TY - JOUR
T1 - The catalytic efficiency of soybean lipoxygenase-1 is enhanced at low gravity
AU - Maccarrone, Mauro
AU - Bari, Monica
AU - Battista, Natalia
AU - Finazzi-Agrò, Alessandro
PY - 2001/3/15
Y1 - 2001/3/15
N2 - Several cellular processes are modified when cells are placed under conditions of weightlessness. As yet, there is no coherent explanation for these observations, nor it is known which biomolecules might act as gravity sensors. Lipoxygenases generate leukotrienes and lipoxins from arachidonic acid, being responsible for many pharmacological and immunological effects, some of which are known to be affected by microgravity. In the course of the 28th parabolic flight campaign of the European Space Agency we measured the activity of pure soybean lipoxygenase-1 on linoleic acid, by a fibre optics spectrometer developed on purpose. It was found that microgravity reduced the apparent Michaelis-Menten constant (Km) of the enzymatic reaction to one fourth with respect to the 1 g control, whereas, the catalytic constant (kcat) was unaffected. Consequently, the catalytic efficiency of lipoxygenase-1 (kcat/Km) was approximately four-fold higher in flight than on ground. This unprecedented finding suggests that lipoxygenase-1 might be a molecular target for gravity.
AB - Several cellular processes are modified when cells are placed under conditions of weightlessness. As yet, there is no coherent explanation for these observations, nor it is known which biomolecules might act as gravity sensors. Lipoxygenases generate leukotrienes and lipoxins from arachidonic acid, being responsible for many pharmacological and immunological effects, some of which are known to be affected by microgravity. In the course of the 28th parabolic flight campaign of the European Space Agency we measured the activity of pure soybean lipoxygenase-1 on linoleic acid, by a fibre optics spectrometer developed on purpose. It was found that microgravity reduced the apparent Michaelis-Menten constant (Km) of the enzymatic reaction to one fourth with respect to the 1 g control, whereas, the catalytic constant (kcat) was unaffected. Consequently, the catalytic efficiency of lipoxygenase-1 (kcat/Km) was approximately four-fold higher in flight than on ground. This unprecedented finding suggests that lipoxygenase-1 might be a molecular target for gravity.
KW - Catalysis
KW - Enzymes
KW - Humans
KW - Lipoxygenase
KW - Microgravity
KW - Plants
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U2 - 10.1016/S0301-4622(01)00132-6
DO - 10.1016/S0301-4622(01)00132-6
M3 - Article
C2 - 11321679
AN - SCOPUS:0035869683
VL - 90
SP - 97
EP - 101
JO - Biophysical Chemistry
JF - Biophysical Chemistry
SN - 0301-4622
IS - 1
ER -