Thirty years of heme peroxidase structural biology

Poulos, T.L.

doi:10.1016/j.abb.2010.02.008

Cited by 108 publications

(109 citation statements)

References 101 publications

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“…To the best of our knowledge, 10 R -DOX-EAS is the fi rst described EAS with an intramolecular and position-specifi c oxygenation mechanism associated with heterolytic scission of the dioxygen bond. Heterolytic scission of dioxygen bonds are also catalyzed by heme peroxidases and presumably also by the secreted EAS of Magnaporthe salvinii ( 41,42 ). Intramolecular oxygen transfer has also been described by arachidonate 12-Lipoxygenase linked to diol synthase activities in the red alga Gracilariopsis lemaneiformis and by 15-Lipoxygenase linked to epoxygenase activities of the fungus Saprolegnia parasitica ( 1,43 ).…”

Section: Crucial Amino Acid Residues Of the Eas Domain Of Mgg_10859mentioning

confidence: 97%

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

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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

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Section: Crucial Amino Acid Residues Of the Eas Domain Of Mgg_10859mentioning

confidence: 97%

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

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“…The roles of plant peroxidases have been under investigation for a long time. Horseradish root POX was the first one to be isolated and characterized in the 1940's (Poulos, 2010), and until today some aspects about its function are not completely understood. In this work, we isolated and characterized a plant peroxidase from umbu xylopodium exsudate.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a peroxidase present in xilopodium exsudates of umbu plants (Spondias tuberosa A.)

Pinto¹,

Ribeiro²,

Araujo³

et al. 2015

Afr. J. Biotechnol.

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Umbu plants are drought resistant trees which are able to store water and several other substances into its adapted root, named xylopodium. The exsudate from xilopodium is a natural solution rich in salts, sugars and a little concentration of proteins. In this work, we report the purification of a peroxidase (POX) from umbu xilopodium exsudate by direct extraction from polyacrylamide electrophoresis gels. Umbu POX showed optimum activity at pHs around 6.0 to 7.0 and high thermal resistance after incubation at 70°C for 6 min. POX activity present in crude extracts was more heat-resistant than in its purified form. When assayed with metal ions, umbu POX activity was shown to be inhibited by Mn 2+ and stimulated by Ca 2+ and Mg 2+ ; it was also inhibited by sodium azide (concentrations higher then 1 mM) and not inhibited by either EDTA or tropolone. POX Km values for guaiacol and methylcatechol substrates were 6.83 and 22.25, respectively. The enzyme is proposed to be a guaiacol peroxidase and was seen to be located at higher concentrations in the outermost layers of xylopodium tissue, such as the endoderm.

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“…In certain cases, the radical in compound I resides on an amino acid, e.g. Trp in cytochrome c peroxidase (28). One-electron reduction of this radical yields compound II, referring to the remaining Fe IV ϭO iron center.…”

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confidence: 99%

Human Indoleamine 2,3-Dioxygenase Is a Catalyst of Physiological Heme Peroxidase Reactions

Freewan

Rees

Plaza

et al. 2013

Journal of Biological Chemistry

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Background: Certain heme proteins exhibit a pseudo-peroxidase activity that alters their function. Results: H 2 O 2 engages the peroxidase activity of indoleamine 2,3-dioxygenase (IDO) to oxidatively inactivate its dioxygenase activity, consume nitric oxide, and promote IDO protein nitration. Conclusion: IDO is a catalyst of physiological peroxidase reactions. Significance: IDO peroxidase activity has novel implications for the control and biological actions of this important immune regulatory enzyme.

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Thirty years of heme peroxidase structural biology

Abstract: The following is a brief review of peroxidase structural biology since the initial structure determination of cytochrome c peroxidase (CCP) 30 years ago. An emphasis will be placed on what CCP has taught us about peroxidase mechanisms, especially Compound I formation and electron transfer.

Cited by 108 publications

References 101 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

Purification and characterization of a peroxidase present in xilopodium exsudates of umbu plants (Spondias tuberosa A.)

Human Indoleamine 2,3-Dioxygenase Is a Catalyst of Physiological Heme Peroxidase Reactions

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