Molecular cloning of wheat dihydrodipicolinate synthase.
نویسندگان
چکیده
منابع مشابه
Characterization of Dihydrodipicolinate Synthase from Pea
Dihydrodipicolinate synthase (EC 4.2.1.52), the first enzyme unique to lysine biosynthesis in bacteria and higher plants, has been purified to homogeneity from etiolated pea (Pisum sativum) seedlings using a combination of conventional and affinity chromatographic steps. This is the first report on a homogeneous preparation of native dihydrodipicolinate synthase from a plant source. The pea dih...
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A novel type of threonine-producing strains, dihydrodipicolinate synthase (DPS)-defective mutants of Brevibacterium flavum, was isolated as alpha-amino-beta-hydroxyvaleric acid (AHV)-resistant producers. The third selection markers used were a strong lysine inhibition of threonine production and a lower production of lysine than that of threonine in those derived from strains with feedback-sens...
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Ethylene response factor proteins are important for regulating gene expression under different stresses. Different isoforms for ERF have previously isolated from bread wheat (Triticum aestivum L.) and related genera and called from TaERF1 to TaERF5. We isolated, cloned and molecular characterized a novel one based on TdERF1, an isoform in durum wheat (Tri...
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Cys biosynthesis in higher plants occurs by a process similar to that known in microorganisms (Kredich, 1987). Cys synthase [O-acetylserine (thio1)-lyase, EC 4.2.99.81 catalyzes the formation of Cys from O-acetylserine and free or carrier-bound sulfide. Cys synthase has been purified from various plants and microorganisms and has been shown to have a molecular mass of 52 to 70 kD. The plant enz...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)38184-5