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  1 / 270 MEDLINE  
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[PMID]:28648602
[Au] Autor:Zhang H; Au SWN
[Ad] Endereço:Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong.
[Ti] Título:Helicobacter pylori does not use spermidine synthase to produce spermidine.
[So] Source:Biochem Biophys Res Commun;490(3):861-867, 2017 Aug 26.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Helicobacter pylori is the primary pathogen associated to gastritis and gastric cancer. Growth of H. pylori depends on the availability of spermidine in vivo. Interestingly, the genome of H. pylori contains an incomplete set of genes for the classical pathway of spermidine biosynthesis. It is thus not clear whether some other genes remained in the pathway would have any functions in spermidine biosynthesis. Here, we study spermidine synthase, which is responsible for the final catalytic process in the classical route. Protein sequence alignment reveals that H. pylori SpeE (HpSpeE) lacks key residues for substrate binding. By using isothermal titration calorimetry, we show that purified recombinant HpSpeE does not interact with the putative substrates putrescine and decarboxylated S-adenosylmethionine, and the product spermidine. High performance liquid chromatography analysis further demonstrates that HpSpeE has no detectable in vitro enzymatic activity. Additionally, intracellular spermidine level in speE-null mutant strain is comparable to that in the wild type strain. Collectively, our results suggest that HpSpeE is functionally distinct from spermidine production. H. pylori may instead employ the alternative pathway for spermidine synthesis which is dominantly exploited by other human gut microbes.
[Mh] Termos MeSH primário: Helicobacter pylori/enzimologia
Helicobacter pylori/metabolismo
Espermidina Sintase/metabolismo
Espermidina/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Infecções por Helicobacter/microbiologia
Helicobacter pylori/química
Seres Humanos
Putrescina/metabolismo
S-Adenosilmetionina/análogos & derivados
S-Adenosilmetionina/metabolismo
Alinhamento de Sequência
Espermidina Sintase/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
22365-13-5 (S-adenosyl-3-methylthiopropylamine); 7LP2MPO46S (S-Adenosylmethionine); EC 2.5.1.16 (Spermidine Synthase); U87FK77H25 (Spermidine); V10TVZ52E4 (Putrescine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE


  2 / 270 MEDLINE  
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[PMID]:28299555
[Au] Autor:Pothipongsa A; Jantaro S; Salminen TA; Incharoensakdi A
[Ad] Endereço:Laboratory of Cyanobacterial Biotechnology, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand.
[Ti] Título:Molecular characterization and homology modeling of spermidine synthase from Synechococcus sp. PCC 7942.
[So] Source:World J Microbiol Biotechnol;33(4):72, 2017 Apr.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Spermidine synthase (Spds) catalyzes the formation of spermidine by transferring the aminopropyl group from decarboxylated S-adenosylmethionine (dcSAM) to putrescine. The Synechococcus spds gene encoding Spds was expressed in Escherichia coli. The purified recombinant enzyme had a molecular mass of 33 kDa and showed optimal activity at pH 7.5, 37 °C. The enzyme had higher affinity for dcSAM (K , 20 µM) than for putrescine (K , 111 µM) and was highly specific towards the diamine putrescine with no activity observed towards longer chain diamines. The three-dimensional structural model for Synechococcus Spds revealed that most of the ligand binding residues in Spds from Synechococcus sp. PCC 7942 are identical to those of human and parasite Spds. Based on the model, the highly conserved acidic residues, Asp89, Asp159 and Asp162, are involved in the binding of substrates putrescine and dcSAM and Pro166 seems to confer substrate specificity towards putrescine.
[Mh] Termos MeSH primário: Putrescina/metabolismo
S-Adenosilmetionina/metabolismo
Espermidina Sintase/química
Espermidina Sintase/metabolismo
Synechococcus/enzimologia
[Mh] Termos MeSH secundário: Asparagina/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Seres Humanos
Concentração de Íons de Hidrogênio
Modelos Moleculares
Peso Molecular
Prolina/metabolismo
Ligação Proteica
Homologia de Sequência do Ácido Nucleico
Espermidina Sintase/genética
Homologia Estrutural de Proteína
Especificidade por Substrato
Synechococcus/química
Synechococcus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 7006-34-0 (Asparagine); 7LP2MPO46S (S-Adenosylmethionine); 9DLQ4CIU6V (Proline); EC 2.5.1.16 (Spermidine Synthase); V10TVZ52E4 (Putrescine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-017-2242-5


