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The Thr–His Connection on the Distal Heme of Catalase‐Related Hemoproteins: A Hallmark of Reaction with Fatty Acid Hydroperoxides
Author(s) -
Mashhadi Zahra,
Newcomer Marcia E.,
Brash Alan R.
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600345
Subject(s) - heme , hemeprotein , catalase , chemistry , biochemistry , fatty acid , connection (principal bundle) , stereochemistry , enzyme , structural engineering , engineering
This review focuses on a group of heme peroxidases that retain the catalase fold in structure, yet show little or no reaction with hydrogen peroxide. Instead of having a role in oxidative defense, these enzymes are involved in secondary metabolite biosynthesis. The prototypical enzyme is catalase‐related allene oxide synthase, an enzyme that converts a specific fatty acid hydroperoxide to the corresponding allene oxide (epoxide). Other catalase‐related enzymes form allylic epoxides, aldehydes, or a bicyclobutane fatty acid. In all catalases (including these relatives), a His residue on the distal face of the heme is absolutely required for activity. Its immediate neighbor in sequence as well as in 3 D space is conserved as Val in true catalases and Thr in the fatty acid hydroperoxide‐metabolizing enzymes. Thr–His on the distal face of the heme is critical in switching the substrate specificity from H 2 O 2 to fatty acid hydroperoxide.