Čeština
EnglishThe enzyme kinetics of the NADP-malic enzyme from tobacco leaves
Ryšlavá, H.; Doubnerová, V.; Müller, Karel; Baťková, Petra; Schnablová, Renáta; Liberda, J.; Synková, Helena; Čeřovská, Noemi
COLLECTION OF CZECHOSLOVAK CHEMICAL COMMUNICATIONS 72 [10]: 1420-1434, 2007
Klíčová slova: oxidoreductases; enzyme kinetics; NADP-malic enzyme; divalent metal ions; Nicotiana tabacum L.
Abstrakt: The enzyme characteristics of NADP-malic enzyme isolated from tobacco was studied. The enzyme pH optimum was found at pH 7.1-7.4. The value of apparent Michaelis constant to substrates was evaluated in the presence of divalent metal ions. The dependence of the reaction rate on concentration of Mg2+ indicates the presence of more than one binding site. The sigmoidal dependence of the reaction rate on Mn2+ concentration and the value of Hill coefficient 7.5 indicate the positive cooperativity of the reaction kinetics in the presence of the ions.
DOI:
Autoři z ÚEB: Noemi Čeřovská, Karel Müller, Helena Synková
COLLECTION OF CZECHOSLOVAK CHEMICAL COMMUNICATIONS 72 [10]: 1420-1434, 2007
Klíčová slova: oxidoreductases; enzyme kinetics; NADP-malic enzyme; divalent metal ions; Nicotiana tabacum L.
Abstrakt: The enzyme characteristics of NADP-malic enzyme isolated from tobacco was studied. The enzyme pH optimum was found at pH 7.1-7.4. The value of apparent Michaelis constant to substrates was evaluated in the presence of divalent metal ions. The dependence of the reaction rate on concentration of Mg2+ indicates the presence of more than one binding site. The sigmoidal dependence of the reaction rate on Mn2+ concentration and the value of Hill coefficient 7.5 indicate the positive cooperativity of the reaction kinetics in the presence of the ions.
DOI:
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