Journal of Microbiology

Review

[MINIREVIEW] Antimicrobial actions of dual oxidases and lactoperoxidase: Demba Sarr , Eszter Tóth , Aaron Gingerich , Balázs Rada; J. Microbiol. 2018;56(6):373-386. Published online June 1, 2018; DOI: https://doi.org/10.1007/s12275-018-7545-1

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The NOX/DUOX family of NADPH oxidases are transmembrane proteins generating reactive oxygen species as their primary enzymatic products. NADPH oxidase (NOX) 1–5 and Dual oxidase (DUOX) 1 and 2 are members of this family. These enzymes have several biological functions including immune defense, hormone biosynthesis, fertilization, cell proliferation and differentiation, extracellular matrix formation and vascular regulation. They are found in a variety of tissues such as the airways, salivary glands, colon, thyroid gland and lymphoid organs. The discovery of NADPH oxidases has drastically transformed our view of the biology of reactive oxygen species and oxidative stress. Roles of several isoforms including DUOX1 and DUOX2 in host innate immune defense have been implicated and are still being uncovered. DUOX enzymes highly expressed in the respiratory and salivary gland epithelium have been proposed as the major sources of hydrogen peroxide supporting mucosal oxidative antimicrobial defenses. In this review, we shortly present data on DUOX discovery, structure and function, and provide a detailed, upto- date summary of discoveries regarding antibacterial, antiviral, antifungal, and antiparasitic functions of DUOX enzymes. We also present all the literature describing the immune functions of lactoperoxidase, an enzyme working in partnership with DUOX to produce antimicrobial substances.

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Research Support, Non-U.S. Gov'ts

Enhanced Expression of Laccase during the Degradation of Endocrine Disrupting Chemicals in Trametes versicolor: Yunjung Kim , Sumin Yeo , Hong-Gyu Song , Hyoung T. Choi; J. Microbiol. 2008;46(4):402-407. Published online August 31, 2008; DOI: https://doi.org/10.1007/s12275-007-0236-y

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Abstract: A putative laccase cDNA from a white-rot basidiomycete, Trametes versicolor, that consisted of 1,769 nucleotides was cloned using the rapid amplification of cDNA ends (RACE)-PCR method. The deduced amino acid sequence had 4 putative copper binding regions, which are common to fungal laccases. In addition, the sequence was 57~97% homologous to sequences of other T. versicolor laccases. Additionally, the expression of laccase and manganese peroxidase in this fungus were both greatly increased under degrading conditions for bisphenol A, nonylphenol and two phthalic esters (benzylbutylphthalate and diethylphthalate), all of which are reportedly endocrine disrupting chemicals (EDCs). Furthermore, the estrogenic activities of the EDCs also decreased rapidly during incubation when examined in a two-hybrid yeast system. Finally, kojic acid inhibited the removal of estrogenic activities generated by bisphenol A and nonylphenol, which confirmed that laccase was involved in the degradation of EDCs in T. versicolor.

Generation of a Transformant Showing Higher Manganese Peroxidase (Mnp) Activity by Overexpression of Mnp Gene in Trametes versicolor: Sumin Yeo , Nammee Park , Hong-Gyu Song , Hyoung T. Choi; J. Microbiol. 2007;45(3):213-218.; DOI: https://doi.org/2540 [pii]

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Abstract: Trametes versicolor has a lignin degrading enzyme system, which is also involved in the degradation of diverse recalcitrant compounds. Manganese-dependent peroxidase (MnP) is one of the lignin degrading enzymes in T. versicolor. In this study, a cDNA clone of a putative MnP-coding gene was cloned and transferred into an expression vector (pBARGPE1) carrying a phosphinothricin resistance gene (bar) as a selectable marker to yield the expression vector, pBARTvMnP2. Transformants were generated through genetic transformation using pBARTvMnP2. The genomic integration of the MnP clone was confirmed by PCR with bar-specific primers. One transformant showed higher enzyme activity than the recipient strain did, and was genetically stable even after 10 consecutive transfers on non-selective medium.

Purification and Characterization of Manganese Peroxidase of the White-Rot Fungus Irpex lacteus: Kwang-Soo Shin , Young Hwan Kim , Jong-Soon Lim; J. Microbiol. 2005;43(6):503-509.; DOI: https://doi.org/2298 [pii]

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Abstract: The production of manganese peroxidase (MnP) by Irpex lacteus, purified to electrophoretic homogeneity by acetone precipitation, HiPrep Q and HiPrep Sephacryl S-200 chromatography, was shown to correlate with the decolorization of textile industry wastewater. The MnP was purified 11.0-fold, with an overall yield of 24.3%. The molecular mass of the native enzyme, as determined by gel filtration chromatography, was about 53 kDa. The enzyme was shown to have a molecular mass of 53.2 and 38.3 kDa on SDS-PAGE and MALDI-TOF mass spectrometry, respectively, and an isoelectric point of about 3.7. The enzyme was optimally active at pH 6.0 and between 30 and 40oC. The enzyme efficiently catalyzed the decolorization of various artificial dyes and oxidized Mn (II) to Mn (III) in the presence of H2O2. The absorption spectrum of the enzyme exhibited maxima at 407, 500, and 640 nm. The amino acid sequence of the three tryptic peptides was analyzed by ESI Q-TOF MS/MS spectrometry, and showed low similarity to those of the extracellular peroxidases of other white-rot basidiomycetes.

