Mitocôndrias Cardíacas/metabolismo
Miocárdio/metabolismo
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/metabolismo
NADP/química
Consumo de Oxigênio
Ratos
Proteínas Recombinantes/química
Rotenona/química
Partículas Submitocôndricas/química
Ácido Succínico/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 03L9OT429T (Rotenone); 31C4KY9ESH (Nitric Oxide); 53-59-8 (NADP); 8L70Q75FXE (Adenosine Triphosphate); AB6MNQ6J6L (Succinic Acid); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170502
[Lr] Data última revisão:
170502
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160816
[St] Status:MEDLINE


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[PMID]:27259388
[Au] Autor:Matsubara T; Hamada S; Wakabayashi A; Kishida M
[Ad] Endereço:Division of Applied Life Science, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, 1-1 Gakuen-cho, Naka-ku, Sakai, Osaka 599-8531, Japan.
[Ti] Título:Fermentative production of l-galactonate by using recombinant Saccharomyces cerevisiae containing the endogenous galacturonate reductase gene from Cryptococcus diffluens.
[So] Source:J Biosci Bioeng;122(5):639-644, 2016 Nov.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The GAR1 gene, encoding d-galacturonate reductase in Cryptococcus diffluens, was isolated, and the GAR1-expression plasmid was constructed by insertion of GAR1 downstream of the yeast constitutive promoter in the yeast-integrating vector. Recombinant Saccharomyces cerevisiae expressing C. diffluensd-galacturonate reductase from a genome integrated copy of the gene was cultured for use the conversion of d-galacturonic acid to l-galactonic acid. The optimum conditions for l-galactonic acid production were determined in terms of the initial concentration of d-galacturonic acid, fermentation pH, and mixed sugars. The following conditions yielded high efficiency in the conversion of d-galacturonic acid to l-galactonic acid in large-scale cultures: 0.1% initial d-galacturonic acid concentration, pH 3.5, and glucose as additional sugar. The aerobic condition was necessary for the conversion of d-galacturonic acid. Subculture of that recombinant was not showing to decrease of the d-galacturonic acid conversion rate even though it was repeated in ten generations. Culturing in scale-up, the conversion rate of d-galacturonic acid to l-galactonic acid was increased.
[Mh] Termos MeSH primário: Cryptococcus/genética
Fermentação
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/genética
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/metabolismo
Saccharomyces cerevisiae
Açúcares Ácidos/metabolismo
[Mh] Termos MeSH secundário: Aerobiose
Cryptococcus/enzimologia
Fermentação/genética
Ácidos Hexurônicos/metabolismo
Organismos Geneticamente Modificados
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hexuronic Acids); 0 (Sugar Acids); 13382-27-9 (galactonic acid); 4JK6RN80GF (galacturonic acid); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 1.1.1.365 (D-galacturonate reductase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160605
[St] Status:MEDLINE


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[PMID]:26959814
[Au] Autor:Zhu J; Khalil SM; Mitchell RD; Bissinger BW; Egekwu N; Sonenshine DE; Roe RM
[Ad] Endereço:Department of Entomology, North Carolina State University, Raleigh, North Carolina, 27695, United States of America.
[Ti] Título:Mevalonate-Farnesal Biosynthesis in Ticks: Comparative Synganglion Transcriptomics and a New Perspective.
