期刊
FEBS LETTERS
卷 582, 期 23-24, 页码 3547-3551出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.09.031
关键词
Cyclooxygenase; 8R-Dioxygenase; 8-Hydroperoxy-linoleic acid; Hydroperoxide isomerase; LC-MS; Myeloperoxidase; Gaeumannomyces graminis
资金
- VR medicine [03X-06523]
- Formas [222-2005-1733]
- Knut and Alice Wallenberg Foundation [2004.0123]
7,8-Linoleate diol synthase (7,8-LDS) of the take-all fungus and cyclooxygenases can be aligned with similar to 24% amino acid identity and both form a tyrosyl radical during catalysis. 7,8-LDS was expressed in insect cells with native 8R-dioxygenase and hydroperoxide isomerase activities. We studied conserved residues of 7,8-LDS, which participate in cyclooxygenases for heme binding (His residues), hydrogen abstraction (Tyr), positioning (Tyr, Trp), and ionic binding of substrates (Arg). Site-directed mutagenesis abolished 8R-dioxygenase activities with exception of the putative distal histidine (His203Gln) and a tyrosine residue important for hydrogen bonding and substrate positioning (Tyr329Phe). The results demonstrate structural similarities between 7,8-LDS and cyclooxygenases. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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