Advances in Aspergillus secondary metabolite research in the post-genomic era

Sanchez, James F.; Somoza, Amber D.; Keller, Nancy P.; Wang, Clay C. C.

doi:10.1039/c2np00084a

Cited by 244 publications

(204 citation statements)

References 144 publications

(175 reference statements)

Supporting

Mentioning

194

Contrasting

Unclassified

Order By: Relevance

“…VIII). The fact that two 10 R -HPODE-producing subfamilies have evolved in parallel strengthens previous reports that 10 R -HPODE is of biological importance ( 44 ).…”

Section: Discussionsupporting

confidence: 70%

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

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

“…VIII). The fact that two 10 R -HPODE-producing subfamilies have evolved in parallel strengthens previous reports that 10 R -HPODE is of biological importance ( 44 ).…”

Section: Discussionsupporting

confidence: 70%

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

View full text Add to dashboard Cite

show abstract

“…19) However, it was reported that certain strains of A. niger could produce ochratoxin and fumonisin while some strains of A. oryzae could produce aflatoxin and cyclopiazonic acid. 20) In the present study, these mycotoxins were not detected in the fermented KGB (data not shown).…”

Section: Methodsmentioning

confidence: 69%

Korean Ginseng Berry Fermented by Mycotoxin Non-producing <i>Aspergillus niger</i> and <i>Aspergillus oryzae</i>: Ginsenoside Analyses and Anti-proliferative Activities

Ahn

Kim

et al. 2016

Biological & Pharmaceutical Bulletin

View full text Add to dashboard Cite

To transform ginsenosides, Korean ginseng berry (KGB) was fermented by mycotoxin non-producing Aspergillus niger and Aspergillus oryzae. Changes of ginsenoside profile and anti-proliferative activities were observed. Results showed that A. niger tended to efficiently transform protopanaxadiol (PPD) type ginsenosides such as Rb1, Rb2, Rd to compound K while A. oryzae tended to efficiently transform protopanaxatriol (PPT) type ginsenoside Re to Rh1 via Rg1. Butanol extracts of fermented KGB showed high cytotoxicity on human adenocarcinoma HT-29 cell line and hepatocellular carcinoma HepG2 cell line while that of unfermented KGB showed little. The minimum effective concentration of niger-fermented KGB was less than 2.5 µg/mL while that of oryzae-fermented KGB was about 5 µg/mL. As A. niger is more inclined to transform PPD type ginsenosides, niger-fermented KGB showed stronger anti-proliferative activity than oryzaefermented KGB.

show abstract

“…Racemic 9-and 13-HPODE were obtained by photo Fungal pathogens may secrete LOXs during invasive growth to generate reactive oxygen species and lysis of membranes. Fungal LOXs may also regulate biosynthesis of secondary metabolites and toxins, including biosynthesis of jasmonates ( 11,(13)(14)(15)(16)(17).…”

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

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

Advances in Aspergillus secondary metabolite research in the post-genomic era

Cited by 244 publications

References 144 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

Korean Ginseng Berry Fermented by Mycotoxin Non-producing <i>Aspergillus niger</i> and <i>Aspergillus oryzae</i>: Ginsenoside Analyses and Anti-proliferative Activities

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

Contact Info

Product

Resources

About