Disease relevance of LOX1

• Expression of the LOX1 gene was examined following infiltration of leaves with virulent (Psm ES4326) and avirulent (Pst MM1065) strains of Pseudomonas syringae [1].

Psychiatry related information on LOX1

• Role of the lipoxygenase/lyase pathway of host-food plants in the host searching behavior of two parasitoid species, Cotesia glomerata and Cotesia plutellae [2].

High impact information on LOX1

• Multiple lipoxygenase sequence alignments and structural modeling of the enzyme/substrate interaction of the cucumber lipid body lipoxygenase suggested histidine 608 as the primary determinant of positional specificity [3].
• The potential involvement of a specific Arabidopsis thaliana lipoxygenase isozyme, LOX2, in the biosynthesis of the plant growth regulators jasmonic acid (JA) and abscisic acid was investigated [4].
• A chloroplast lipoxygenase is required for wound-induced jasmonic acid accumulation in Arabidopsis [4].
• Purified monogalactosyl diglyceride was not converted to the sn1-(12-oxophytodienoyl) derivative by the combined action of (soybean) lipoxygenase and (A. thaliana) allene oxide synthase, an enzyme ensemble that converts free alpha-linolenic acid to free 12-oxophytodienoic acid [5].
• Under cadmium stress, the 9 LOX pathway added to the 13 LOX one [6].

Biological context of LOX1

• The coding region of the LOX1 gene consists of 8 exons separated by 7 introns [7].
• AtLox2 encodes a 102-kD protein, AtLOX2, which has 42 to 45% amino acid sequence identity with other plant LOX sequences [8].
• Various physiological imbalances lead to reactive oxygen species (ROS) overproduction and/or increases in lipoxygenase (LOX) activities, both events ending in lipid peroxidation of polyunsaturated fatty acids (PUFAs) [6].
• Arabidopsis lipoxygenase 1 (cytoplasmic) expression is greatly increased but lipoxygenase 2 (plastidial) expression is sharply reduced during leaf senescence [9].
• A genomic clone containing a complete lipoxygenase gene was isolated from an almond DNA library [10].

Associations of LOX1 with chemical compounds

• In mature plants, LOX1 mRNA levels increased upon treatment with the stress-related hormones abscisic acid and methyl jasmonate and remained high for at least 96 h [1].
• Trans-2-hexenal induction thus closely mimics the group of genes induced by methyl jasmonate (MeJA), also a LOX-derived volatile [11].
• The differences in C6-aldehyde formation among the fatty acid mutants of Arabidopsis appeared not to result from alteration of lipoxygenase/hydroperoxide lyase pathway enzymes [12].
• Our results also suggest that AOS expression is limiting JA levels in wounded plants, but that the AOS hydroperoxide substrate levels, controlled by upstream enzymes (lipoxygenase and phospholipase), determine JA levels in unwounded plants [13].
• The inductive effect seemed to be limited to C6-related volatiles, as C8-, C9- and other related volatiles did not induce LOX mRNA levels [11].

Physical interactions of LOX1

• A search for plant eIF4E-binding proteins from Arcabictopsis thaliana using the yeast genetic interaction system identified a clone encoding a lipoxygenase type 2 (AtLOX2) [14].

Other interactions of LOX1

• With the exception of intron 1, the LOX1 introns are smaller in size than the LOX3 introns [7].
• C6-aldehydes are synthesized via lipoxygenase/hydroperoxide lyase action on polyunsaturated fatty acid (PUFA) substrates in plant leaves [12].
• RT-PCR analysis showed that the induction of transcripts for vegetative storage protein and lipoxygenase genes, previously shown to be inducible by wound and jasmonate application in the wild-type, was absent in the aos mutant [13].

Analytical, diagnostic and therapeutic context of LOX1

• The presence of an active lipoxygenase was confirmed by western blot analysis and by measuring the enzymatic activity in microsomal and soluble protein samples purified from almond seeds at this stage of development [10].
• Molecular cloning and biochemical characterization of a lipoxygenase in almond (Prunus dulcis) seed [10].

References