Cloning of a Manganese Peroxidase cDNA Gene Repressed by Manganese in Trametes versicolor: Yongho Kim , Sumin Yeo , Joohee Kum , Hong-Gyu Song , Hyoung T. Choi; J. Microbiol. 2005;43(6):569-571.; DOI: https://doi.org/2288 [pii]

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Abstract: White-rot fungi have the following enzyme systems for lignin degradation: laccase, lignin peroxidase and manganese peroxidase. There are other types of peroxidases related to lignin degradation, one of which we have cloned a cDNA gene of manganese-repressed peroxidase (MrP) in Trametes versicolor isolated in South Korea. The mrp transcript level has been decreased by 1 M of Mn2+.

Journal Article

The Role of Enzymes Produced by White-Rot Fungus Irpex lacteus in the Decolorization of the Textile Industry Effluent: Kwang-Soo Shin; J. Microbiol. 2004;42(1):37-41.; DOI: https://doi.org/2003 [pii]

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Abstract: The textile industry wastewater has been decolorized efficiently by the white rot fungus, Irpex lacteus, without adding any chemicals. The degree of the decolorization of the dye effluent by shaking or stationary cultures is 59 and 93%, respectively, on the 8th day. The higher level of manganese-dependent peroxidase (MnP) and non-specific peroxidase (NsP) was detected in stationary cultures than in the cultures shaken. Laccase activities were equivalent in both cultures and its level was not affected significantly by the culture duration. Neither lignin peroxidase (LiP) nor Remazol Brilliant Blue R oxidase (RBBR ox) was detected in both cultures. The absorbance of the dye effluent was significantly decreased by the stationary culture filtrate of 7 days in the absence of Mn (II) and veratryl alcohol. In the stationary culture filtrate, three or more additional peroxidase bands were detected by the zymogram analysis.

Pleiotrohpic effect of a gene fragment conferring H₂O₂resistance in streptomyces coelicolor: Um, Tae Han , Oh, Chung Hun , Lee, Jong Soo , Park, Yong Doo , Roe, Jung Hye , Kim, Jae Heon; J. Microbiol. 1995;33(4):339-343.

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Abstract: We isolated a 10 kb Bam HI fragment originated from the chromosome of a H₂O₂-resistant mutant strain of Streptomyces coelicolor, which confer H₂O₂-resistance to S. lividance upon transformation. Among various subclones ot 10kb Bam HI fragment tested for their H₂O₂-resistant phenotype in S. lividans, a subclone containing 5.2 kb Bam HI-BglII fragment was found to be responsible for H₂O₂-resistance. The plasmid containing this 5.2 kb fragment was then transformed into S. coellicolor A3(2) at early and tested for their phenotype of H₂O₂-resistance and the change in various enzymes whose activity can be stained in the gel. We found out that the 5.2 kb insert DNA conferred H₂O₂-resisstance in S. coelicolor A3(2) at early phase of cell growth. The presence of this DNA also resulted in higher level of peroxidase compared with the wild type cell containing parental vector (pIJ702) only. Esterase activity was also higher in this clone. However, alcohol dehydrogenase activity decreased compared with the wild type. These results suggest that the presence of a gene in 5.2 kb BamHI-BglII DNA fragment causes multiple changes in S. coelicolor related to its response against hydrogen peroxide. The result also implies that not only peroxidase but also esterase may function in the defencse meahsnism agianst H₂O₂.

Growth on methanol of a carboxydobacterium, acinetobacter sp. strain JC1 DSM 3803: Ro, Young Tae , Seo, Jae Goo , Lee, Joo Hun , Kim, Dae Myung , Chung, In Kwon , Kim, Tae Ue , Kim, Young Min; J. Microbiol. 1997;35(1):30-39.

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Abstract: Acinetobacter sp. strain JC1 DSM 3803, a carboxydobacterium, was found to grow methylotrophically at the expense of methanol and methlamine, but not of methane, formaldehyde, formate, dimethylamine, or trimethylamine, as the sole source of carbon and energy. The doubling times of the bacterium growing on methanol (0.5% v/v) and methylamine (0.5% w/v) at 30℃ and pH 6.8 were 4.8 h and 5.7 h respectively. Cells grown on methanol, however, failed to show typical methanol dehydrogenase and oxidase activities. The cell was found to contain no c-type cytochromes. Cells grown on methanol exhibited higher catalase activity than those grown on pyruvate or glucose. The catalase present in the cells also exhibited peroxidase activity. The catalase activity, growth on methanol of the cell, and oxygen consumption by methanol-grown maldehyde dehydrogenase, formaldehyde reductase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase activities were detected from cells grown on methanol.

