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Title: Cloning and characterization of a cDNA encoding glyoxal oxidase, a H2O2-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium

Source: Proc. Natl. Acad. Sci.; Vol. 90, pp. 7411-7413, August 1993

Author(s)Kersten, Philip J.; Cullen, Daniel

Publication Year: 1993  View PDF »

Category: Journal Articles

Abstract: Glyoxal oxidase is produced by ligninolytic cultures of the white-rot fungus Phanerochaete chrysosporium and is a source of the extracellular H2O2 that is required by ligninolytic peroxidases. We report here the cloning and characterization of glx-1c cDNA, which encodes glyoxal oxidase. The deduced mature protein has 537 amino acids, a molecular size of 57 kDa, and a pI of 5.1. Five potential N-glycosylation sites are present. The predicted N-terminal sequence is identical to the experimentally determined sequence of purified enzyme and is preceded by a leader peptide of 22 amino acids. The sequence of glx-1c lacks significant homology with known sequences. Specific comparisons were made between the glx-1c translated sequence and that of galactose oxidase from Dactylium dendroides because of previously observed catalytic similarities of the enzyme. Although no significant homology is observed, in both cases extensive B-sheet regions are predicted from the primary sequences. Glyoxal oxidase activity correlates with transcript levels and is also coordinate with the lignin peroxidases in nutrient nitrogen-starved cultures.

Keywords: P. chrysosporium, cloning, cDNA, glyoxal oxidase

File size: 303 kb(s)

Date posted: 05/19/2010
Current FPL Scientists associated with this product (listed alphabetically)
Cullen, Daniel
Research Microbiologist
Kersten, Philip J.
Research Microbiologist
 

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