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. 1987 May;169(5):2195–2201. doi: 10.1128/jb.169.5.2195-2201.1987

Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium.

P J Kersten, T K Kirk
PMCID: PMC212128  PMID: 3553159

Abstract

The importance of extracellular H2O2 in lignin degradation has become increasingly apparent with the recent discovery of H2O2-requiring ligninases produced by white-rot fungi. Here we describe a new H2O2-producing activity of Phanerochaete chrysosporium that involves extracellular oxidases able to use simple aldehyde, alpha-hydroxycarbonyl, or alpha-dicarbonyl compounds as substrates. The activity is expressed during secondary metabolism, when the ligninases are also expressed. Analytical isoelectric focusing of the extracellular proteins, followed by activity staining, indicated that minor proteins with broad substrate specificities are responsible for the oxidase activity. Two of the oxidase substrates, glyoxal and methylglyoxal, were also identified, as their quinoxaline derivatives, in the culture fluid as secondary metabolites. The significance of these findings is discussed with respect to lignin degradation and other proposed systems for H2O2 production in P. chrysosporium.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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