Phosphoenolpyruvate Carboxylase from Spinach Leaf Tissue
نویسندگان
چکیده
منابع مشابه
Biosynthesis of ribulose-1,5-bisphosphate carboxylase in spinach leaf protoplasts.
Spinach leaf (Spinacia oleracea L. var. Kyoho) protoplasts sustain protein-synthesizing activity as measured by the incorporation of [(14)C]-leucine into the protein fraction both in the light and in the dark. By the immunoprecipitation of ribulose-1,5-bisphosphate (RuP(2)) carboxylase with rabbit antibody raised against the purified spinach enzyme preparation, it was found that approximately 7...
متن کاملMalate Inhibition of Phosphoenolpyruvate Carboxylase from
Phosphoenolpyruvate carboxylase partially purified from leaves of Crassula and rendered insensitive to malate by storage without adjuvants can be altered to the form sensitive to malate inhibition by brief, 5-minute preincubation with 5 millimolar malate. The induction of malate sensitivity is reversible by lowering the malate2concentration. Of the reaction components only HC03increases the sen...
متن کاملIn Vivo Regulatory Phosphorylation Site in C 4 - Leaf Phosphoenolpyruvate Carboxylase from Maize and Sorghum 1
Reversible seryl-phosphorylation contributes to the light/dark regulation of C4-leaf phosphoenolpyruvate carboxylase (PEPC) activity in vivo. The specific regulatory residue that, upon in vitro phosphorylation by a maize-leaf protein-serine kinase(s), leads to an increase in catalytic activity and a decrease in malatesensitivity of the target enzyme has been recently identified as Ser-15 in 32P...
متن کاملIn Vivo Regulatory Phosphorylation Site in C 4 - Leaf Phosphoenolpyruvate Carboxylase from Maize and Sorghum 1
Reversible seryl-phosphorylation contributes to the light/dark regulation of C4-leaf phosphoenolpyruvate carboxylase (PEPC) activity in vivo. The specific regulatory residue that, upon in vitro phosphorylation by a maize-leaf protein-serine kinase(s), leads to an increase in catalytic activity and a decrease in malatesensitivity of the target enzyme has been recently identified as Ser-15 in 32P...
متن کاملIn vivo regulatory phosphorylation site in c(4)-leaf phosphoenolpyruvate carboxylase from maize and sorghum.
Reversible seryl-phosphorylation contributes to the light/dark regulation of C(4)-leaf phosphoenolpyruvate carboxylase (PEPC) activity in vivo. The specific regulatory residue that, upon in vitro phosphorylation by a maize-leaf protein-serine kinase(s), leads to an increase in catalytic activity and a decrease in malate-sensitivity of the target enzyme has been recently identified as Ser-15 in ...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1974
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.53.6.829