[So] Source:PLoS One;11(3):e0141084, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Juvenile hormone (JH) controls the growth, development, metamorphosis, and reproduction of insects. For many years, the general assumption has been that JH regulates tick and other acarine development and reproduction the same as in insects. Although researchers have not been able to find the common insect JHs in hard and soft tick species and JH applications appear to have no effect on tick development, it is difficult to prove the negative or to determine whether precursors to JH are made in ticks. The tick synganglion contains regions which are homologous to the corpora allata, the biosynthetic source for JH in insects. Next-gen sequencing of the tick synganglion transcriptome was conducted separately in adults of the American dog tick, Dermacentor variabilis, the deer tick, Ixodes scapularis, and the relapsing fever tick, Ornithodoros turicata as a new approach to determine whether ticks can make JH or a JH precursor. All of the enzymes that make up the mevalonate pathway from acetyl-CoA to farnesyl diphosphate (acetoacetyl-CoA thiolase, HMG-S, HMG-R, mevalonate kinase, phosphomevalonate kinase, diphosphomevalonate decarboxylase, and farnesyl diphosphate synthase) were found in at least one of the ticks studied but most were found in all three species. Sequence analysis of the last enzyme in the mevalonate pathway, farnesyl diphosphate synthase, demonstrated conservation of the seven prenyltransferase regions and the aspartate rich motifs within those regions typical of this enzyme. In the JH branch from farnesyl diphosphate to JH III, we found a putative farnesol oxidase used for the conversion of farnesol to farnesal in the synganglion transcriptome of I. scapularis and D. variabilis. Methyltransferases (MTs) that add a methyl group to farnesoic acid to make methyl farnesoate were present in all of the ticks studied with similarities as high as 36% at the amino acid level to insect JH acid methyltransferase (JHAMT). However, when the tick MTs were compared to the known insect JHAMTs from several insect species at the amino acid level, the former lacked the farnesoic acid binding motif typical in insects. The P450s shown in insects to add the C10,11 epoxide to methyl farnesoate, are in the CYP15 family; this family was absent in our tick transcriptomes and in the I. scapularis genome, the only tick genome available. These data suggest that ticks do not synthesize JH III but have the mevalonate pathway and may produce a JH III precursor.
[Mh] Termos MeSH primário: Vias Biossintéticas
Corpora Allata/metabolismo
Farneseno Álcool/análogos & derivados
Ácido Mevalônico/metabolismo
Carrapatos/genética
Carrapatos/metabolismo
Transcriptoma/genética
[Mh] Termos MeSH secundário: Aedes/enzimologia
Sequência de Aminoácidos
Animais
Colesterol/biossíntese
Farneseno Álcool/metabolismo
Feminino
Geraniltranstransferase/química
Geraniltranstransferase/metabolismo
Hormônios Juvenis/metabolismo
Masculino
Metiltransferases/química
Metiltransferases/metabolismo
Camundongos
Modelos Biológicos
Dados de Sequência Molecular
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/química
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/metabolismo
Filogenia
Alinhamento de Sequência
[Pt] Tipo de publicação:COMPARATIVE STUDY; 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 (Juvenile Hormones); 4602-84-0 (Farnesol); 97C5T2UQ7J (Cholesterol); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 1.1.1.216 (farnesol dehydrogenase); EC 2.1.1.- (Methyltransferases); EC 2.5.1.10 (Geranyltranstransferase); R265G157TQ (farnesal); S5UOB36OCZ (Mevalonic Acid)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160310
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0141084


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[PMID]:26600471
[Au] Autor:Ahmad-Sohdi NA; Seman-Kamarulzaman AF; Mohamed-Hussein ZA; Hassan M
[Ad] Endereço:Institute of Systems Biology, Universiti Kebangsaan Malaysia (UKM), 43600 UKM, Bangi, Selangor, Malaysia.
[Ti] Título:Purification and Characterization of a Novel NAD(P)+-Farnesol Dehydrogenase from Polygonum minus Leaves.
