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Uchida, K. and Stadtman, E.R. (1992) Modification of Histidine Residues in Proteins by Reaction with 4-Hydroxyno- nenal. Proceedings of the National Academy of Sciences of the United States of America, 89, 4544-4548. http://dx.doi.org/10.1073/pnas.89.10.4544

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.