Tight association of N-terminal and catalytic subunits of rabbit 12/15-lipoxygenase is important for protein stability and catalytic activity

Article ID	Journal	Published Year	Pages	File Type
8303189	Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids	2011	10 Pages	PDF

Abstract

âº Tight interdomain association is important for structural performance of 12/15-LOX. âº Tyr98 is involved in aromatic interaction between two subunits of 12/15-LOX. âº A loss of an aromatic interaction destabilize tertiary structure of 12/15-LOX. âº This structural alteration is associated with a functional distortion of 12/15-LOX.

Keywords

HEPES IPTG DTT 12-HETE 15-HETE Molecular enzymology 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid Linoleic acid eicosanoids dithiothreitol structural biology Soybean lipoxygenase-1 lipoxygenase(s)Thermal stability Lipid peroxidation

Related Topics

Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry

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Tight association of N-terminal and catalytic subunits of rabbit 12/15-lipoxygenase is important for protein stability and catalytic activity

Authors

Igor Ivanov, Almerinda Di Venere, Thomas Horn, Patrick Scheerer, Eleonora Nicolai, Sabine Stehling, Constanze Richter, Ewa Skrzypczak-Jankun, Giampiero Mei, Mauro Maccarrone, Hartmut Kühn,