  3 / 270 MEDLINE  
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[PMID]:27930671
[Au] Autor:Yang J; Saggiomo V; Velders AH; Cohen Stuart MA; Kamperman M
[Ad] Endereço:Laboratory of Physical Chemistry and Soft Matter, Wageningen University, Wageningen, the Netherlands.
[Ti] Título:Reaction Pathways in Catechol/Primary Amine Mixtures: A Window on Crosslinking Chemistry.
[So] Source:PLoS One;11(12):e0166490, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Catechol chemistry is used as a crosslinking tool abundantly in both natural organisms (e.g. mussels, sandcastle worms) and synthetic systems to achieve the desired mechanical properties. Despite this abundance and success, the crosslinking chemistry is still poorly understood. In this study, to simplify the system, yet to capture the essential chemistry, model compounds 4-methyl catechol and propylamine are used. The reaction of 4-methyl catechol (2 mM) with propylamine (6 mM) is carried out in the presence of NaIO4 (2 mM) in 10 mM Na2CO3 aqueous solution. A variety of spectroscopic/spectrometric and chromatographic methods such as 1H NMR, LC-MS, and UV-VIS are used to track the reaction and identify the products/intermediates. It is found that the crosslinking chemistry of a catechol and an amine is both fast and complicated. Within five minutes, more than 60 products are formed. These products encompass 19 different masses ranging from molecular weight of 179 to 704. By combining time-dependent data, it is inferred that the dominant reaction pathways: the majority is formed via aryloxyl-phenol coupling and Michael-type addition, whereas a small fraction of products is formed via Schiff base reactions.
[Mh] Termos MeSH primário: Aminas Biogênicas/química
Catecolaminas/química
[Mh] Termos MeSH secundário: Catecóis/química
Cromatografia Líquida
Espectroscopia de Ressonância Magnética
Espectrometria de Massas
Ácido Periódico/química
Espectroscopia Fotoeletrônica
Bases de Schiff/química
Espermidina Sintase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biogenic Amines); 0 (Catecholamines); 0 (Catechols); 0 (Schiff Bases); 10450-60-9 (Periodic Acid); 12GLI7JGB3 (4-methylcatechol); B45A1BUM4Q (metaperiodate); EC 2.5.1.16 (Spermidine Synthase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161209
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0166490


  4 / 270 MEDLINE  
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[PMID]:27460582
[Au] Autor:Pothipongsa A; Jantaro S; Incharoensakdi A
[Ad] Endereço:Laboratory of Cyanobacterial Biotechnology, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand.
[Ti] Título:Spermidine Synthase is Required for Growth of Synechococcus sp. PCC 7942 Under Osmotic Stress.
[So] Source:Curr Microbiol;73(5):639-45, 2016 Nov.
[Is] ISSN:1432-0991
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Synechococcus sp. PCC 7942 spermidine synthase encoded by spds gene (Synpcc7942_0628) is responsible for spermidine biosynthesis. Two Synechococcus strains, the overexpressing spds (OX-spds) and the spds knockout (Δspds), were constructed and characterized for their growth and photosynthetic efficiency under osmotic stress imposed by sorbitol. The growth of Δspds was completely inhibited when cells were grown in the presence of 400 mM sorbitol. Under the same condition, the OX-spds showed a slightly higher growth than the wild type. The OX-spds under osmotic stress also had a significant increase of spermidine level in conjunction with the up-regulation of the genes involved in spermidine biosynthesis. A higher ratio of spermidine to putrescine, an index for stress tolerance, under osmotic stress was found in the OX-spds strain than in the wild type. Overall results indicated that the spermidine synthase enzyme plays an essential role in the survival of Synechococcus sp. PCC 7942 under osmotic stress.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Espermidina Sintase/metabolismo
Synechococcus/enzimologia
Synechococcus/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Viabilidade Microbiana
Pressão Osmótica
Espermidina Sintase/genética
Synechococcus/química
Synechococcus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 2.5.1.16 (Spermidine Synthase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160728
[St] Status:MEDLINE
[do] DOI:10.1007/s00284-016-1107-8


