Minor, W., Steczko, J., Stec, B., Otwinowski, Z., Bolin, J.T., Walter, R. and Axelrod, B. (1996) Crystal Structure of Soybean Lipoxygenase L-1 at 1.4 Angstrom Resolution. Biochemistry, 35, 10687-10701. http://dx.doi.org/10.1021/bi960576u

has been cited by the following article:

• TITLE: Formation of (2E)-4-Hydroxy-2-nonenal and (2E)-4-Hydroxy-2-hexenal by Plant Enzymes: A Review Suggests a Role in the Physiology of Plants

  AUTHORS: Harold W. Gardner

  KEYWORDS: (3Z)-Nonenal, (3Z)-Hexenal, (2E)-4-Hydroxy-2-nonenal, (2E)-4-Hydroxy-2-hexenal, (2E)-4-Hydroperoxy-2-hexenal, Lipoxygenase, Hydroperoxide Peroxygenase, Hydroperoxide Lyase, (2E)-4-Hydroperoxy-2-Nonenal, 3, 4-Epoxynonanal, (2E)-4-Oxo-2-nonenal, Glycine max, Vica faba, Plant Pathogen

  JOURNAL NAME: Advances in Enzyme Research, Vol.4 No.2, June 8, 2016

  ABSTRACT: It is demonstrated that (3Z)-nonenal (NON) and (3Z)-hexenal (HEX) are oxidized in a cascade by lipoxygenase (LOX) and hydroperoxide peroxygenase (HP peroxygenase) into (2E)-4-hydroxy-2- nonenal (HNE) and (2E)-4-hydroxy-2-hexenal (HHE), respectively. In turn, HNE inactivates LOX terminating the cascade. The hydroxy-alkenals produced serve to inhibit plant pathogens, which initiated the cascade. In addition to LOX, other unknown oxygenases may be involved in the cascade.