Hydroperoxide lyases (CYP74C and CYP74B) catalyze the homolytic isomerization of fatty acid hydroperoxides into hemiacetals

Grechkin, Alexander N.; Brühlmann, Fredi; Mukhtarova, Lucia S.; Gogolev, Yu. V.; Hámberg, Mats

doi:10.1016/j.bbalip.2006.09.002

Cited by 64 publications

(48 citation statements)

References 23 publications

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“…HPL activity was first measured in watermelon seedlings [11], tea leaves [12], alfalfa seedlings [13], soya leaf [14], spinach leaves [15] and olive fruits [16]. However the enzymatic mechanism was completely elucidated only a few years ago [17,18]. HPL enzymes act as isomerases performing homolytic rearrangements of HPOs into transient hemiacetals which upon decomposition produce aldehydes and acids.…”

Section: Introductionmentioning

confidence: 99%

Optimization and scaling up of a biotechnological synthesis of natural green leaf volatiles using Beta vulgaris hydroperoxide lyase

Gigot

Ongena

Fauconnier

et al. 2012

Process Biochemistry

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a b s t r a c tFollowing a promising preliminary study concerning sugar beet leaves valorization and to fulfill the high demand in natural C 6 -aldehydes flavors, an efficient biocatalytic reaction was developed to synthesize (2E)-hexenal at large scale. As major product of the lipoxygenase enzyme, 13-HPOT was converted by sugar beet hydroperoxide lyase extracted from leaves or expressed by recombinant Escherichia coli strains. With the adaptation of a fed-batch substrate addition and a continuous extraction of volatiles, 3.46 mM and 1.37 mM of C 6 -aldehydes were produced with the native hydroperoxide lyase at respectively 2 and 100 L scale. Furthermore, higher molar productivity of green leaf volatiles was reached with recombinant hydroperoxide lyase (5.5 mM at 2 L scale) while no others side products from the lipoxygenase pathway were formed. Once purified, these natural aromas are suitable for food and beverage preparations, perfumes or cosmetic products.

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Section: Introductionmentioning

confidence: 99%

Optimization and scaling up of a biotechnological synthesis of natural green leaf volatiles using Beta vulgaris hydroperoxide lyase

Gigot

Ongena

Fauconnier

et al. 2012

Process Biochemistry

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“…While subsequent reactions can be construed as following a radical pathway to product (e.g. in the hydroperoxide lyase reaction (19)), others are considered to involve an electron transfer step, giving a carbocation intermediate in the penultimate steps to product (22) (Fig. 1).…”

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confidence: 99%

Evidence for an Ionic Intermediate in the Transformation of Fatty Acid Hydroperoxide by a Catalase-related Allene Oxide Synthase from the Cyanobacterium Acaryochloris marina

