<Note>Kinetic Analysis of the Noncompetitive Inhibition of Lignin Peroxidase by Cellobiose : Quinone Oxidoreductase

この論文は国立情報学研究所の学術雑誌公開支援事業により電子化されました。The steady-state kinetics of the redox interaction between lignin peroxidase (LiP) and cellobiose: quinone oxidoreductase (CBQ) was analyzed. To explain the unique noncompetitive inhibition of LiP by CBQ, a scheme was proposed with a novel equation derived. The inhibition constant here differs from that occurring in the equation for the inhibition of LiP by oxalic acid (OX), in that it involves more parameters

<Original>Lignin Peroxidase-Catalyzed Oxidation of Monomeric Lignin Model Substrates

この論文は国立情報学研究所の学術雑誌公開支援事業により電子化されました。The substrate specificity of lignin peroxidase (LiP) was investigated by determining the K_ms and V_s of LiP for the four lignin model substrates of 3,4-dimethoxybenzyl alcohol (I), 3,4-dimethoxybenzyl glycerol (II), 3,4,5-trimethoxybenzyl alcohol (III), and 3, 4, 5-trimethoxybenzyl glycerol (IV). The K_ms (μM) and V_s (turnover number, sec^) of LiP were determined. The K_m/V_ values calculated to be 4.7, 18.2, 29.9, and 76.7 for I, II, III, and IV, respectively. Among the substrates tested, I (veratryl alcohol), which is a secondary metabolite of white-rot fungi, was found to be the best substrate for LiP