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Title: Cloning and characterization of a cDNA encoding glyoxal oxidase, a H[sub 2]O[sub 2]-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
;  [1]
  1. Department of Agriculture, Madison, WI (United States) Univ. of Wisconsin, Madison (United States)

Glyoxal oxidase is produced by ligninolytic cultures of the white-rot fungus Phanerochaete chrysosporium and is a source of the extracellular H[sub 2]O[sub 2] that is required by ligninolytic peroxidases. The authors 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 [beta]-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. 19 refs., 2 figs.

DOE Contract Number:
FG02-87ER13712
OSTI ID:
5839132
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 90:15; ISSN 0027-8424
Country of Publication:
United States
Language:
English