Can soybean lipoxygenases be real models for mammalian lipoxygenases? A bioinformatics approach

Abstract

Soybean lipoxygenase-1 is one of well-studied enzymes because it is considered as a model enzyme for mammalian lipoxygenases. In general, the soybean lipoxygenase-1 is used in the test of inhibitory activities of various compounds. The present study provides a bioinformatics approach for comparison of various lipoxygenases in the databases. Their various physical and chemical parameters such as molecular weight, theoretical pI, amino acid composition, aliphatic index, and grand average of hydropathicity and the multiple sequence alignments of the lipoxygenases were computed by using several bioinformatics tools. In order to see phylogenetic relationships among lipoxygenases, a phylogenetic tree was constructed. The first three most abundant amino acids in soybean lipoxygenase-1 and 15-lipoxygenase (human) are L (10.3 %), S (7.4 %), A (6.7 %) and L (13.3 %), G (7.4 %), V (7.1 %), respectively. According to the phylogenetic tree, the soybean lipoxygenases are within separate clade compared to the mammalian lipoxygenases. In conclusion, soybean lipoxygenase-1 may not fully characterize the human lipoxygenase-15 since there are remarkable sequence-based differences, which are obtained by using bioinformatics tools between soybean lipoxygenase-1 and lipoxygenases from other sources especially from human. In this context, the researchers, who are aware of the problems described above and who have similar concerns, have begun to use recombinant DNA technology to produce recombinant human lipoxygenase-15 enzyme.

Bioactive Peptides and Protein Hydrolysates as Lipoxygenase Inhibitors

“…Positive control or reference compounds such as nordihydroguaiaretic acid [19], diclofenac sodium [17], and ascorbic acid [39] were used in several studies. Nevertheless, bioinformatic analysis by Cengiz Şahin and Cavas [53] suggested that soybean LOXs are not a suitable model for human LOXs due to significant sequence-based differences. In concurrence with this, Muñoz-Ramírez and coworkers [54] found that although catechols extracted from Lithraea caustica inhibited both soybean 15-LOX and human 5-LOX, the catechols were more selective against the human LOX.…”

Bioactive Peptides and Protein Hydrolysates as Lipoxygenase Inhibitors

“…Positive control or reference compounds such as nordihydroguaiaretic acid [19], diclofenac sodium [17], and ascorbic acid [39] were used in several studies. Nevertheless, bioinformatic analysis by Cengiz Şahin and Cavas [53] suggested that soybean LOXs are not a suitable model for human LOXs due to significant sequence-based differences. In concurrence with this, Muñoz-Ramírez, et al [54] found that although catechols extracted from Lithraea caustica inhibited both soybean 15-LOX and human 5-LOX, the catechols were more selective against the human LOX.…”