Song, Jianling; Zou, Xiaoyan; Liu, Pandao; Cardoso, Juan Andres; Schultze-Kraft, Rainer; Liu, Guodao; Luo, Lijuan; Chen, Zhijian published the artcile< Differential expressions and enzymatic properties of malate dehydrogenases in response to nutrient and metal stresses in Stylosanthes guianensis>, Reference of 112-63-0, the main research area is Stylosanthes malate dehydrogenase nutrient metal stress; Enzymatic properties; Gene expression; Malate; Malate dehydrogenase; Metal stress; Nutrient deficiency; Stylosanthes guianensis.
Malate dehydrogenase (MDH, EC 1.1.1.37) is a key enzyme that catalyzes a reversible NAD-dependent dehydrogenase reaction from oxaloacetate (OAA) to malate. Although MDH has been documented to participate in cellular metabolism and redox homeostasis in plants, the roles of MDH members in the tropical legume Stylosanthes guianensis (stylo) remain less definitive. In this study, except SgMDH1 that had been previously characterized, six novel MDH genes were isolated from stylo and were then designated as SgMDH2 to SgMDH7. All of the SgMDH proteins possessed the common features of NAD binding, dimerization interface and substrate binding sites. Expression anal. showed that three SgMDHs exhibited preferential expressions in leaves, and one SgMDH was mainly expressed in roots. Furthermore, SgMDHs were regulated by nutrient deficiencies in stylo roots, especially for phosphorus (-P) and potassium (-K) deficiencies. Differential responses of SgMDHs to trace metal stress and heavy metal toxicity were observed in stylo roots, suggesting the involvement of SgMDHs in the response of stylo to metal stresses. The six novel SgMDHs were subsequently expressed and purified from Escherichia coli to analyze their biochem. properties. Although SgMDHs exhibited variations in subcellular localizations, each SgMDH protein displayed a high level of catalytic efficiency towards OAA and NADH but a low level of catalytic efficiency towards malate and NAD+. In addition, the activities of recombinant SgMDH proteins were pH-dependent and temperature-sensitive, and exhibited differential regulations by various metal ions. These results together suggest the potential roles of SgMDHs in stylo coping with nutrient and metal stresses. The sequence data of the six novel SgMDHs were deposited in GenBank under accession numbers OK188912, OK188913, OK188914, OK188915, OK188916 and OK188917 for SgMDH2 to SgMDH7, resp.
Plant Physiology and Biochemistry (Issy-les-Moulineaux, France) published new progress about Chlorophylls Role: BSU (Biological Study, Unclassified), BIOL (Biological Study). 112-63-0 belongs to class esters-buliding-blocks, and the molecular formula is C19H34O2, Reference of 112-63-0.
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