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Journal archive > 2010 > N 2 March-April

THERMOINACTIVATION OF POTATO 5-LIPOXYGENASE AND EFFECT OF?PHOSPHATIDIC
ACID ON ACTIVATION ENERGY?OF?DENATURATION

T. D. Skaterna, G. I. Kharitonenko, O.?V.?Kharchenko

Institute of Bioorgenic Chemistry and
Petrolchemistry, National Academy of Sciences of Ukraine;
e-mail: This email address is being protected from spambots. You need JavaScript enabled to view it.

The investigation aim was to establish the structural-functional relations of individual lipid metabolism components: enzymes – lipoxygenases and membrane phospholipids. Influence of phosphatidic acid (PA)– allosteric activator of potato tuber 5-lipoxygenase (5-LO) – on thermoinactivation thermodynamic parameters of enzyme was studied.
It was established that PA changes essentially the 5-LO thermostability, namely activation energy Еа of enzyme denaturation increases several times in this phospholipid presence. Such changes can evidence that PA interaction with 5-LO leads to conformational changes of enzyme probably due to hydrophobic interactions. Obtained results give a possibility to interpret the action mechanism of PA as 5-LO allosteric activator, which can displace the substrate molecules in binding sites and increase the level of formation of specific products of linoleic acid oxygenation by 5-LO.

Key words: 5-lipoxygenase, linoleic acid, allosteric effector, phosphatidic acid, thermoinactivation.

The original article in Ukrainian is available for download in PDF format.

© The Ukrainian Biochemical Journal