HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mester, T. Articles by Field, J. A. Search for Related Content PubMed PubMed Citation Articles by Mester, T. Articles by Field, J. A. Social Bookmarking                      What's this?

J Biol Chem, Vol. 273, Issue 25, 15412-15417, June 19, 1998

Characterization of a Novel Manganese Peroxidase-Lignin Peroxidase Hybrid Isozyme Produced by Bjerkandera Species Strain BOS55 in the Absence of Manganese

From the Division of Industrial Microbiology, Department of Food Technology and Nutrition Sciences, Wageningen Agricultural University, P. O. Box 8129, 6700 EV Wageningen, The Netherlands

A novel manganese-dependent peroxidase (MnP) isozyme produced in manganese-free cultures of Bjerkandera sp. strain BOS55 was purified and characterized. The production of the enzyme was greatly stimulated by the exogenous addition of various physiological organic acids such as glycolate, glyoxylate, and oxalate. The physical properties of the enzyme are similar to those of MnP isozymes from different white rot fungi (M_r = 43,000, pI 3.88, and _407 nm = 123 mM¹ cm¹). The Bjerkandera MnP was efficient in the oxidation of Mn(II), as indicated by the kinetic constants (low K_m of 51 µM and turnover number of 59 s¹). Furthermore, the isozyme was able to oxidize various substrates in the absence of manganese, such as 2,6-dimethoxyphenol, guaiacol, ABTS, 3-hydroxyanthranilic acid, and o- and p-anisidine. An interesting characteristic of the isozyme was its ability to oxidize nonphenolic substrates, veratryl alcohol and 1,4-dimethoxybenzene, without manganese addition. The affinity for veratryl alcohol (K_m = 116 µM) and its turnover number (2.8 s¹) are comparable to those of lignin peroxidase (LiP) isozymes from other white rot fungi. Manganese at concentrations greater than 0.1 mM severely inhibited the oxidation of veratryl alcohol. The results suggest that this single isozyme is a hybrid between MnP and LiP found in other white rot fungi. The N-terminal amino acid sequence showed a very high homology to those of both MnP and LiP isozymes from Trametes versicolor.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				T. Tsukihara, Y. Honda, R. Sakai, T. Watanabe, and T. Watanabe Mechanism for Oxidation of High-Molecular-Weight Substrates by a Fungal Versatile Peroxidase, MnP2 Appl. Envir. Microbiol., May 1, 2008; 74(9): 2873 - 2881. [Abstract] [Full Text] [PDF]

				R. Pogni, M. C. Baratto, C. Teutloff, S. Giansanti, F. J. Ruiz-Duenas, T. Choinowski, K. Piontek, A. T. Martinez, F. Lendzian, and R. Basosi A Tryptophan Neutral Radical in the Oxidized State of Versatile Peroxidase from Pleurotus eryngii: A COMBINED MULTIFREQUENCY EPR AND DENSITY FUNCTIONAL THEORY STUDY J. Biol. Chem., April 7, 2006; 281(14): 9517 - 9526. [Abstract] [Full Text] [PDF]

				D. Schlosser and C. Hofer Laccase-Catalyzed Oxidation of Mn2+ in the Presence of Natural Mn3+ Chelators as a Novel Source of Extracellular H2O2 Production and Its Impact on Manganese Peroxidase Appl. Envir. Microbiol., July 1, 2002; 68(7): 3514 - 3521. [Abstract] [Full Text] [PDF]

				R. Cohen, O. Yarden, and Y. Hadar Lignocellulose Affects Mn2+ Regulation of Peroxidase Transcript Levels in Solid-State Cultures of Pleurotus ostreatus Appl. Envir. Microbiol., June 1, 2002; 68(6): 3156 - 3158. [Abstract] [Full Text] [PDF]

				F. J. Ruiz-Dueñas, M. J. Martínez, and A. T. Martínez Heterologous Expression of Pleurotus eryngii Peroxidase Confirms Its Ability To Oxidize Mn2+ and Different Aromatic Substrates Appl. Envir. Microbiol., October 1, 1999; 65(10): 4705 - 4707. [Abstract] [Full Text]

				S. Camarero, S. Sarkar, F. J. Ruiz-Duenas, M. J. Martinez, and A. T. Martinez Description of a Versatile Peroxidase Involved in the Natural Degradation of Lignin That Has Both Manganese Peroxidase and Lignin Peroxidase Substrate Interaction Sites J. Biol. Chem., April 9, 1999; 274(15): 10324 - 10330. [Abstract] [Full Text] [PDF]

				L. Caramelo, M. J. Martínez, and A. T. Martínez A Search for Ligninolytic Peroxidases in the Fungus Pleurotus eryngii Involving alpha -Keto-gamma -Thiomethylbutyric Acid and Lignin Model Dimers Appl. Envir. Microbiol., March 1, 1999; 65(3): 916 - 922. [Abstract] [Full Text]

				B. Böckle, M. J. Martínez, F. Guillén, and A. T. Martínez Mechanism of Peroxidase Inactivation in Liquid Cultures of the Ligninolytic Fungus Pleurotus pulmonarius Appl. Envir. Microbiol., March 1, 1999; 65(3): 923 - 928. [Abstract] [Full Text]

				P. J. Collins, M. M. O'Brien, and A. D. W. Dobson Cloning and Characterization of a cDNA Encoding a Novel Extracellular Peroxidase from Trametes versicolor Appl. Envir. Microbiol., March 1, 1999; 65(3): 1343 - 1347. [Abstract] [Full Text]

				T. Mester, K. Ambert-Balay, S. Ciofi-Baffoni, L. Banci, A. D. Jones, and M. Tien Oxidation of a Tetrameric Nonphenolic Lignin Model Compound by Lignin Peroxidase J. Biol. Chem., June 15, 2001; 276(25): 22985 - 22990. [Abstract] [Full Text] [PDF]