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PMID: 3553159 Published · ppublish English Journal Article

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

Journal of bacteriology ·Vol. 169 ·No. 5 ·1987-05-00 ·Pages 2195-201

Kersten PJ, Kirk TK

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.

MeSH Terms
Alcohol Oxidoreductases/metabolism Aldehydes/metabolism Basidiomycota/enzymology Biodegradation, Environmental Extracellular Space/enzymology Glyoxal/metabolism Hydrogen Peroxide/metabolism Hydrogen-Ion Concentration Isoelectric Focusing Kinetics Lignin/metabolism Oxidation-Reduction Oxidoreductases/metabolism Substrate Specificity
Chemicals
Aldehydes Glyoxal Lignin Hydrogen Peroxide Oxidoreductases Alcohol Oxidoreductases glyoxal oxidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kersten P J
Kirk T K
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24 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1987-05-00
Pages
2195-201
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC212128
Subset
IM
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