Discovery of a linoleate 9S-dioxygenase and an allene oxide synthase in a fusion protein of Fusarium oxysporum

Hoffmann, Inga; Oliw, Ernst H.

doi:10.1194/jlr.m044347

Cited by 26 publications

(26 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A third subfamily comprises 10 R -DOX of aspergilli, and these proteins lack the functional heme thiolate ligand in the CYP domain ( 14,15 ). Recent additions are the 9 R -DOX-AOS subfamily of certain aspergilli and the 9 S -DOX-AOS subfamily of the genera Fusarium and Colletotrichum ( 16,17 ).…”

Section: Methodsmentioning

confidence: 99%

Epoxy alcohol synthase of the rice blast fungus represents a novel subfamily of dioxygenase-cytochrome P450 fusion enzymes

Hoffmann

Jernerén

Oliw

2014

Journal of Lipid Research

Self Cite

View full text Add to dashboard Cite

human cells by cyclooxygenases and cytochrome P450 (CYP) to prostaglandins, thromboxanes, prostacyclin, and related compounds and by lipoxygenases to hydroperoxides, leukotrienes, and epoxy alcohols ( 3,4 ). These eicosanoids exert a plethora of both physiological and pathophysiological functions (e.g., in control of reproduction, cancer development, skin water permeability, fever, and infl ammation). Homologous enzymes are found in plants and fungi with functions in reproduction, development, and infection, and they usually use linoleic and linolenic acids as substrates ( 5-7 ).Plant lipoxygenases and allene oxide synthases (AOSs) catalyze the fi rst steps during biosynthesis of jasmonic acid, which is a potent regulator of growth and defense with structural similarities to prostaglandins ( 7,8 ). Pathogens can induce expression of lipoxygenases and fatty acid ␣ -dioxygenase (DOX) in plants with formation of jasmonic acid and other oxylipins, which act as defense molecules. Oxylipins are also formed by fungi, which are human and plant pathogens. These fungi express lipoxygenases and DOX-CYP fusion proteins ( 5 ). The DOX domains are homologs to animal heme peroxidases, which include cyclooxygenases and ␣ -DOX, and their CYP domains take advantage of the peroxide shunt pathway in analogy with thromboxane and prostacyclin synthases ( 9 ). Oxylipins designate oxygenated metabolites of unsaturated fatty acids, and they are mainly formed by eukaryotic organisms ( 1, 2 ). Arachidonic acid is oxygenated in Abstract The genome of the rice blast fungus

show abstract

Section: Methodsmentioning

confidence: 99%

Epoxy alcohol synthase of the rice blast fungus represents a novel subfamily of dioxygenase-cytochrome P450 fusion enzymes

Hoffmann

Jernerén

Oliw

2014

Journal of Lipid Research

Self Cite

View full text Add to dashboard Cite

show abstract

“…This has sparked interest in the pattern of oxygenation of C 18 fatty acids by this fungus. The genome codes for several dioxygenases of linoleic and ␣ -linolenic acid: 9 S -dioxygenase-allene oxide synthase, 10 R -dioxygenase-epoxy alcohol synthase, a related 9 R -dioxygenase, and two LOXs designated FoxLOX and F. oxysporum manganese LOX (Fo-MnLOX) ( 18,19 ) ( Fig. 1 ).…”

Section: Methodsmentioning

confidence: 99%

Manganese lipoxygenase of F. oxysporum and the structural basis for biosynthesis of distinct 11-hydroperoxy stereoisomers

