Phylogenetic analysis, molecular modeling, substrate–inhibitor specificity, and active site comparison of bacterial, fungal, and plant heme peroxidases

Singh, Swati; Pandey, Veda P.; Naaz, Huma; Dwivedi, Upendra N.

doi:10.1002/bab.1025

Cited by 11 publications

(2 citation statements)

References 49 publications

(47 reference statements)

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“…The heme peroxidases of non-animal origin show low amino acid sequence identity (less than 20%) but, share similar helical folds independent to the presence (in plant and fungal peroxidases) and absence (in bacterial peroxidases) of disulfide bridges and structural calcium ions. Recently [31] have also studied the comparative account of non-animal heme peroxidases and reported that the peroxidases are clustered into three major classes. In addition, [6] have suggested that the class I peroxidases are the origin point for the other two classes of peroxidases.…”

Section: Evolutionary Relationship Between Heme Peroxidasesmentioning

confidence: 99%

A Comprehensive Review on Function and Application of Plant Peroxidases

Pandey¹,

Awasthi²,

Singh³

et al. 2017

Biochem Anal Biochem

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Peroxidases, one of the key antioxidant enzymes, are widely distributed in nature and catalyze oxidation of various electron donor substrates concomitant with the decomposition of H 2 O 2. The non-animal plant peroxidases (class III peroxidase) are involved in various essential physiological processes of plant growth and development throughout their life cycle. In view of the capability of peroxidases to catalyze the redox reaction for a wide range of substrates, they are considered as one of the important enzyme from the point of view of their various medicinal, biochemical, immunological, biotechnological and industrial applications. They have been successfully used for biopulping and biobleaching in the paper and textile industries. Peroxidases have also been used in organic synthesis, bioremediation, as well as various analytical applications in diagnostic kits, ELISA. Peroxidase based biosensors find application in analytical systems for determination of hydrogen peroxide, glucose, alcohols, glutamate, and choline etc. Thus, in view of array of physiological functions as well as industrial applications, the peroxidases have conquered a dominant position in research groups and become one of the most extensively studied enzymes. In this direction, the present review embodies the classification, mechanism of action, major physiological functions as well as industrial applications of plant peroxidases.

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Section: Evolutionary Relationship Between Heme Peroxidasesmentioning

confidence: 99%

A Comprehensive Review on Function and Application of Plant Peroxidases

Pandey¹,

Awasthi²,

Singh³

et al. 2017

Biochem Anal Biochem

Self Cite

245

213

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“…7). 28 With regard to BOA-N-glucosylation, it is likely that peroxidases fulfill a function in glucoside carbamate production. These enzymes could be responsible for the generation of BOA radicals.…”

Section: Effects Of Peroxidase Inhibitor 23-butanedionementioning

confidence: 99%

Benzoxazolinone detoxification byN-Glucosylation: The multi-compartment-network ofZea maysL.

Schulz¹,

Filary²,

Kühn³

et al. 2016

Plant Signaling & Behavior

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The major detoxification product in maize roots after 24 h benzoxazolin-2(3H)-one (BOA) exposure was identified as glucoside carbamate resulting from rearrangement of BOA-N-glucoside, but the pathway of N-glucosylation, enzymes involved and the site of synthesis were previously unknown. Assaying whole cell proteins revealed the necessity of H2O2 and Fe(2+) ions for glucoside carbamate production. Peroxidase produced BOA radicals are apparently formed within the extraplastic space of the young maize root. Radicals seem to be the preferred substrate for N-glucosylation, either by direct reaction with glucose or, more likely, the N-glucoside is released by glucanase/glucosidase catalyzed hydrolysis from cell wall components harboring fixed BOA. The processes are accompanied by alterations of cell wall polymers. Glucoside carbamate accumulation could be suppressed by the oxireductase inhibitor 2-bromo-4´-nitroacetophenone and by peroxidase inhibitor 2,3-butanedione. Alternatively, activated BOA molecules with an open heterocycle may be produced by microorganisms (e.g., endophyte Fusarium verticillioides) and channeled for enzymatic N-glucosylation. Experiments with transgenic Arabidopsis lines indicate a role of maize glucosyltransferase BX9 in BOA-N-glycosylation. Western blots with BX9 antibody demonstrate the presence of BX9 in the extraplastic space. Proteomic analyses verified a high BOA responsiveness of multiple peroxidases in the apoplast/cell wall. BOA incubations led to shifting, altered abundances and identities of the apoplast and cell wall located peroxidases, glucanases, glucosidases and glutathione transferases (GSTs). GSTs could function as glucoside carbamate transporters. The highly complex, compartment spanning and redox-regulated glucoside carbamate pathway seems to be mainly realized in Poaceae. In maize, carbamate production is independent from benzoxazinone synthesis.

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Optimization of the enzymatic hydrolysis of Moringa oleifera Lam oil using molecular docking analysis for fatty acid specificity

Barbosa

Freire

Almeida

et al. 2019

Biotech and App Biochem

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Alternative strategies are required to develop the optimized production of fatty acids using biocatalysis; molecular docking and response surface methodology are efficient tools to achieve this goal. In the present study, we demonstrate a novel and robust methodology for the sustainable production of fatty acids from Moringa oleifera Lam oil using lipase‐catalyzed hydrolysis (without the presence of emulsifiers or buffer solutions). Seven commercial lipases from Candida rugosa (CRL), Burkholderia cepacia (BCL), Thermomyces lanuginosus (TLL), Rhizopus niveus (RNL), Pseudomonas fluorescens (PFL), Mucor javanicus (MJL), and porcine pancreas (PPL) were used as biocatalysts. Initial screening showed that CRL had the highest hydrolytic activity (hydrolysis degree of 81%). Molecular docking analysis contributed to the experimental results, showing that CRL displays more stable binding free energy with oleic acid (C18:1), which is the fatty acid of highest concentration in Moringa oleifera Lam oil. To evaluate and optimize the hydrolysis process, response surface methodology (RSM) was used. The effect of temperature, mass ratio oil:water, and hydrolytic activity on enzymatic hydrolysis was evaluated by central composite design using RSM. Under the optimized conditions (temperature of 37 °C, mass ratio oil:water of 25%, and hydrolytic activity of 550 U goil−1), the maximum hydrolysis degree (100%) was achieved. The present study provides a robust method for the enzymatic hydrolysis of different oils for efficient and sustainable fatty acid production.

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Phylogenetic analysis, molecular modeling, substrate–inhibitor specificity, and active site comparison of bacterial, fungal, and plant heme peroxidases

Cited by 11 publications

References 49 publications

A Comprehensive Review on Function and Application of Plant Peroxidases

A Comprehensive Review on Function and Application of Plant Peroxidases

Benzoxazolinone detoxification byN-Glucosylation: The multi-compartment-network ofZea maysL.

Optimization of the enzymatic hydrolysis of Moringa oleifera Lam oil using molecular docking analysis for fatty acid specificity

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