Predicted secondary structure of hydroperoxide lyase from green bell pepper cloned in the yeast Yarrowia lipolytica

Santiago-Gómez, Mirna P.; Kermasha, Sélim; Nicaud, Jean‐Marc; Belin, Jean‐Marc; Husson, Florence

doi:10.1016/j.molcatb.2010.01.009

Cited by 9 publications

(6 citation statements)

References 19 publications

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“…For example, the green bell pepper HPL is composed of 480 amino acids and has a molecular weight of approximately 55 kDa. Circular dichroism analysis demonstrated that the protein secondary structure of dodecyl maltoside is composed of approximately 13% α‐helix, 32% β‐sheet, 21% turn and 31% unordered coils (Panagakou et al ., ; Santiago‐Gómez et al ., ). Similarly, the Solanum tuberosum HPL is a protein of approximately 54 kDa (Mu et al ., ).…”

Section: Biosynthesis Of Glvsmentioning

confidence: 97%

“…Three types of enzymes, that is AOS, HPL and divinylether synthase (DES), are included in the CYP74 subfamily, and the AOS and HPL genes have been found in all sequenced plant genomes (Brash, ; Hughes et al ., ). The genes encoding HPL are found mainly in algae, mushrooms, Penicillium and higher plants and have been characterized and cloned in many plant species, such as cucumber, green bell pepper, tomato and alfalfa (Atwal et al ., ; Noordermeer et al ., ; Santiago‐Gómez et al ., ; Wan et al ., ). Most HPLs are membrane bound; HPLs in plants such as Arabidopsis contain a chloroplast transit peptide, whereas HPLs in other plants, such as tomato and melon, do not have a clear transit peptide and are suggested to be microsome localized (Bate et al ., ; Froehlich et al ., ; Noordermeer et al ., ).…”

Section: Biosynthesis Of Glvsmentioning

confidence: 99%

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Green leaf volatiles: biosynthesis, biological functions and their applications in biotechnology

Naeem-ul-Hassan

Zainal

Ismail

2015

Plant Biotechnology Journal

143

111

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SummaryPlants have evolved numerous constitutive and inducible defence mechanisms to cope with biotic and abiotic stresses. These stresses induce the expression of various genes to activate defence-related pathways that result in the release of defence chemicals. One of these defence mechanisms is the oxylipin pathway, which produces jasmonates, divinylethers and green leaf volatiles (GLVs) through the peroxidation of polyunsaturated fatty acids (PUFAs). GLVs have recently emerged as key players in plant defence, plant-plant interactions and plant-insect interactions. Some GLVs inhibit the growth and propagation of plant pathogens, including bacteria, viruses and fungi. In certain cases, GLVs released from plants under herbivore attack can serve as aerial messengers to neighbouring plants and to attract parasitic or parasitoid enemies of the herbivores. The plants that perceive these volatile signals are primed and can then adapt in preparation for the upcoming challenges. Due to their 'green note' odour, GLVs impart aromas and flavours to many natural foods, such as vegetables and fruits, and therefore, they can be exploited in industrial biotechnology. The aim of this study was to review the progress and recent developments in research on the oxylipin pathway, with a specific focus on the biosynthesis and biological functions of GLVs and their applications in industrial biotechnology.

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Section: Biosynthesis Of Glvsmentioning

confidence: 97%

Section: Biosynthesis Of Glvsmentioning

confidence: 99%

Green leaf volatiles: biosynthesis, biological functions and their applications in biotechnology

Naeem-ul-Hassan

Zainal

Ismail

2015

Plant Biotechnology Journal

143

111

View full text Add to dashboard Cite

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“…Like all CYP74, HPL is a heme protein with 2.2 mol of heme b per mol enzyme [105,138,145]. Circular dichroism analysis demonstrated that the protein secondary structure is composed of approximately 13% α-helix, 32% β-sheet, 21% turns, and 31% unordered coils [146,147].…”

Section: Hpl Activitymentioning

confidence: 99%

Biocatalytic Synthesis of Natural Green Leaf Volatiles Using the Lipoxygenase Metabolic Pathway

et al. 2019

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In higher plants, the lipoxygenase enzymatic pathway combined actions of several enzymes to convert lipid substrates into signaling and defense molecules called phytooxylipins including short chain volatile aldehydes, alcohols, and esters, known as green leaf volatiles (GLVs). GLVs are synthesized from C18:2 and C18:3 fatty acids that are oxygenated by lipoxygenase (LOX) to form corresponding hydroperoxides, then the action of hydroperoxide lyase (HPL) produces C6 or C9 aldehydes that can undergo isomerization, dehydrogenation, and esterification. GLVs are commonly used as flavors to confer a fresh green odor of vegetable to perfumes, cosmetics, and food products. Given the increasing demand in these natural flavors, biocatalytic processes using the LOX pathway reactions constitute an interesting application. Vegetable oils, chosen for their lipid profile are converted in natural GLVs with high added value. This review describes the enzymatic reactions of GLVs biosynthesis in the plant, as well as the structural and functional properties of the enzymes involved. The various stages of the biocatalytic production processes are approached from the lipid substrate to the corresponding aldehyde or alcoholic aromas, as well as the biotechnological improvements to enhance the production potential of the enzymatic catalysts.

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“…However, compared with these fused lipoxygenases, the quite exceptional trait of PhLOX was its LOX-AOS-HPL activities in one catalytic domain which belongs to a conserved nonheme LOX family. And unlike some HPL enzymes harvested from some plants, , PhLOX does not contain a N-terminal transit peptide. Hence, there was no insertion of the recombinant enzyme in the membrane during expression in E. coli , and a larger amount of the enzyme could thus be recovered in the soluble protein fraction.…”

Section: Discussionmentioning

confidence: 99%

One-Step Bioconversion of Fatty Acids into C8–C9 Volatile Aroma Compounds by a Multifunctional Lipoxygenase Cloned from Pyropia haitanensis

Zhu

Chen

et al. 2018

J. Agric. Food Chem.

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The multifunctional lipoxygenase PhLOX cloned from Pyropia haitanensis was expressed in Escherichia coli with 24.4 mg·L yield. PhLOX could catalyze the one-step bioconversion of C18-C22 fatty acids into C8-C9 volatile organic compounds (VOCs), displaying higher catalytic efficiency for eicosenoic and docosenoic acids than for octadecenoic acids. C20:5 was the most suitable substrate among the tested fatty acids. The C8-C9 VOCs were generated in good yields from fatty acids, e.g., 2E-nonenal from C20:4, and 2E,6Z-nonadienal from C20:5. Hydrolyzed oils were also tested as substrates. The reactions mainly generated 2E,4E-pentadienal, 2E-octenal, and 2E,4E-octadienal from hydrolyzed sunflower seed oil, corn oil, and fish oil, respectively. PhLOX showed good stability after storage at 4 °C for 2 weeks and broad tolerance to pH and temperature. These desirable properties of PhLOX make it a promising novel biocatalyst for the industrial production of volatile aroma compounds.

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Predicted secondary structure of hydroperoxide lyase from green bell pepper cloned in the yeast Yarrowia lipolytica

Cited by 9 publications

References 19 publications

Green leaf volatiles: biosynthesis, biological functions and their applications in biotechnology

Green leaf volatiles: biosynthesis, biological functions and their applications in biotechnology

Biocatalytic Synthesis of Natural Green Leaf Volatiles Using the Lipoxygenase Metabolic Pathway

One-Step Bioconversion of Fatty Acids into C8–C9 Volatile Aroma Compounds by a Multifunctional Lipoxygenase Cloned from Pyropia haitanensis

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