Heinfling A, Martínez M J, Martínez A T, Bergbauer M, Szewzyk U
FG Microbial Ecology, Technical University Berlin, Germany.
FEMS Microbiol Lett. 1998 Aug 1;165(1):43-50. doi: 10.1111/j.1574-6968.1998.tb13125.x.
A peroxidase oxidizing Mn2+ (MnP) is described for the first time in Bjerkandera adusta, a fungus efficiently degrading xenobiotic compounds. The MnP appeared as two isoenzymes, which were purified to homogeneity together with two lignin peroxidases (LiP). Their N-terminal sequences were identical, but the MnP isoenzymes showed more basic isoelectric points and differences in amino acid composition and catalytic properties. The B. adusta LiP is similar to LiP from Phanerochaete chrysoporium. However, the interest of the MnP described here is related to its ability to catalyze Mn(2+)-mediated as well as Mn(2+)-independent reactions on aromatic compounds, which may be of use for applications in biotechnology and environmental technology.
首次在高效降解外源化合物的真菌烟管菌中描述了一种氧化Mn2+的过氧化物酶（MnP）。MnP表现为两种同工酶，它们与两种木质素过氧化物酶（LiP）一起被纯化至均一。它们的N端序列相同，但MnP同工酶显示出更多的碱性等电点以及氨基酸组成和催化特性的差异。烟管菌LiP与黄孢原毛平革菌的LiP相似。然而，这里描述的MnP的有趣之处在于其催化Mn(2+)介导的以及对芳香族化合物的非Mn(2+)依赖性反应的能力，这可能在生物技术和环境技术应用中有用。
