Kinetic Analysis of the Noncompetitive Inhibition of the Lignin-Peroxidase-catalyzed Reaction by Oxalic Acid.

DOI Web Site 被引用文献1件 参考文献1件

この論文をさがす

抄録

Oxalic acid was found to inhibit noncompetitively the Cα-Cβ bond cleavage of veratrylglycerol catalyzed by a lignin peroxidase (LiP) isozyme of the white-rot fungus P.chrysosporium. With greater amounts of oxalic acid in the LiP system, the substrate was not converted to veratraldehyde but was almost all recovered. Oxalic acid was shown to be decomposed to CO2 during the enzymatic reaction. The results clearly indicate that oxalic acid reduced the cation radical intermediate formed in the reaction back to the substrate to block the production of veratraldehyde. A novel equation has been derived to explain the mechanism for this unique non-competitive inhibition that is different from the classical noncompetitive one. The inhibition constant Ki obtained here, which is different from the classical inhibition constant Ki, is defined as the ratio of the rate constant (Kp) for product formation to the rate constant (Ki) for the reduction of the cation radical to the substrate.

収録刊行物

被引用文献 (1)*注記

もっと見る

参考文献 (1)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