Enzyme Activities Related to the Methanol Oxidation of Mycobacterium sp. strain JC1 DSM 3803: Youngtae Ro , Eungbin Kim , Youngmin Kim; J. Microbiol. 2000;38(4):209-217.

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Abstract: Mycobacterium sp. strain JC1 DSM 3803 grown in methanol showed no methanol dehydrogenase or oxidase activities found in most methylotrophic bacteria and yeasts, respectively. Even though the methanol-grown cells exhibited a little methanol-dependent oxidation by cytochrome c-dependent methanol dehydrogenase and alcohol dehydrogenase, they were not the key enzymes responsible for the methanol oxidation of the cells, in that the cells contained no c-type cytochrome and the methanol oxidizing activity from the partially purified alcohol dehydrogenase was too low, respectively. In substrate switching experiments, we found that only a catalase-peroxidase among the three types of catalase found in glucose-grown cells was highly expressed in the methanol-grown cells and that its activity was relatively high during the exponential growth phase in Mycobacterium sp. JC1. Therefore, we propose that catalase-peroxidase is an essential enzyme responsible for the methanol metabolism directly or indirectly in Mycobacterium sp. JC1.

Analysis of Catalases from Photosynthetic Bacterium Rhodospirillum rubrum S1: Hee-Kyoung Lim , Young-Mi Kim , Dong-Heon Lee , Hyung-Yeel Kahng , Duck-Chul Oh; J. Microbiol. 2001;39(3):168-176.

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Abstract: Five different types of catalases from photosynthetic bacterium Rhodospirillum rubrum S1 grown aerobically in the dark were found in this study, and designated Cat1 (350 kDa), Cat2 (323 kDa), Cat3 (266 kDa), Cat4 (246 kDa), and Cat5 (238 kDa). Analysis of native PAGE revealed that Cat2, Cat3, and Cat4 were also produced in the cells anaerobically grown in the light. It is notable that only Cat2 was expressed much more strongly in response to the anaerobic condition. Enzyme activity staining demonstrated that Cat3 and Cat4 had bifunctional catalase-peroxidase activities, while Cat1, Cat2, and Cat5 were typical monofunctional catalases. S1 cells grown aerobically in the presence of malate as the sole source of carbon exhibited an apparent catalase Km value of 10 mM and a Vmax of about 705 U/mg protein at late stationary growth phase. The catalase activity of S1 cells grown in the anaerobic environment exhibited a much lower Vmax of about 109 U/mg protein at late logarithmic growth phase. The catalytic activity was stable in the broad range of temperatures (30 C-60 C), and pH (6.0-10.0). R. rubrum S1 was much more resistant to H_2 O_2 in the stationary growth phase than in the exponential growth phase regardless of growth conditions. Cells of stationary growth phase treated with 15 mM H 2 O 2 for 1 h showed 3-fold higher catalase activities than the untreated cells. In addition, L-glutamate induced an 80-fold increase in total catalase activity of R. rubrum S1 compared with malic acid. Through fraction analyses of S1 cells, Cat2, Cat3, Cat4 and Cat5 were found in both cytoplasm and periplasm, while Cat1 was localized only in the cytoplasm.

Mutation Spectrum of Manganese (II) Peroxidase Gene in the Pleurotusostreatus Mutants Induced by Gamma Radiation: Hwa-Hyoung Chang^ , Young-Keun Lee^ , Jae-Sung Kim^ , Ki-Sung Lee^ , Kyu Seong Cho^; J. Microbiol. 2003;41(1):52-57.

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Abstract: The mutational spectra in the manganese (II) peroxidase gene (mnp) of the Pleurotus ostreatus mutants induced by gamma radiation (Co^60) give evidence to prove the effect of gamma radiation on the gene. mnp of each mutant was cloned, sequenced and analyzed. Among the 1941 base pairs of the sequenced region of the mnp genes of 4 mutants (PO-5, -6, -15 and -16), nine mutational hotspots on which the same base was mutated simultaneously were found, additionally 6 mutations were also found at different positions in the mnp gene. These mutation-spectra were predominantly A:T_G:C transitions (50.1%). By the analysis of putative amino acid sequences, PO-5 and PO-16 mutants have 3 and 1 mutated residues, respectively. Since the mutational spectra reported herein are specific to the mnp gene, we propose that the mutational hotspots for the gamma radiation could be in the gene(s) within cells.

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