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Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms
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SYSNO ASEP 0350036 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms Author(s) Černý, M. (CZ)
Doubnerová, V. (CZ)
Müller, Karel (UEB-Q) RID, ORCID
Ryšlavá, H. (CZ)Source Title Biochimie. - : Elsevier - ISSN 0300-9084
Roč. 92, č. 10 (2010), s. 1362-1370Number of pages 9 s. Language eng - English Country FR - France Keywords Phosphoenolpyruvate carboxylase ; Phosphorylation ; Seed Subject RIV EI - Biotechnology ; Bionics R&D Projects 1M0505 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50380511 - UEB-Q (2005-2011) UT WOS 000283637800013 DOI 10.1016/j.biochi.2010.06.019 Annotation Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) from mature maize seeds (Zea mays L.) was purified to homogeneity and a final specific activity of 13.3 mmol min-1 mg-1. Purified PEPC was treated with phosphatase from bovine intestinal mucosa or protein kinase A to study its apparent phosphorylation level. Kinetic parameters of the enzyme reaction catalyzed by phosphorylated and dephosphorylated forms under different conditions were compared, as well as an effect of modulators. The enzyme dephosphorylation resulted in the change of hyperbolic kinetics to the sigmoidal one (with respect to PEP), following with the decrease of maximal reaction rate and the increase of sensitivity to L-malate inhibition. The hyperbolic kinetics of native PEPC present in dry maize seeds was not changed after the protein kinase A treatment, while it was converted to the sigmoidal one after dephosphorylation. Level of PEPC phosphorylation was not affected during seed imbibition. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2011
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