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s adenosylmethionine/batata
O link é salvo na área de transferência
Página 1 a partir de 17 resultados
Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of potato.
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S-adenosylmethionine decarboxylase (SAMDC) is involved in the biosynthesis of the polyamines, spermidine and spermine. Recently, we reported the isolation of a putative cDNA clone of the SAMDC clone of potato (Plant Mol Biol 20; 641-651). In order to confirm that the potato genes does encode SAMDC,
Manipulation of S-adenosylmethionine decarboxylase activity in potato tubers. An increase in activity leads to an increase in tuber number and a change in tuber size distribution.
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S-Adenosylmethionine decarboxylase (SAMDC; EC 4.1.1.50) is a key enzyme in the biosynthesis of the polyamines spermidine and spermine from putrescine and its activity is rate limiting in this pathway. Transgenic potato (Solanum tuberosum L. cv. Desiree) plants containing both sense and antisense
Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes.
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S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl enzyme, and the pyruvate is formed in an intramolecular reaction that cleaves a proenzyme precursor and converts a serine residue into pyruvate. The wild type potato AdoMetDC proenzyme processed much faster than the human proenzyme and did
Novel properties of malarial S-adenosylmethionine decarboxylase as revealed by structural modelling.
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In the malaria parasite, the two main regulatory activities of polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) occur in a single bifunctional protein. The AdoMetDC domain was modeled using the human and potato X-ray crystal structures as
Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase.
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S-adenosylmethionine decarboxylase (AdoMetDC) is a critical regulatory enzyme of the polyamine biosynthetic pathway and belongs to a small class of pyruvoyl-dependent amino acid decarboxylases. Structural elucidation of the prokaryotic AdoMetDC is of substantial interest in order to determine the
Cloning, functional identification and structural modelling of Vitis vinifera S-adenosylmethionine decarboxylase.
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In this paper we report the cloning and full sequencing of S-adenosylmethionine decarboxylase (SAMDC, EC 4.1.1.50) cDNA from Vitis vinifera L. (VV) leaves, an enzyme belonging to the polyamine biosynthetic pathway, which appears to play an important role in the regulation of plant growth and
Cloning and characterization of leaf senescence up-regulated genes in sweet potato.
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Genes that are expressed during leaf senescence in sweet potato (Ipomoea batatas, cv. Tainong 57) were identified by the isolation of cDNA fragments with the mRNA differential display method. Eight senescence-associated cDNA clones for mRNAs differentially expressed during leaf senescence were
Regulation of aspartate-derived amino acid homeostasis in potato plants (Solanum tuberosum L.) by expression of E. coli homoserine kinase.
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The availability of the carbon backbone O-phosphohomoserine (OPHS) is critical to methionine (met) and threonine (thr) synthesis. OPHS derives from homoserine and is formed by homoserine kinase (HSK). To clarify the function of HSK in cellular metabolism, the E. coli HSK ortholog thrB was expressed
Expression and sequence analysis of cDNAs induced during the early stages of tuberisation in different organs of the potato plant (Solanum tuberosum L.).
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cDNA clones of two genes (TUB8 and TUB13) which show a 25-30-fold increase in transcript in the stolon tip during the early stages of tuberisation, have been isolated by differential screening. These genes are also expressed in leaves, stems and roots and the expression pattern in these organs
Polyamine metabolism of potato seed-tubers during long-term storage and early sprout development.
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Growth potential of potato (Solanum tuberosum L.) plants is influenced by seed-tuber age. After 24 days of growth, single-eye seedcores from 7-month-old seed-tubers produced 64% more foliar dry matter than those from 19-month-old seed-tubers, reflecting a higher growth rate. This study was initiated
Monomeric S-adenosylmethionine decarboxylase from plants provides an alternative to putrescine stimulation.
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S-Adenosylmethionine decarboxylase has been implicated in cell growth and differentiation and is synthesized as a proenzyme, which undergoes autocatalytic cleavage to generate an active site pyruvoyl group. In mammals, S-adenosylmethionine decarboxylase is active as a dimer in which each protomer
Immunolocalisation of spermidine synthase in Solanum tuberosum.
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Spermidine synthase (SPDS) catalyses the formation of spermidine, which is an essential polyamine and widespread in living organisms. Spermidine is formed from putrescine by transfer of an aminopropyl group from decarboxylated S-adenosylmethionine. Spermidine is also a precursor to further
Engineering of cysteine and methionine biosynthesis in potato.
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Methionine and cysteine, two amino acids containing reduced sulfur, are not only an important substrate of protein biosynthesis but are also precursors of various other metabolites such as glutathione, phytochelatines, S-adenosylmethionine, ethylene, polyamines, biotin, and are involved as methyl
Characterization and expression of two members of the S-adenosylmethionine decarboxylase gene family in carnation flower.
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S-adenosylmethionine decarboxylase (SAMDC; EC 4.1.4.50) is one of the key enzymes in polyamine biosynthesis, and the product of its catalytic reaction, decarboxylated S-adenosylmethionine (dcSAM), serves as an aminopropyl donor in the biosynthesis of spermidine and spermine. In order to provide
Structural biology of S-adenosylmethionine decarboxylase.
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S-adenosylmethionine decarboxylase (AdoMetDC) is a critical enzyme in the polyamine biosynthetic pathway and a subject of many structural and biochemical investigations for anti-cancer and anti-parasitic therapy. The enzyme undergoes an internal serinolysis reaction as a post-translational
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