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

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kuan, I. C. Articles by Tien, M. Search for Related Content PubMed PubMed Citation Articles by Kuan, I. C. Articles by Tien, M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 264, Issue 34, 20350-20355, 12, 1989

Phosphorylation of lignin peroxidases from Phanerochaete chrysosporium. Identification of mannose 6-phosphate

IC Kuan and M Tien
Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.

Many of the extracellular lignin-degrading peroxidases from the wood- degrading fungus Phanerochaete chrysosporium are phosphorylated. Immunoprecipitation of the extracellular fluid of cultures grown with H2K32PO4 with a polyclonal antibody raised against one of the lignin peroxidase isozymes, H8 (pI 3.5), revealed the incorporation of H2K32PO4 into lignin peroxidases. Analyses of the purified isozymes from labeled cultures by isoelectric focusing showed that, in addition to isozyme H8, lignin peroxidase isozymes H2 (pI 4.4), H6 (pI 3.7), and H10 (pI 3.3) are also phosphorylated. These analyses also showed that lignin peroxidase isozyme H1 (pI 4.7) and manganese-dependent peroxidase isozymes H3 (pI 4.9) and H4 (pI 4.5) are not phosphorylated. Phosphate quantitation indicated the presence of one molecule of phosphate/molecule of enzyme for all of the phosphorylated isozymes. To locate the site of phosphorylation, one-dimensional phosphoamino acid analysis was performed with hydrolyzed 32P-protein. However, phosphotyrosine, phosphoserine, and phosphothreonine could not be identified. Coupled enzyme assays of acid hydrolysate indicated the presence of mannose 6-phosphate as the phosphorylated component on the lignin peroxidase isozymes. Digestion of the isozymes with N-glycanase released the phosphate component, indicating that the mannose 6- phosphate is contained on an asparagine-linked oligosaccharide.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				L. F. Larrondo, S. Lobos, P. Stewart, D. Cullen, and R. Vicuña Isoenzyme Multiplicity and Characterization of Recombinant Manganese Peroxidases from Ceriporiopsis subvermispora and Phanerochaete chrysosporium Appl. Envir. Microbiol., May 1, 2001; 67(5): 2070 - 2075. [Abstract] [Full Text]

				Y. J. Cai, S. J. Chapman, J. A. Buswell, and S.-t. Chang Production and Distribution of Endoglucanase, Cellobiohydrolase, and beta -Glucosidase Components of the Cellulolytic System of Volvariella volvacea, the Edible Straw Mushroom Appl. Envir. Microbiol., February 1, 1999; 65(2): 553 - 559. [Abstract] [Full Text]