  5 / 270 MEDLINE  
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[PMID]:26881725
[Au] Autor:Yamasaki K; Tani O; Tateishi Y; Tanabe E; Namatame I; Niimi T; Furukawa K; Sakashita H
[Ad] Endereço:Biomedical Research Institute , National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, 305-8566, Japan.
[Ti] Título:An NMR Biochemical Assay for Fragment-Based Drug Discovery: Evaluation of an Inhibitor Activity on Spermidine Synthase of Trypanosoma cruzi.
[So] Source:J Med Chem;59(5):2261-6, 2016 Mar 10.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although NMR in fragment-based drug discovery is utilized almost exclusively to evaluate physical binding between molecules, it should be also a powerful tool for biochemical assay, evaluating inhibitory effect of compounds on enzymatic activity. Time-dependent spectral change in real-time monitoring or inhibitor concentration-dependent spectral change after constant-time reaction was processed by factor analysis, by which reaction rate or IC50 value was obtained. Applications to spermidine synthase of Trypanosoma cruzi, which causes Chagas disease, are described.
[Mh] Termos MeSH primário: Cicloexilaminas/farmacologia
Descoberta de Drogas
Ressonância Magnética Nuclear Biomolecular
Espermidina Sintase/antagonistas & inibidores
Trypanosoma cruzi/enzimologia
[Mh] Termos MeSH secundário: Doença de Chagas/tratamento farmacológico
Cicloexilaminas/síntese química
Cicloexilaminas/química
Relação Dose-Resposta a Droga
Ativação Enzimática/efeitos dos fármacos
Estrutura Molecular
Espermidina Sintase/metabolismo
Relação Estrutura-Atividade
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cyclohexylamines); 6321-23-9 (4-methylcyclohexylamine); EC 2.5.1.16 (Spermidine Synthase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160311
[Lr] Data última revisão:
160311
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160217
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.5b01769


  6 / 270 MEDLINE  
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[PMID]:26362015
[Au] Autor:Das M; Singh S; Dubey VK
[Ad] Endereço:Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Assam, 781039, India.
[Ti] Título:Novel Inhibitors of Ornithine Decarboxylase of Leishmania Parasite (LdODC): The Parasite Resists LdODC Inhibition by Overexpression of Spermidine Synthase.
[So] Source:Chem Biol Drug Des;87(3):352-60, 2016 Mar.
[Is] ISSN:1747-0285
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ornithine decarboxylase (LdODC), a key enzyme in polyamine biosynthesis in Leishmania donovani, catalyzes the conversion of ornithine to putrescine that is finally used for synthesis of spermidine and other polyamines. Inhibition of ornithine decarboxylase is likely to deplete the parasite trypanothione and may result in increased reactive oxygen species (ROS). Sequence as well as structure of LdODC and human ODC shows significant difference; therefore, we have identified novel specific inhibitors of LdODC. These inhibitors are able to inhibit recombinant LdODC and decrease intracellular putrescine concentration showing target specificity. The Ki values of LdODC inhibition do not correlate with IC50 values in Leishmania promastigote possibly due to different stability/pharmacokinetics. These inhibitors, except compound M-5, have only minor effect on Leishmania promastigotes, and IC50 values are several folds higher as compared to Ki values. In case of compound M-5, IC50 value is less than Ki value indicating that the compound may have additional targets. Our studies suggest that the parasite resists these LdODC inhibitors by overexpression of spermidine synthase mRNA.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Leishmania/enzimologia
Ornitina Descarboxilase/efeitos dos fármacos
Espermidina Sintase/metabolismo
[Mh] Termos MeSH secundário: Animais
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Reactive Oxygen Species); EC 2.5.1.16 (Spermidine Synthase); EC 4.1.1.17 (Ornithine Decarboxylase)
[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:150913
[St] Status:MEDLINE
[do] DOI:10.1111/cbdd.12665


