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Volume 155, Issue 8

Oxalate decarboxylase of the white-rot fungus demonstrates a novel enzyme primary structure and non-induced expression on wood and in liquid cultures Free

Abstract

Oxalate decarboxylase (ODC) catalyses the conversion of oxalic acid to formic acid and CO in bacteria and fungi. In wood-decaying fungi the enzyme has been linked to the regulation of intra- and extracellular quantities of oxalic acid, which is one of the key components in biological decomposition of wood. ODC enzymes are biotechnologically interesting for their potential in diagnostics, agriculture and environmental applications, e.g. removal of oxalic acid from industrial wastewaters. We identified a novel ODC in mycelial extracts of two wild-type isolates of , and cloned the corresponding gene. The primary structure of the Ds-ODC protein contains two conserved Mn-binding cupin motifs, but at the N-terminus, a unique, approximately 60 aa alanine-serine-rich region is found. Real-time quantitative RT-PCR analysis confirmed gene expression when the fungus was cultivated on wood and in liquid medium. However, addition of oxalic acid in liquid cultures caused no increase in transcript amounts, thereby indicating a constitutive rather than inducible expression of . The detected stimulation of ODC activity by oxalic acid is more likely due to enzyme activation than to transcriptional upregulation of the gene. Our results support involvement of ODC in primary rather than secondary metabolism in fungi.

  • Received:
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  • Published Online:
Keyword(s): FDH, formate dehydrogenase , FPLC, fast protein liquid chromatography , GAPDH, glyceraldehyde-3-phosphate dehydrogenase , ODC, oxalate decarboxylase , OXC, oxalyl-CoA decarboxylase , OXO, oxalate oxidase , qRT-PCR, quantitative RT-PCR and UTR, untranscribed region
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2009-08-01
2024-04-19
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Oxalate decarboxylase of the white-rot fungus Dichomitus squalens demonstrates a novel enzyme primary structure and non-induced expression on wood and in liquid cultures
Microbiology 155, 2726 (2009); https://doi.org/10.1099/mic.0.028860-0
/content/journal/micro/10.1099/mic.0.028860-0
/content/journal/micro/10.1099/mic.0.028860-0
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