Identification of a Naturally Occurring Peroxidase-Lipoxygenase Fusion Protein

Author:

Koljak Reet123,Boutaud Olivier123,Shieh Bih-Hwa123,Samel Nigulas123,Brash Alan R.123

Affiliation:

1. 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.

2. O. Boutaud, B.-H. Shieh, A. R. Brash, Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232–6602, USA.

3. N. Samel, Department of Bioorganic Chemistry, Institute of Chemistry, Tallinn, Estonia EE0026.

Abstract

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference34 articles.

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5. Brash A. R., J. Am. Chem. Soc. 111, 1891 (1989).

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