A Catalase-related Hemoprotein in Coral Is Specialized for Synthesis of Short-chain Aldehydes

Teder, Tarvi; Lõhelaid, Helike; Boeglin, William E.; Calcutt, Wade M.; Brash, Alan R.; Samel, Nigulas

doi:10.1074/jbc.m115.660282

Cited by 27 publications

(26 citation statements)

References 56 publications

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“…The enzymes of this type described to date are involved in pathways of oxylipin biosynthesis. Examples are the fatty acid allene oxide synthases of corals and cyanobacteria [1–3], the fatty acid hydroperoxide lyase discovered recently in coral [4], and a cyanobacterial enzyme that forms fatty acid diols and a fatty acid containing a bicyclobutane ring [5, 6]. These enzymes all exist as the N-terminal domain of a natural fusion protein that has the lipoxygenase that forms their fatty acid hydroperoxide substrate on the C-terminus.…”

Section: Introductionmentioning

confidence: 99%

A fungal catalase reacts selectively with the 13S fatty acid hydroperoxide products of the adjacent lipoxygenase gene and exhibits 13S-hydroperoxide-dependent peroxidase activity

Teder

Boeglin

Schneider

et al. 2017

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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The genome of the fungal plant pathogen Fusarium graminearum harbors six catalases, one of which has the sequence characteristics of a fatty acid peroxide-metabolizing catalase. We cloned and expressed this hemoprotein (designated as Fg-cat) along with its immediate neighbor, a 13S-lipoxygenase (cf. Brodhun et al, PloS One, e64919, 2013) that we considered might supply a fatty acid hydroperoxide substrate. Indeed, Fg-cat reacts abruptly with the 13S-hydroperoxide of linoleic acid (13S-HPODE) with an initial rate of 700–1300 s−1. By comparison there was no reaction with 9R- or 9S-HPODEs and extremely weak reaction with 13R-HPODE (~0.5% of the rate with 13S-HPODE). Although we considered Fg-cat as a candidate for the allene oxide synthase of the jasmonate pathway in fungi, the main product formed from 13S-HPODE was identified by UV, MS, and NMR as 9-oxo-10E-12,13-cis-epoxy-octadecenoic acid (with no traces of AOS activity). The corresponding analog is formed from the 13S-hydroperoxide of α-linolenic acid along with novel diepoxy-ketones and two C13 aldehyde derivatives, the reaction mechanisms of which are proposed. In a peroxidase assay monitoring the oxidation of ABTS, Fg-cat exhibited robust activity (kcat 550 s−1) using the 13S-hydroperoxy-C18 fatty acids as the oxidizing co-substrate. There was no detectable peroxidase activity using the corresponding 9S-hydroperoxides, nor with t-butyl hydroperoxide, and very weak activity with H2O2 or cumene hydroperoxide at micromolar concentrations of Fg-cat. Fg-cat and the associated lipoxygenase gene are present together in fungal genera Fusarium, Metarhizium and Fonsecaea and appear to constitute a partnership for oxidations in fungal metabolism or defense.

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Section: Introductionmentioning

confidence: 99%

A fungal catalase reacts selectively with the 13S fatty acid hydroperoxide products of the adjacent lipoxygenase gene and exhibits 13S-hydroperoxide-dependent peroxidase activity

Teder

Boeglin

Schneider

et al. 2017

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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“…The coral C. imbricata contains both a cAOS‐LOX and a closely related fusion protein with a catalase‐related hydroperoxide lyase (cHPL) domain that cleaves 8 R ‐HPETE to an aldehyde acid and alkyl aldehyde . This type of fatty acid aldehyde synthesis parallels the HPL activity of CYP74 cytochrome P450s in plants .…”

Section: Introductionmentioning

confidence: 99%

The Thr–His Connection on the Distal Heme of Catalase‐Related Hemoproteins: A Hallmark of Reaction with Fatty Acid Hydroperoxides

2016

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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 a role in oxidative defense, generally these enzymes are involved in secondary metabolite biosynthesis. The prototypical enzyme is the catalase-related allene oxide synthase (cAOS), 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 catalase 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 three-dimensional space is conserved as Val in true catalases and changed to Thr in the fatty acid hydroperoxide-metabolizing enzymes. As explained herein, the Thr-His connection on the distal face of the heme is critical in switching the substrate specificity from H2O2 to the transformation of fatty acid hydroperoxide.

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“…9) For cleavage on the allylic C-C bonding, the formation of epoxy allylic carbon radical from alkoxyl radical, followed by a rearrangement and subsequent hydroxylation to yield a hemiacetal ester is proposed by examining the reaction mechanisms of an angiosperm HPL, 32) and a catalaserelated hemoprotein in coral. 33) According to the proposed mechanism of cleavage on the allylic C-C bonding, the fate of alkoxyl radical must be controlled to avoid spontaneous reaction mostly leading to nonallylic C-C bonding, but instead be controlled to form epoxy allylic carbon radical. Presently, we do not know whether MpLOX7 employs the same mechanism to cleave the non-allylic C-C bonding, and further detailed study must be done.…”

Section: Discussionmentioning

confidence: 99%

n-Hexanal and (Z)-3-hexenal are generated from arachidonic acid and linolenic acid by a lipoxygenase in Marchantia polymorpha L.

Tawfik

Yamato

Kohchi

et al. 2017

Bioscience, Biotechnology, and Biochemistry

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Most terrestrial plants form green leaf volatiles (GLVs), which are mainly composed of six-carbon (C6) compounds. In our effort to study the distribution of the ability of lipoxygenase (LOX) to form GLVs, we found that a liverwort, Marchantia polymorpha, formed n-hexanal and (Z)-3-hexenal. Some LOXs execute a secondary reaction to form short chain volatiles. One of the LOXs from M. polymorpha (MpLOX7) oxygenized arachidonic and α-linolenic acids at almost equivalent efficiency and formed C6-aldehydes during its catalysis; these are likely formed from hydroperoxides of arachidonic and α-linolenic acids, with a cleavage of the bond between carbon at the base of the hydroperoxy group and carbon of double bond, which is energetically unfavorable. These lines of evidence suggest that one of the LOXs in liverwort employs an unprecedented reaction to form C6 aldehydes as by-products of its reaction with fatty acid substrates.

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A Catalase-related Hemoprotein in Coral Is Specialized for Synthesis of Short-chain Aldehydes

Cited by 27 publications

References 56 publications

A fungal catalase reacts selectively with the 13S fatty acid hydroperoxide products of the adjacent lipoxygenase gene and exhibits 13S-hydroperoxide-dependent peroxidase activity

A fungal catalase reacts selectively with the 13S fatty acid hydroperoxide products of the adjacent lipoxygenase gene and exhibits 13S-hydroperoxide-dependent peroxidase activity

The Thr–His Connection on the Distal Heme of Catalase‐Related Hemoproteins: A Hallmark of Reaction with Fatty Acid Hydroperoxides

n-Hexanal and (Z)-3-hexenal are generated from arachidonic acid and linolenic acid by a lipoxygenase in Marchantia polymorpha L.

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