Characterization of phosphoenolpyruvate carboxylase from mature
maize seeds: Properties of phosphorylated and dephosphorylated
forms

J 2010

Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms

ČERNÝ, Martin; Veronika DOUBNEROVÁ; Karel MÜLLER a Helena RYŠLAVÁ

Základní údaje

Originální název

Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms

Název česky

Charakterizace fosfoenolpyruvátkarboxylasy ze zralých semen kukuřice: vlastnosti fosforylované a defosforylované formy

Autoři

ČERNÝ, Martin; Veronika DOUBNEROVÁ; Karel MÜLLER a Helena RYŠLAVÁ

Vydání

Biochimie, Paris, Elsevier Masson SAS, 2010, 0300-9084

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.787

Označené pro přenos do RIV

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000283637800013

Klíčová slova česky

fosfoenolpyruvát karboxylasa; fosforylace; zrno; sigmoidní kinetika; Zea mays

Klíčová slova anglicky

Phosphoenolpyruvate carboxylase; Phosphorylation; Seed; Sigmoidal kinetics; Zea mays

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 19. 5. 2011 15:42, doc. Mgr. Martin Černý, Ph.D.

Anotace

V originále

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 [mu]mol 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.

Citovat

ČERNÝ, Martin; Veronika DOUBNEROVÁ; Karel MÜLLER a Helena RYŠLAVÁ. Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms. Biochimie. Paris: Elsevier Masson SAS, 2010, roč. 92, č. 10, s. 1362-1370. ISSN 0300-9084.

@article{900394,
   author = {Černý, Martin and Doubnerová, Veronika and Müller, Karel and Ryšlavá, Helena},
   article_location = {Paris},
   article_number = {10},
   keywords = {Phosphoenolpyruvate carboxylase; Phosphorylation; Seed; Sigmoidal kinetics; Zea mays},
   language = {eng},
   issn = {0300-9084},
   journal = {Biochimie},
   title = {Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms},
   url = {http://www.sciencedirect.com/science/article/B6VRJ-50DW3YT-3/2/3abb9d9951f6deed74e66c2dc8e8df6a},
   volume = {92},
   year = {2010}
}

TY  - JOUR
ID  - 900394
AU  - Černý, Martin - Doubnerová, Veronika - Müller, Karel - Ryšlavá, Helena
PY  - 2010
TI  - Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms
JF  - Biochimie
VL  - 92
IS  - 10
SP  - 1362-1370
EP  - 1362-1370
PB  - Elsevier Masson SAS
SN  - 03009084
KW  - Phosphoenolpyruvate carboxylase
KW  - Phosphorylation
KW  - Seed
KW  - Sigmoidal kinetics
KW  - Zea mays
UR  - http://www.sciencedirect.com/science/article/B6VRJ-50DW3YT-3/2/3abb9d9951f6deed74e66c2dc8e8df6a
N2  - 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 [mu]mol 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.
ER  -

ČERNÝ, Martin; Veronika DOUBNEROVÁ; Karel MÜLLER a Helena RYŠLAVÁ. Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: Properties of phosphorylated and dephosphorylated forms. \textit{Biochimie}. Paris: Elsevier Masson SAS, 2010, roč.~92, č.~10, s.~1362-1370. ISSN~0300-9084.

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