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  • 1
    Electronic Resource
    Electronic Resource
    The role of nicotianamine synthase in response to Fe nutrition status in Gramineae (1996)
    Springer
    Plant and soil 178 (1996), S. 171-177 
    Details
    ISSN: 1573-5036
    Keywords: Fe-deficiency ; graminaceous plant ; mugineic acids ; phytosiderophore ; nicotianamine synthase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Nicotianamine is an intermediate for the biosynthesis of mugineic acid-family phytosiderophores (MAs) in the Gramineae and a key substance for iron metabolism in dicots. Nicotianamine synthase catalyzes the formation of nicotianamine from S-adenosylmethionine. Nicotianamine synthase activity was induced in barley roots at the 3rd day after withholding Fe supply and declined within one day followmg the supply of Fe3+-epihydroxymugineic acid. The induction of nicotianamine synthase activity by Fe-deficiency was observed also in sorghum, maize, and rye, and the level of nicotianamine synthase activity was highly associated with the MAs secreted among graminaceous plant tested. Therefore, the nicotianamine synthase gene may be a suitable candidate for making a transgenic plant tolerant to Fe-deficiency.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00011580
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and characterization of nicotianamine synthase from Fe-deficient barley roots (1994)
    Springer
    Plant and soil 165 (1994), S. 173-179 
    Details
    ISSN: 1573-5036
    Keywords: barley roots ; Fe-deficiency ; mugineic acid ; nicotianamine synthase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Nicotianamine (NA), the key precursor of the mugineic acid family phytosiderophores (MAs), is synthesized from S-adenosylmethionine (SAM). The NA synthase was strongly induced by Fe-deficiency treatment, and the activity increased to the maximum level faster than the time of maximum level of MAs secretion and also before the appearance of severest chlorosis. The enzyme was mainly localized in the roots of barley. NA synthase had the optimum pH at 9.0, a molecular weight of about 40,000∼50,000 estimated by gel filtration or about 30,000 by SDS-PAGE. Using hydrophobic chromatography, hydroxylapatite chromatography, and preparative SDS-PAGE, NA synthase was purified as one band on SDS-PAGE.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00008059
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    Paper (German National Licenses)
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