[So] Source:PLoS One;10(11):e0143310, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Juvenile hormones have attracted attention as safe and selective targets for the design and development of environmentally friendly and biorational insecticides. In the juvenile hormone III biosynthetic pathway, the enzyme farnesol dehydrogenase catalyzes the oxidation of farnesol to farnesal. In this study, farnesol dehydrogenase was extracted from Polygonum minus leaves and purified 204-fold to apparent homogeneity by ion-exchange chromatography using DEAE-Toyopearl, SP-Toyopearl, and Super-Q Toyopearl, followed by three successive purifications by gel filtration chromatography on a TSK-gel GS3000SW. The enzyme is a heterodimer comprised of subunits with molecular masses of 65 kDa and 70 kDa. The optimum temperature and pH were 35°C and pH 9.5, respectively. Activity was inhibited by sulfhydryl reagents, metal-chelating agents and heavy metal ions. The enzyme utilized both NAD+ and NADP+ as coenzymes with Km values of 0.74 mM and 40 mM, respectively. Trans, trans-farnesol was the preferred substrate for the P. minus farnesol dehydrogenase. Geometrical isomers of trans, trans-farnesol, cis, trans-farnesol and cis, cis-farnesol were also oxidized by the enzyme with lower activity. The Km values for trans, trans-farnesol, cis, trans-farnesol and cis, cis-farnesol appeared to be 0.17 mM, 0.33 mM and 0.42 mM, respectively. The amino acid sequences of 4 tryptic peptides of the enzyme were analyzed by MALDI-TOF/TOF-MS spectrometry, and showed no significant similarity to those of previously reported farnesol dehydrogenases. These results suggest that the purified enzyme is a novel NAD(P)+-dependent farnesol dehydrogenase. The purification and characterization established in the current study will serve as a basis to provide new information for recombinant production of the enzyme. Therefore, recombinant farnesol dehydrogenase may provide a useful molecular tool in manipulating juvenile hormone biosynthesis to generate transgenic plants for pest control.
[Mh] Termos MeSH primário: Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/isolamento & purificação
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/metabolismo
Folhas de Planta/enzimologia
Polygonum/enzimologia
[Mh] Termos MeSH secundário: Concentração de Íons de Hidrogênio
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 1.1.1.216 (farnesol dehydrogenase)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151125
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0143310


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[PMID]:26463132
[Au] Autor:Fujii M; Kitagawa Y; Iida S; Kato K; Ono M
[Ad] Endereço:School of Pharmacy, International University of Health and Welfare, 2600-1 Kitakanemaru, Ohtawara, Tochigi 324-8501, Japan; Faculty of Pharmaceutical Sciences, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan. Electronic address: mfujii@iuhw.ac.jp.
[Ti] Título:Novel concept of enzyme selective nicotinamide adenine dinucleotide (NAD)-modified inhibitors based on enzyme taxonomy from the diphosphate conformation of NAD.
[So] Source:Bioorg Med Chem Lett;25(22):5133-6, 2015 Nov 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The dihedral angle θ of the diphosphate part of NAD(P) were investigated to distinguish the differences in the binding-conformation of NAD(P) to enzymes and to create an enzyme taxonomy. Furthermore, new inhibitors with fixed dihedral angles showed that enzymes could recognize the differences in the dihedral angle θ. We suggest the taxonomy and the dihedral angle θ are important values for chemists to consider when designing inhibitors and drugs that target enzymes.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/química
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/química
NAD/análogos & derivados
NAD/química
Oxirredutases/química
Tiazóis/química
[Mh] Termos MeSH secundário: Animais
Galinhas
Cinética
Conformação Molecular
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/antagonistas & inibidores
Oxirredutases/antagonistas & inibidores
Oxirredutases/classificação
Fosfotransferases (Aceptor do Grupo Álcool)/antagonistas & inibidores
Fosfotransferases (Aceptor do Grupo Álcool)/química
Saccharomyces cerevisiae
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Thiazoles); 0U46U6E8UK (NAD); EC 1.- (Oxidoreductases); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.23 (NAD kinase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:151031
[Lr] Data última revisão:
151031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151015
[St] Status:MEDLINE


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[PMID]:26289300
[Au] Autor:Arneaud SL; Porter JR
[Ad] Endereço:Department of Biological Sciences, University of the Sciences, 600 South 43rd Street, Philadelphia, PA, 19104, USA. sarneaud@mail.usciences.edu.
[Ti] Título:Investigation and Expression of the Secoisolariciresinol Dehydrogenase Gene Involved in Podophyllotoxin Biosynthesis.
