A novel enzymatic decarboxylation of oxalic acid by the lignin peroxidase system of white-rot fungus Phanerochaete chrysosporium.
Oxidation of veratryl alcohol by lignin peroxidase (LiP) was potently inhibited by oxalic acid. The inhibition analysis with Lineweaver-Burk plots clearly showed that the type of inhibition is non-competitive. The enzymatic oxidation of veratryl alcohol in the presence of 14C-oxalic acid yielded radioactive carbon dioxide. The results indicate that the apparent inhibition of LiP is caused by reduction of the veratryl alcohol cation radical intermediate back to the substrate level by oxalate, which is concomitantly oxidized to carbon dioxide.
Akamatsu
Y
Y
Wood Research Institute, Kyoto University, Japan.
Ma
D B
DB
Higuchi
T
T
Shimada
M
M
D001592:Benzyl Alcohols / Q000378:metabolism; D003653:Decarboxylation; D005658:Fungi / Q000201:enzymology*; D066298:In Vitro Techniques; D007700:Kinetics; D008031:Lignin / Q000378:metabolism*; D010070:Oxalates / Q000378:metabolism*; D019815:Oxalic Acid; D010544:Peroxidases / Q000378:metabolism*
D001592:Benzyl Alcohols; D010070:Oxalates; D008031:Lignin; D019815:Oxalic Acid; D010544:Peroxidases; C042197:veratryl alcohol