Wennman

Magnuson

Hámberg

et al. 2015

Journal of Lipid Research

Self Cite

View full text Add to dashboard Cite

This article is available online at http://www.jlr.org Lipoxygenases (LOXs) belong to a common gene family ( 1, 2 ). The catalytic domain is formed by ␣ -helices, which harbor fi ve metal ligands. The 3D structure is known for over 10 enzymes from plants, animals, and bacteria with 13 S -LOX of soybean LOX-1 (sLOX-1) and 8 R -LOX of Plexaura homomalla as old and new prototypes ( 3-5 ). The latter was recently crystallized with its substrate in the active site ( 5 ). Information on the active site and reaction mechanism has also been gained by site-directed mutagenesis and by analysis of various substrates, deuterated fatty acids, and LOX inhibitors ( 1, 6 ). With few exceptions, LOXs oxidize polyunsaturated fatty acids with one or more cis , cis-1,4-pentadiene units to hydroperoxides, which in many cases are precursors of biological mediators ( 1, 6, 7 ). Mammalian LOXs initiate biosynthesis of leukotrienes and epoxy alcohols, which are involved in allergic infl ammation, asthma, formation of the skin-water barrier, and cancer development ( 6,8 ). Plant LOXs form jasmonates and related oxylipins with functions in defense against pathogens and in wound healing ( 9,10 ).The N-terminal parts of mammalian and plant LOXs usually consist of ␤ -sheets with homology to polycystin-1/ LOX/ ␣ -toxin (PLAT) domains with regulatory functions. The N-terminal domains of fungal LOXs lack this homology, but they often contain a secretion signal ( 11, 12 ). Abbreviations: Af-MnLOX, Aspergillus fumigatus manganese lipoxygenase; Cg-MnLOX, Colletotrichum gloeosporioides manganese lipoxygenase; CP, chiral phase; EPR, electron paramagnetic resonance; FeLOX, iron lipoxygenase; Fo-MnLOX, Fusarium oxysporum manganese lipoxygenase; HPODE, hydroperoxyoctadecadienoic acid; 9 S -H(P)ODE, 9 S -hydro(pero) xy-10 E ,12 Z -octadecadienoic acid; 11 S -H(P)ODE, 11 S -hydro(pero)xy-9 Z ,12 Z -octadecadienoic acid; 13 R -H(P)ODE, 13 R -hydro(pero)xy-9 Z ,11 Eoctadecadienoic acid; HPOTrE, hydroperoxyoctadecatrienoic acid; 9 S -H(P)OTrE, 9 S -hydro(pero)xy-10 E ,12 Z ,15Z-octadecatrienoic acid; 11 R -H(P)OTrE, 11 R -hydro(pero)xy-9 Z ,12 Z ,15 Z -octadecatrienoic acid; 13 R -H(P)OTrE, 13 R -hydro(pero)xy-9 Z ,11 E ,15Z-octadecatrienoic acid; ICP-AES, inductively coupled plasma atomic emission spectroscopy; LOX, lipoxygenase; MnLOX, manganese lipoxygenase; Mo-MnLOX, Magnaporthe oryzae manganese lipoxygenase; RP, reversed phase; sLOX-1, soybean lipoxygenase-1; TPP, triphenylphosphine . Abstract The biosynthesis of jasmonates in plants is

show abstract

“…Hoffmann and co-worker reported, however, on the identification of a novel 9 R -dioxygenase-AOS fusion enzyme that oxidizes linoleic acid to its corresponding 9 S -hydroperoxy derivative and further isomerizes this intermediate yielding 9 S (10)-epoxy-10,12-octadecadienoic acid in F . oxysporum [26]. Interestingly, a similar enzymatic activity has also been found in L .…”

Section: Introductionmentioning

confidence: 57%

Optimized Jasmonic Acid Production by Lasiodiplodia theobromae Reveals Formation of Valuable Plant Secondary Metabolites

et al. 2016

View full text Add to dashboard Cite

Jasmonic acid is a plant hormone that can be produced by the fungus Lasiodiplodia theobromae via submerged fermentation. From a biotechnological perspective jasmonic acid is a valuable feedstock as its derivatives serve as important ingredients in different cosmetic products and in the future it may be used for pharmaceutical applications. The objective of this work was to improve the production of jasmonic acid by L. theobromae strain 2334. We observed that jasmonic acid formation is dependent on the culture volume. Moreover, cultures grown in medium containing potassium nitrate as nitrogen source produced higher amounts of jasmonic acid than analogous cultures supplemented with ammonium nitrate. When cultivated under optimal conditions for jasmonic acid production, L. theobromae secreted several secondary metabolites known from plants into the medium. Among those we found 3-oxo-2-(pent-2-enyl)-cyclopentane-1-butanoic acid (OPC-4) and hydroxy-jasmonic acid derivatives, respectively, suggesting that fungal jasmonate metabolism may involve similar reaction steps as that of plants. To characterize fungal growth and jasmonic acid-formation, we established a mathematical model describing both processes. This model may form the basis of industrial upscaling attempts. Importantly, it showed that jasmonic acid-formation is not associated to fungal growth. Therefore, this finding suggests that jasmonic acid, despite its enormous amount being produced upon fungal development, serves merely as secondary metabolite.

show abstract

Discovery of a linoleate 9S-dioxygenase and an allene oxide synthase in a fusion protein of Fusarium oxysporum

Cited by 26 publications

References 45 publications

Epoxy alcohol synthase of the rice blast fungus represents a novel subfamily of dioxygenase-cytochrome P450 fusion enzymes

Epoxy alcohol synthase of the rice blast fungus represents a novel subfamily of dioxygenase-cytochrome P450 fusion enzymes

Manganese lipoxygenase of F. oxysporum and the structural basis for biosynthesis of distinct 11-hydroperoxy stereoisomers

Optimized Jasmonic Acid Production by Lasiodiplodia theobromae Reveals Formation of Valuable Plant Secondary Metabolites

Contact Info

Product

Resources

About