[So] Source:Mol Biotechnol;57(11-12):961-73, 2015 Dec.
[Is] ISSN:1559-0305
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Podophyllotoxin (PPT) is a plant natural product that serves as a precursor for the synthesis of many well-known chemotherapeutic drugs. The limited availability and high demand for the source plants of PPT have led to the exploration of alternative sources for this compound. In this study, we utilized the endophytic fungus Phialocephala podophylli (strain PPE7) that we isolated from the rhizomes of Podophyllum peltatum and is known to produce detectable amounts of PPT in broth culture. To date, the complete PPT biosynthetic pathway has yet to be determined in any species. Since fungi are well known for clustering genes that belong to secondary metabolite pathways, use of a fungal system for investigation of the PPT biosynthesis genes may ultimately lead to elucidation of the entire pathway. In this study, we investigated the secoisolariciresinol dehydrogenase (SD) gene that facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in PPT biosynthesis. We utilized PCR amplification to acquire the complete SD gene sequence in PPE7 and opted to synthesize the P. peltatum SD sequence for expression. Through western blotting, we confirmed the expression of the recombinant SD (PpSD) and verified protein functionality with a bioconversion assay followed by HPLC and LC-MS analyses. Here, we report the identification of the SD gene in PPE7; this is the first report of the SD gene in an endophytic fungus. Additionally, we established the groundwork for the future expression of the complete PPT biosynthetic pathway in the heterologous host Pichia pastoris.
[Mh] Termos MeSH primário: Ascomicetos/enzimologia
Proteínas Fúngicas/metabolismo
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/metabolismo
Podofilotoxina/biossíntese
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Ascomicetos/genética
Ascomicetos/isolamento & purificação
Sequência de Bases
Vias Biossintéticas
Clonagem Molecular
Meios de Cultura
DNA Fúngico/genética
Proteínas Fúngicas/genética
Dados de Sequência Molecular
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/genética
Podophyllum peltatum/microbiologia
Conformação Proteica
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Culture Media); 0 (DNA, Fungal); 0 (Fungal Proteins); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 1.1.1.331 (secoisolariciresinol dehydrogenase); L36H50F353 (Podophyllotoxin)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150821
[St] Status:MEDLINE
[do] DOI:10.1007/s12033-015-9888-8


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[PMID]:26143925
[Au] Autor:Benavente R; Esteban-Torres M; Kohring GW; Cortés-Cabrera Á; Sánchez-Murcia PA; Gago F; Acebrón I; de las Rivas B; Muñoz R; Mancheño JM
[Ad] Endereço:Department of Crystallography and Structural Biology, Institute of Physical Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
[Ti] Título:Enantioselective oxidation of galactitol 1-phosphate by galactitol-1-phosphate 5-dehydrogenase from Escherichia coli.
[So] Source:Acta Crystallogr D Biol Crystallogr;71(Pt 7):1540-54, 2015 Jul.
