Cloning and characterization of cDNA encoding glyoxal oxidase, a H2O2-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium.
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 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.
Kersten
P J
PJ
Institute for Microbial and Biochemical Technology, U.S. Department of Agriculture, Madison, WI 53705.
Cullen
D
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D000429:Alcohol Oxidoreductases / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D001487:Basidiomycota / Q000201:enzymology / Q000235:genetics*; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics*; D015870:Gene Expression; D005800:Genes, Fungal; D008031:Lignin / Q000378:metabolism; D008969:Molecular Sequence Data; D012331:RNA, Fungal / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics
D005656:Fungal Proteins; D012331:RNA, Fungal; D012333:RNA, Messenger; D008031:Lignin; D004247:DNA; D000429:Alcohol Oxidoreductases; C052371:glyoxal oxidase