A functional role identified for conserved charged residues at the active site entrance of lipoxygenase with double specificity
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- 作者：Jean-Christophe Albertia ; b ; Magali Mariania ; Virginie Brunini-Bronzini de Caraffaa ; Claude Gambottia ; Ernst H. Oliwc ; Liliane Bertia ; Jacques Maurya ; maury@univ-corse.fr" class="auth_mail" title="E-mail the corresponding author
- 关键词：HPOD ; hydroperoxyoctadecadienoic acid ; HPOT ; hydroperoxyoctadecatrienoic acid ; IPTG ; isopropyl-β-d-thiogalactopyranoside ; LOX ; lipoxygenase
- 刊名：Journal of Molecular Catalysis B: Enzymatic
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：123
- 期：Complete
- 页码：167-173
- 全文大小：1890 K
文摘
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Olive LOX1 active site entrance is surrounded by conserved positively charged residues.
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Substitution of R265, R268 and K283 by glutamine has an effect on kinetic parameters.
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These residues may interact with the substrate carboxylate.
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K283 could play a more important role attributable to its position on α2 helix.
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The role of these residues may be extended to all plant LOXs with double specificity.