[Is] ISSN:1399-0047
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Galactitol-1-phosphate 5-dehydrogenase (GPDH) is a polyol dehydrogenase that belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily. It catalyses the Zn(2+)- and NAD(+)-dependent stereoselective dehydrogenation of L-galactitol 1-phosphate to D-tagatose 6-phosphate. Here, three crystal structures of GPDH from Escherichia coli are reported: that of the open state of GPDH with Zn(2+) in the catalytic site and those of the closed state in complex with the polyols Tris and glycerol, respectively. The closed state of GPDH reveals no bound cofactor, which is at variance with the conformational transition of the prototypical mammalian liver alcohol dehydrogenase. The main intersubunit-contacting interface within the GPDH homodimer presents a large internal cavity that probably facilitates the relative movement between the subunits. The substrate analogue glycerol bound within the active site partially mimics the catalytically relevant backbone of galactitol 1-phosphate. The glycerol binding mode reveals, for the first time in the polyol dehydrogenases, a pentacoordinated zinc ion in complex with a polyol and also a strong hydrogen bond between the primary hydroxyl group and the conserved Glu144, an interaction originally proposed more than thirty years ago that supports a catalytic role for this acidic residue.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Escherichia coli/química
Escherichia coli/metabolismo
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/química
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Domínio Catalítico
Cátions Bivalentes/metabolismo
Cristalografia por Raios X
Glicerol/metabolismo
Modelos Moleculares
Dados de Sequência Molecular
NAD/metabolismo
Oxirredução
Conformação Proteica
Alinhamento de Sequência
Estereoisomerismo
Trometamina/metabolismo
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cations, Divalent); 0 (Escherichia coli Proteins); 023C2WHX2V (Tromethamine); 0U46U6E8UK (NAD); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 1.1.1.251 (galactitol-1-phosphate 5-dehydrogenase, E coli); J41CSQ7QDS (Zinc); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150707
[Lr] Data última revisão:
150707
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150707
[St] Status:MEDLINE
[do] DOI:10.1107/S1399004715009281


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[PMID]:25143316
[Au] Autor:Amaya I; Osorio S; Martinez-Ferri E; Lima-Silva V; Doblas VG; Fernández-Muñoz R; Fernie AR; Botella MA; Valpuesta V
[Ad] Endereço:Instituto Andaluz de Investigación y Formación Agraria y Pesquera (IFAPA), Centro de Churriana, Málaga, Spain.
[Ti] Título:Increased antioxidant capacity in tomato by ectopic expression of the strawberry D-galacturonate reductase gene.
[So] Source:Biotechnol J;10(3):490-500, 2015 Mar.
[Is] ISSN:1860-7314
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Increasing L-ascorbic acid (AsA, vitamin C) content in fruits is a common goal in current breeding programs due to its beneficial effect on human health. Attempts to increase AsA content by genetic engineering have resulted in variable success likely due to AsA's complex regulation. Here, we report the effect of ectopically expressing in tomato the D-galacturonate reductase (FaGalUR) gene from strawberry, involved in AsA biosynthesis, either under the control of the constitutive 35S or the tomato fruit-specific polygalucturonase (PG) promoters. Although transgenic lines showed a moderate increase on AsA content, complex changes in metabolites were found in transgenic fruits. Metabolomic analyses of ripe fruits identified a decrease in citrate, glutamate, asparagine, glucose, and fructose, accompanied by an increase of sucrose, galactinol, and chlorogenic acid. Significant metabolic changes also occurred in leaves of 35S-FaGalUR lines, which showed higher non-photochemical fluorescence quenching (NPQ), indicative of a higher constitutive photo-protective capacity. Overall, overexpression of FaGalUR increased total antioxidant capacity in fruits and the results suggest a tight control of AsA content, probably linked to a complex regulation of cellular redox state and metabolic adjustment.
[Mh] Termos MeSH primário: Antioxidantes/metabolismo
Expressão Ectópica do Gene
Fragaria/enzimologia
Lycopersicon esculentum/genética
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/metabolismo
Plantas Geneticamente Modificadas/metabolismo
[Mh] Termos MeSH secundário: Ácido Ascórbico/metabolismo
Frutas/metabolismo
Regulação da Expressão Gênica de Plantas
Genes de Plantas
Seres Humanos
Lycopersicon esculentum/metabolismo
Metabolômica/métodos
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/genética
Folhas de Planta/metabolismo
Regiões Promotoras Genéticas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antioxidants); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 1.1.1.365 (D-galacturonate reductase); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:150316
[Lr] Data última revisão:
150316
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140822
[St] Status:MEDLINE
[do] DOI:10.1002/biot.201400279


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[PMID]:25003994
[Au] Autor:Naganuma T; Kihara A
[Ad] Endereço:Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
[Ti] Título:Two modes of regulation of the fatty acid elongase ELOVL6 by the 3-ketoacyl-CoA reductase KAR in the fatty acid elongation cycle.