  7 / 270 MEDLINE  
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[PMID]:26277788
[Au] Autor:Gupta ED; Pachauri M; Ghosh PC; Rajam MV
[Ad] Endereço:Department of Genetics, University of Delhi South Campus, Benito Juarez Road, New Delhi, 110021, India.
[Ti] Título:Targeting polyamine biosynthetic pathway through RNAi causes the abrogation of MCF 7 breast cancer cell line.
[So] Source:Tumour Biol;37(1):1159-71, 2016 Jan.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The diamine putrescine and polyamines, spermidine (triamine) and spermine (tetraamine) are small organic polycations that play an indispensable role in key cellular processes such as the regulation of growth, differentiation, and macromolecular functions. Elevated levels of polyamines (PAs) have been shown to be one of the major factors involved in carcinogenesis. In this study, specific silencing of the expression of three genes of PA biosynthesis pathway, ornithine decarboxylase (ODC), S-adenosylmethionine decarboxylase (SAMDC), and spermidine synthase (SPDSYN) was achieved using RNA interference in MCF 7 breast cancer cell line. For optimizing the effective small interfering nucleic acid (siNA), three variants of ODC siNA [siRNA, locked nucleic acid (LNA)-modified siRNA, and siHybrid (RNA and DNA hybrid)] were used and a dose- and time-dependent study was conducted. The PA biosynthetic genes were targeted individually and in combination. RNAi-mediated reduction in the expression of PA biosynthesis genes resulted in distorted cell morphology, reduced cancer cell viability, and migration characteristic. The most promising results were observed with the combined treatment of siSPDSYN and siODC with 83 % cell growth inhibition. On analyzing the messenger RNA (mRNA) expression profile of the cell cycle and apoptosis-related genes, it was observed that RNAi against PA biosynthetic genes downregulated the expression of CDK8, CCNE2, CCNH, CCNT1, CCNT2, CCNF, PCNA, CCND1, and CDK2, and upregulated the expression of E2F4, BAX, FAS, TP53, CDKN1A, BAK1, CDKN1B, ATM, GRANB, and ATR genes when compared with control-transfected cells. These results suggest that the targeting polyamine biosynthesis through RNAi approach could be a promising strategy for breast cancer therapy and might be extended for therapy of other cancers.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Poliaminas/química
Interferência de RNA
[Mh] Termos MeSH secundário: Adenosilmetionina Descarboxilase/metabolismo
Apoptose
Neoplasias da Mama/genética
Diferenciação Celular
Divisão Celular
Movimento Celular
Proliferação Celular
Sobrevivência Celular
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Células MCF-7
Ornitina Descarboxilase/metabolismo
Putrescina/biossíntese
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/metabolismo
Espermidina/biossíntese
Espermidina Sintase/metabolismo
Espermina/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyamines); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 2FZ7Y3VOQX (Spermine); EC 2.5.1.16 (Spermidine Synthase); EC 4.1.1.17 (Ornithine Decarboxylase); EC 4.1.1.50 (Adenosylmethionine Decarboxylase); U87FK77H25 (Spermidine); V10TVZ52E4 (Putrescine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150817
[St] Status:MEDLINE
[do] DOI:10.1007/s13277-015-3912-2


  8 / 270 MEDLINE  
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[PMID]:26327378
[Au] Autor:Amano Y; Namatame I; Tateishi Y; Honboh K; Tanabe E; Niimi T; Sakashita H
[Ad] Endereço:Drug Discovery Research, Astellas Pharma Inc., 21 Miyukigaoka, Tsukuba, Ibaraki 305-8585, Japan.
[Ti] Título:Structural insights into the novel inhibition mechanism of Trypanosoma cruzi spermidine synthase.
[So] Source:Acta Crystallogr D Biol Crystallogr;71(Pt 9):1879-89, 2015 Sep.
[Is] ISSN:1399-0047
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Trypanosoma cruzi causes Chagas disease, a severe disease affecting 8-10 million people in Latin America. While nifurtimox and benznidazole are used to treat this disease, their efficacy is limited and adverse effects are observed. New therapeutic targets and novel drugs are therefore urgently required. Enzymes in the polyamine-trypanothione pathway are promising targets for the treatment of Chagas disease. Spermidine synthase is a key enzyme in this pathway that catalyzes the transfer of an aminopropyl group from decarboxylated S-adenosylmethionine (dcSAM) to putrescine. Fragment-based drug discovery was therefore conducted to identify novel, potent inhibitors of spermidine synthase from T. cruzi (TcSpdSyn). Here, crystal structures of TcSpdSyn in complex with dcSAM, trans-4-methylcyclohexylamine and hit compounds from fragment screening are reported. The structure of dcSAM complexed with TcSpdSyn indicates that dcSAM stabilizes the conformation of the `gatekeeping' loop to form the putrescine-binding pocket. The structures of fragments bound to TcSpdSyn revealed two fragment-binding sites: the putrescine-binding pocket and the dimer interface. The putrescine-binding pocket was extended by an induced-fit mechanism. The crystal structures indicate that the conformation of the dimer interface is required to stabilize the gatekeeping loop and that fragments binding to this interface inhibit TcSpdSyn by disrupting its conformation. These results suggest that utilizing the dynamic structural changes in TcSpdSyn that occur upon inhibitor binding will facilitate the development of more selective and potent inhibitors.
[Mh] Termos MeSH primário: Espermidina Sintase/química
Trypanosoma cruzi/enzimologia
[Mh] Termos MeSH secundário: Regulação Alostérica
Animais
Sítios de Ligação
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Ligações de Hidrogênio
Modelos Moleculares
Conformação Proteica
Espermidina Sintase/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); EC 2.5.1.16 (Spermidine Synthase)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:150902
[Lr] Data última revisão:
150902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150902
[St] Status:MEDLINE
[do] DOI:10.1107/S1399004715013048


