Počet záznamů: 1
Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms
- 1.
SYSNO ASEP 0350036 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms Tvůrce(i) Černý, M. (CZ)
Doubnerová, V. (CZ)
Müller, Karel (UEB-Q) RID, ORCID
Ryšlavá, H. (CZ)Zdroj.dok. Biochimie. - : Elsevier - ISSN 0300-9084
Roč. 92, č. 10 (2010), s. 1362-1370Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. FR - Francie Klíč. slova Phosphoenolpyruvate carboxylase ; Phosphorylation ; Seed Vědní obor RIV EI - Biotechnologie a bionika CEP 1M0505 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy CEZ AV0Z50380511 - UEB-Q (2005-2011) UT WOS 000283637800013 DOI 10.1016/j.biochi.2010.06.019 Anotace 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. Pracoviště Ústav experimentální botaniky Kontakt David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Rok sběru 2011
Počet záznamů: 1