Nicotianamine synthase (NAS), the key enzyme in the biosynthetic pathway for the mugineic acid family of phytosiderophores, catalyzes the trimerization of S-adenosylmethionine to form one molecule of nicotianamine. We purified NAS protein and isolated the genes nas1, nas2, nas3, nas4, nas5-1, nas5-2, and nas6, which encode NAS and NAS-like proteins from Fe-deficient barley (Hordeum vulgare L. cv Ehimehadaka no. 1) roots. Escherichia coli expressing nas1 showed NAS activity, confirming that this gene encodes a functional NAS. Expression of nas genes as determined by northern-blot analysis was induced by Fe deficiency and was root specific. The NAS genes form a multigene family in the barley and rice genomes.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Nicotianamine synthase (NAS), the key enzyme in the biosynthetic pathway for the mugineic acid family of phytosiderophores, catalyzes the trimerization of S-adenosylmethionine to form one molecule of nicotianamine. We purified NAS protein and isolated the genes nas1, nas2, nas3, nas4, nas5-1, nas5-2, and nas6, which encode NAS and NAS-like proteins from Fe-deficient barley (Hordeum vulgare L. cv Ehimehadaka no. 1) roots. Escherichia coli expressing nas1 showed NAS activity, confirming that this gene encodes a functional NAS. Expression of nas genes as determined by northern-blot analysis was induced by Fe deficiency and was root specific. The NAS genes form a multigene family in the barley and rice genomes.
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| skos:exactMatch | |
| uniprot:name |
Plant Physiol.
|
| uniprot:author |
Higuchi K.,
Mori S.,
Nakanishi H.,
Nishizawa N.-K.,
Suzuki K.,
Yamaguchi H.
|
| uniprot:date |
1999
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| uniprot:pages |
471-480
|
| uniprot:title |
Cloning of nicotianamine synthase genes, novel genes involved in the biosynthesis of phytosiderophores.
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| uniprot:volume |
119
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| dc-term:identifier |
doi:10.1104/pp.119.2.471
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