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Science 26 September 1997:
Vol. 277. no. 5334, pp. 1994 - 1996
DOI: 10.1126/science.277.5334.1994

Reports

Identification of a Naturally Occurring Peroxidase-Lipoxygenase Fusion Protein

Reet Koljak, Olivier Boutaud, Bih-Hwa Shieh, Nigulas Samel, Alan R. Brash *

A distant relative of catalase that is specialized for metabolism of a fatty acid hydroperoxide was identified. This heme peroxidase occurs in coral as part of a fusion protein, the other component of which is a lipoxygenase that forms the hydroperoxide substrate. The end product is an unstable epoxide (an allene oxide) that is a potential precursor of prostaglandin-like molecules. These results extend the known chemistry of catalase-like proteins and reveal a distinct type of enzymatic construct involved in the metabolism of polyunsaturated fatty acids.

R. Koljak, Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6602, USA, and Department of Bioorganic Chemistry, Institute of Chemistry, Tallinn, Estonia EE0026.
O. Boutaud, B.-H. Shieh, A. R. Brash, Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6602, USA.
N. Samel, Department of Bioorganic Chemistry, Institute of Chemistry, Tallinn, Estonia EE0026.
*   To whom correspondence should be addressed. E-mail: alan.brash{at}mcmail.vanderbilt.edu


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J. Biol. Chem. 276, 7033-7040
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The origin of 15R-prostaglandins in the Caribbean coral Plexaura homomalla: Molecular cloning and expression of a novel cyclooxygenase.
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