一种新型细胞外过氧化物酶的证据。来自白腐真菌Bjerkandera sp. BOS 55的锰抑制过氧化物酶。
Evidence for a new extracellular peroxidase. Manganese-inhibited peroxidase from the white-rot fungus Bjerkandera sp. BOS 55.
作者信息
de Jong E, Field J A, de Bont J A
机构信息
Department of Food Science, Agricultural University Wageningen, The Netherlands.
出版信息
FEBS Lett. 1992 Mar 24;299(1):107-10. doi: 10.1016/0014-5793(92)80111-s.
A novel enzyme activity was detected in the extracellular fluid of Bjerkandera sp. BOS 55. The purified enzyme could oxidize several compounds, such as Phenol red, 2,6-dimethoxyphenol (DMP), Poly R-478, ABTS and guaiacol, with H2O2 as an electron acceptor. In contrast, veratryl alcohol was not a substrate. This enzyme also had the capacity to oxidize DMP in the absence of H2O2. With some substrates, a strong inhibition of the peroxidative activity by Mn2+ was observed. Phenol red oxidation was inhibited by 84% with only 1 mM of this metal ion. Because DMP oxidation by this enzyme is only slightly inhibited by Mn2+, this substrate should not be used in assays to detect manganese peroxidase. The enzyme is tentatively named 'Manganese-Inhibited Peroxidase'.
在白腐菌Bjerkandera sp. BOS 55的细胞外液中检测到一种新的酶活性。纯化后的酶能够以过氧化氢作为电子受体，氧化多种化合物，如酚红、2,6-二甲氧基苯酚（DMP）、聚R-478、ABTS和愈创木酚。相比之下，藜芦醇不是该酶的底物。这种酶在没有过氧化氢的情况下也具有氧化DMP的能力。对于某些底物，观察到锰离子对其过氧化物活性有强烈抑制作用。仅1 mM这种金属离子就能使酚红氧化受到84%的抑制。由于该酶对DMP的氧化仅受到锰离子的轻微抑制，因此在检测锰过氧化物酶的测定中不应使用此底物。该酶暂命名为“锰抑制过氧化物酶”。
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