Gao

Boeglin

Zheng

et al. 2009

Journal of Biological Chemistry

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Allene oxides are reactive epoxides biosynthesized from fatty acid hydroperoxides by specialized cytochrome P450s or by catalase-related hemoproteins. Here we cloned, expressed, and characterized a gene encoding a lipoxygenase-catalase/peroxidase fusion protein from Acaryochloris marina. We identified novel allene oxide synthase (AOS) activity and a by-product that provides evidence of the reaction mechanism. The fatty acids 18.43 and 18.33 are oxygenated to the 12R-hydroperoxide by the lipoxygenase domain and converted to the corresponding 12R,13-epoxy allene oxide by the catalase-related domain. Linoleic acid is oxygenated to its 9R-hydroperoxide and then, surprisingly, converted ϳ70% to an epoxyalcohol identified spectroscopically and by chemical synthesis as 9R,10S-epoxy-13S-hydroxyoctadeca-11E-enoic acid and only ϳ30% to the 9R,10-epoxy allene oxide. Experiments using oxygen-18-labeled 9R-hydroperoxide substrate and enzyme incubations conducted in H A diverse spectrum of signaling molecules is biosynthesized in nature from polyunsaturated fatty acids, their peroxides, and further transformations of the fatty acid peroxides. The peroxides are formed by two classes of dioxygenase enzyme. The hemoprotein dioxygenases include prostaglandin H synthase (cyclooxygenase) in animals (1), ␣-dioxygenase in plants (2), and several linoleate dioxygenases in fungi (3-5). The nonheme iron lipoxygenases are even more widespread, being almost ubiquitous among organisms that contain polyunsaturated fatty acids (6 -8). Although further biosynthetic transformation is sometimes accomplished by an additional catalytic activity of the initiating dioxygenase (e.g. leukotriene A 4 synthase (9) or aldehyde-synthesizing hydroperoxide cleaving activity (10) among the LOX 2 enzymes), commonly another distinct enzyme is used to rearrange or otherwise modify the reactive fatty acid peroxide intermediate. Two hemoprotein types are found that have become specialized for this biosynthetic role: cytochrome P450s and catalase-related enzymes.The fatty acid peroxide-metabolizing P450s are by far the better known and include CYP5 (thromboxane synthase) and CYP8A (prostacyclin synthase) in animals (11), and the entire family of CYP74 in plants (12). The individual CYP74 enzymes include allene oxide synthase (AOS), one of which catalyzes a key step in cyclopentenone synthesis in the jasmonate pathway, hydroperoxide lyase, divinyl ether synthase, and epoxyalcohol synthase (12, 13). The catalase-related enzymes are distinctive in that they have been found naturally as a fusion protein with the LOX enzyme that forms their hydroperoxide substrate (14). The known activities include AOS in Plexaura homomalla and other marine corals (with a different specificity for fatty acid hydroperoxide compared with the plant P450 AOS) (15,16), and the unique bicyclobutane synthase and other allylic epoxide synthase activities of the enzyme in the cyanobacterium Anabaena 18). Currently we are trying to understand the scope of the reactions catalyzed by this catala...

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“…The oxygen rebound from Compound II gives rise to a hemiacetal intermediate. Our isotopic analysis and results by Grechkin and co-workers (21,33) clearly demonstrate that water is not involved in this process and that both of the original hydroperoxide oxygens are retained in the products. Notably, the chain cleavage in the P450 and cHPL type of fatty acid hydroperoxide lyase occurs within the original pentadiene of the fatty acid hydroperoxide, between C8 and C9 in the case of coral cHPL.…”

Section: Discussionmentioning

confidence: 74%

“…These include allene oxide synthase and divinyl ether synthase transformations (2,3,32). In the third possibility, the HPL route, the rearrangement leads to a covalently complete yet unstable final product, a full-length fatty acid hemiacetal, which through spontaneous decomposition gives the two short-chain aldehydic products (21,33). The equivalent pathway for the coral cHPL is illustrated in Scheme 2.…”

Section: Discussionmentioning

confidence: 99%

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

Teder

Lõhelaid

Boeglin

et al. 2015

Journal of Biological Chemistry

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Background: Biosynthetic transformation of fatty acid peroxides commonly is catalyzed by cytochromes P450. Results: A catalase-related hemoprotein in the coral Capnella imbricata converts 8R-hydroperoxy-eicosatetraenoic acid in a P450-type reaction to short-chain aldehydes. Conclusion: A catalase-related hydroperoxide lyase is identified in Animalia. Significance: The catalase-related hemoprotein has the catalytic competence of a P450.

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Hydroperoxide lyases (CYP74C and CYP74B) catalyze the homolytic isomerization of fatty acid hydroperoxides into hemiacetals

Cited by 64 publications

References 23 publications

Optimization and scaling up of a biotechnological synthesis of natural green leaf volatiles using Beta vulgaris hydroperoxide lyase

Optimization and scaling up of a biotechnological synthesis of natural green leaf volatiles using Beta vulgaris hydroperoxide lyase

Evidence for an Ionic Intermediate in the Transformation of Fatty Acid Hydroperoxide by a Catalase-related Allene Oxide Synthase from the Cyanobacterium Acaryochloris marina

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

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