[So] Source:PLoS One;9(7):e101823, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fatty acids (FAs) are diverse molecules, and such diversity is important for lipids to exert their functions under several environmental conditions. FA elongation occurs at the endoplasmic reticulum and produces a variety of FA species; the FA elongation cycle consists of four distinct enzyme reactions. For this cycle to be driven efficiently, there must exist coordinated regulation of protein components of the FA elongation machinery. However, such regulation is poorly understood. In the present study, we performed biochemical analyses using the FA elongase ELOVL6 and the 3-ketoacyl-CoA reductase KAR, which catalyze the first and second steps of the FA elongation cycle, respectively. In vitro FA elongation assays using membrane fractions demonstrated that ELOVL6 activity was enhanced ∼10-fold in the presence of NADPH, although ELOVL6 itself did not require NADPH for its catalysis. On the other hand, KAR does use NADPH as a reductant in its enzyme reaction. Activity of purified ELOVL6 was enhanced by ∼3-fold in the presence of KAR. This effect was KAR enzyme activity-independent, since it was observed in the absence of NADPH and in the KAR mutant. However, ELOVL6 enzyme activity was further enhanced in a KAR enzyme activity-dependent manner. Therefore, KAR regulates ELOVL6 via two modes. In the first mode, KAR may induce conformational changes in ELOVL6 to become structure that can undergo catalysis. In the second mode, conversion of 3-ketoacyl-CoA to 3-hydroxyacyl-CoA by KAR may facilitate release of the product from the presumed ELOVL6-KAR complex.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Ácidos Graxos/biossíntese
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/fisiologia
[Mh] Termos MeSH secundário: Acetiltransferases/química
Acil Coenzima A/metabolismo
Vias Biossintéticas
Células HEK293
Células HeLa
Seres Humanos
Cinética
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)/química
Saccharomyces cerevisiae
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Fatty Acids); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (fatty acid elongases)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140709
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0101823


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[PMID]:24790007
[Au] Autor:Sato-Masumoto N; Ito M
[Ad] Endereço:Department of Pharmacognosy, Graduate School of Pharmaceutical Sciences, Kyoto University.
[Ti] Título:Isolation and characterization of isopiperitenol dehydrogenase from piperitenone-type Perilla.
[So] Source:Biol Pharm Bull;37(5):847-52, 2014.
[Is] ISSN:1347-5215
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Studying the biosynthesis of oil compounds in Perilla will help to elucidate regulatory systems for secondary metabolites and reaction mechanisms for natural product synthesis. In this study, two types of alcohol dehydrogenases, isopiperitenol dehydrogenases 1 and 2 (ISPD1 and ISPD2), which are thought to participate the oxidation of isopiperitenol in the biosynthesis of perilla, were isolated from three pure lines of perilla. Both ISPD1 and ISPD2 oxidized isopiperitenol into isopiperitenone with an oxidized form of nicotinamide adenine dinucleotide (NAD(+)) cofactor. ISPD1 used both isopiperitenol diastereomers, whereas ISPD2 used cis-isomer as a substrate. However, only ISPD2 was isolated from piperitenone-type perilla. These results suggests that in perilla, ISPD2 is related to the biosynthesis of piperitenone, which was formed via (-)-cis-isopiperitenol.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/isolamento & purificação
Oxirredutases do Álcool/metabolismo
Monoterpenos/metabolismo
Perilla/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Vias Biossintéticas
Clonagem Molecular
Dados de Sequência Molecular
NAD/metabolismo
Álcool Oxidorredutases Dependentes de NAD(+) e NADP(+)
Óleos Voláteis
Terpenos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Monoterpenes); 0 (Oils, Volatile); 0 (Terpenes); 0U46U6E8UK (NAD); 491-05-4 (isopiperitenol); 529-01-1 (isopiperitenone); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.- (NAD (+) and NADP (+) Dependent Alcohol Oxidoreductases); EC 1.1.1.223 (isopiperitenol dehydrogenase); IKR841W74D (piperitenone)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140503
[St] Status:MEDLINE



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