Abstract
Lipoxygenases (LOXs) are well-studied enzymes in plants
and mammals. However, fungal LOXs are less studied. In
this study, we have compared fungal LOX protein sequences
to all known characterized LOXs. For this, a script was
written using Shell commands to extract sequences from
the NCBI database and to align the sequences obtained
using Multiple Sequence Comparison by Log-Expectation. We
constructed a phylogenetic tree with the use of Quicktree
to visualize the relation of fungal LOXs towards other
LOXs. These sequences were analyzed with respect to the
signal sequence, C-terminal amino acid, the
stereochemistry of the formed oxylipin, and the metal ion
cofactor usage. This study shows fungal LOXs are divided
into two groups, the Ile- and the Val-groups. The
Ile-group has a conserved WRYAK sequence that appears to
be characteristic for fungal LOXs and has as a C-terminal
amino acid Ile. The Val-group has a highly conserved
WL-L/F-AK sequence that is also found in LOXs of plant
and animal origin. We found that fungal LOXs with this
conserved sequence have a Val at the C-terminus in
contrast to other LOXs of fungal origin. Also, these LOXs
have signal sequences implying these LOXs will be
expressed extracellularly. Our results show that in this
group, in addition to the Gaeumannomyces graminis and the
Magnaporthe salvinii LOXs, the Aspergillus fumigatus LOX
uses manganese as a cofactor.
Original language | English |
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Pages (from-to) | 1261-1270 |
Journal | Applied Microbiology and Biotechnology |
Volume | 98 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2014 |
MoE publication type | A1 Journal article-refereed |
Keywords
- aspergillus fumigatus
- cofactor
- gaeumannomyces graminis
- lipoxygenase
- manganese
- phylogenetic tree