Modulation of nitrate reductase: some new insights, an unusual case and a potentially important side reaction
Author:
Publisher
Oxford University Press (OUP)
Subject
Plant Science,Physiology
Link
http://academic.oup.com/jxb/article-pdf/53/370/875/18072547/530875.pdf
Reference37 articles.
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2. Athwal GS, Huber JL, Huber SC. 1998. Biological significance of divalent metal ion binding to 14‐3‐3‐proteins in relationship to nitrate reductase inactivation. Plant Cell Physiology39,1065–1072.
3. Bachmann M, McMichael RW, Huber JL, Kaiser WM, Huber SC. 1995. Partial purification and characterisation of a calcium‐dependent protein kinase and an inhibitor protein required for the activation of spinach leaf nitrate reductase. Plant Physiology108,1083–1091.
4. Bachmann M, Shiraishi N, Campbell WH, Yoo B‐C, Harmon AC, Huber SC. 1996 a. Identification of Ser‐543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. The Plant Cell8,505–517.
5. Bachmann M, Huber JL, Athwal GS, Wu K, Ferl JR, Huber SC. 1996 b. 14‐3‐3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in a isoform specific manner and reduce dephosphorylation of Ser‐543 by endogenous protein phosphatases. FEBS Letters398,26–30.
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