[Hybrid Mn-peroxidases from basidiomycetes: a review].
The Mn-peroxidase from the fungus Panus tigrinus 8/18 is a hybrid enzyme. It catalyzes both Mn2+-dependent and Mn2+-independent oxidation of organic substrates. The spectral properties of intermediates and the pathway of the catalytic cycle are typical of hybrid Mn-peroxidases. The enzyme catalyzes the "oxidase" reaction (NADH oxidation) without peroxide and with the presence of Mn2+, which takes part in hydrogen peroxide production via Mn3+ and preserves the enzyme from inactivation. With the presence of organic mediators, the hybrid Mn-peroxidase oxidizes nonphenolic compounds: aromatic alcohols and a nonphenolic lignin model compound. The degree of conversion of 2,4,6-trichlorophenol is higher with the presence of l-hydroxybenzotriazole.
A V
AV
Lisov
A A
AA
Leont'evskiĭ
L A
LA
Golovleva
D001487:Basidiomycota / Q000201:enzymology*; D002384:Catalysis; D002413:Cations, Divalent; D002733:Chlorophenols / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D008031:Lignin / Q000378:metabolism; D008345:Manganese / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D010544:Peroxidases / Q000378:metabolism*; D013379:Substrate Specificity; D014230:Triazoles / Q000378:metabolism
D002413:Cations, Divalent; D002733:Chlorophenols; D014230:Triazoles; D009243:NAD; D008345:Manganese; D008031:Lignin; C011852:1-hydroxybenzotriazole; D006861:Hydrogen Peroxide; D010544:Peroxidases; C051129:manganese peroxidase; C024564:2,4,6-trichlorophenol