14-3-3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-543 by endogenous protein phosphatases

FEBS Letters

Volumn 398, Issue 1, 1996, Pages 26-30

  Bachmann, Markus ^a   Huber, Joan L ^a   Athwal, Gurdeep S ^a   Wu, Ke ^b   Ferl, Robert J ^b   Huber, Steven C ^a  

^a NORTH CAROLINA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF FLORIDA   (United States)

Author keywords

14 3 3 protein; Binding site; Inhibitor protein; Isoform specificity; Nitrate reductase; Protein phosphatase; Regulatory phosphorylation site

Indexed keywords

NITRATE REDUCTASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN INHIBITOR; SYNTHETIC PEPTIDE;

ARTICLE; BINDING SITE; DEPHOSPHORYLATION; ENZYME BINDING; ENZYME INHIBITION; IN VITRO STUDY; PRIORITY JOURNAL; SPINACH;

14-3-3 PROTEINS; AMINO ACID SEQUENCE; ARABIDOPSIS; BINDING SITES; ENZYME ACTIVATION; ISOENZYMES; MOLECULAR SEQUENCE DATA; NITRATE REDUCTASE; NITRATE REDUCTASES; PEPTIDE FRAGMENTS; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; PLANT LEAVES; PLANT PROTEINS; PROTEINS; SERINE; SPINACIA OLERACEA; TYROSINE 3-MONOOXYGENASE;

SPINACIA OLERACEA;

EID: 0030602179     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(96)01188-X     Document Type: Article

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