  9 / 270 MEDLINE  
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[PMID]:26214415
[Au] Autor:You E; Wang Y; Ding ZT; Zhang XF; Pan LL; Zheng C
[Ad] Endereço:Tea Research Institute, Qingdao Agricultural University, Qingdao, Shandong, China.
[Ti] Título:Codon usage bias analysis for the spermidine synthase gene from Camellia sinensis (L.) O. Kuntze.
[So] Source:Genet Mol Res;14(3):7368-76, 2015 Jul 03.
[Is] ISSN:1676-5680
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:The spermidine synthase (SPDS) gene exists widely in all types of plants. In this paper, the codon usage of the SPDS gene from Camellia sinensis (CsSPDS) was analyzed. The results showed that the codon usage of the CsSPDS gene is biased towards the T-ended or A-ended codons, which is similar to that observed in 73 genes selected from the C. sinensis genome. An ENC-plot for 15 SPDS genes from various plant species suggested that mutational bias was the major factor in shaping codon usage in these genes. Codon usage frequency analysis indicated that there was little difference between the CsSPDS gene and dicot genomes, such as Arabidopsis thaliana and Nicotiana tabacum, but significant differences in codon usage were observed between the CsSPDS gene and monocot genomes, such as Triticum aestivum and Zea mays. Therefore, A. thaliana and N. tabacum expression systems may be more suitable for the expression of the CsSPDS gene.
[Mh] Termos MeSH primário: Camellia sinensis/enzimologia
Camellia sinensis/genética
Códon
Espermidina Sintase/genética
[Mh] Termos MeSH secundário: Análise por Conglomerados
Regulação da Expressão Gênica de Plantas
Genoma de Planta
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Codon); EC 2.5.1.16 (Spermidine Synthase)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:150728
[Lr] Data última revisão:
150728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150728
[St] Status:MEDLINE
[do] DOI:10.4238/2015.July.3.12


  10 / 270 MEDLINE  
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[PMID]:26056006
[Au] Autor:Imamura T; Fujita K; Tasaki K; Higuchi A; Takahashi H
[Ad] Endereço:Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijuku, Katsushika, Tokyo 125-8585, Japan.
[Ti] Título:Characterization of spermidine synthase and spermine synthase--The polyamine-synthetic enzymes that induce early flowering in Gentiana triflora.
[So] Source:Biochem Biophys Res Commun;463(4):781-6, 2015 Aug 07.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polyamines are essential for several living processes in plants. However, regulatory mechanisms of polyamines in herbaceous perennial are almost unknown. Here, we identified homologs of two Arabidopsis polyamine-synthetic enzymes, spermidine synthase (SPDS) and spermine synthase (SPMS) denoted as GtSPDS and GtSPMS, from the gentian plant, Gentiana triflora. Our results showed that recombinant proteins of GtSPDS and GtSPMS possessed SPDS and SPMS activities, respectively. The expression levels of GtSPDS and GtSPMS increased transiently during vegetative to reproductive growth phase and overexpression of the genes hastened flowering, suggesting that these genes are involved in flowering induction in gentian plants.
[Mh] Termos MeSH primário: Poliaminas Biogênicas/biossíntese
Flores/crescimento & desenvolvimento
Gentiana/fisiologia
Espermidina Sintase/metabolismo
Espermina Sintase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Arabidopsis/genética
Genes de Plantas
Gentiana/genética
Gentiana/metabolismo
Dados de Sequência Molecular
Plantas Geneticamente Modificadas
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência de Aminoácidos
Espermidina Sintase/química
Espermidina Sintase/genética
Espermina Sintase/química
Espermina Sintase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biogenic Polyamines); 0 (Recombinant Proteins); EC 2.5.1.16 (Spermidine Synthase); EC 2.5.1.22 (Spermine Synthase)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150708
[Lr] Data última revisão:
150708
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150610
[St] Status:MEDLINE



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