Regulation of spinach-leaf nitrate reductase by reversible phosphorylation

Carol MacKintosh

doi:10.1016/0167-4889(92)90109-O

Regulation of spinach-leaf nitrate reductase by reversible phosphorylation

Carol MacKintosh

Research output: Contribution to journal › Comment/debate › peer-review

123 Citations (Scopus)

Abstract

Okadaic acid and microcystin (but not the inactive methyl esters of these toxins) prevented the rapid light-induced activation of nitrate reductase (NR) in intact spinach leaves. In vitro, nitrate reductase was inactivated by a protein kinase and activated by PP2A. The role of reversible protein phosphorylation in regulation of light-coupled cytoplasmic metabolism is discussed.

Original language	English
Pages (from-to)	121-126
Number of pages	6
Journal	Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Volume	1137
Issue number	1
DOIs	https://doi.org/10.1016/0167-4889(92)90109-O
Publication status	Published - 1992

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title = "Regulation of spinach-leaf nitrate reductase by reversible phosphorylation",

abstract = "Okadaic acid and microcystin (but not the inactive methyl esters of these toxins) prevented the rapid light-induced activation of nitrate reductase (NR) in intact spinach leaves. In vitro, nitrate reductase was inactivated by a protein kinase and activated by PP2A. The role of reversible protein phosphorylation in regulation of light-coupled cytoplasmic metabolism is discussed.",

author = "Carol MacKintosh",

year = "1992",

doi = "10.1016/0167-4889(92)90109-O",

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T1 - Regulation of spinach-leaf nitrate reductase by reversible phosphorylation

AU - MacKintosh, Carol

PY - 1992

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N2 - Okadaic acid and microcystin (but not the inactive methyl esters of these toxins) prevented the rapid light-induced activation of nitrate reductase (NR) in intact spinach leaves. In vitro, nitrate reductase was inactivated by a protein kinase and activated by PP2A. The role of reversible protein phosphorylation in regulation of light-coupled cytoplasmic metabolism is discussed.

AB - Okadaic acid and microcystin (but not the inactive methyl esters of these toxins) prevented the rapid light-induced activation of nitrate reductase (NR) in intact spinach leaves. In vitro, nitrate reductase was inactivated by a protein kinase and activated by PP2A. The role of reversible protein phosphorylation in regulation of light-coupled cytoplasmic metabolism is discussed.

U2 - 10.1016/0167-4889(92)90109-O

DO - 10.1016/0167-4889(92)90109-O

M3 - Comment/debate

SN - 0167-4889

VL - 1137

SP - 121

EP - 126

JO - Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

JF - Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

IS - 1

ER -

Regulation of spinach-leaf nitrate reductase by reversible phosphorylation

Abstract

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