Jönsson L, Becker H G, Nyman P O
Chemical Center, University of Lund, Sweden.
Biochim Biophys Acta. 1994 Aug 17;1207(2):255-9. doi: 10.1016/0167-4838(94)00083-2.
The wood-decaying fungus Trametes versicolor secretes a large number of peroxidase isozymes, presumed to partake in the degradation of lignin. From enzymic studies, two types of peroxidases have been distinguished: lignin peroxidases and manganese peroxidases. We here report the finding of a T. versicolor peroxidase gene, PG V, which displays several features not observed in previously studied peroxidase genes from white-rot fungi, such as a high number of introns (12). Eight of the 12 introns have positions equivalent to introns of peroxidase genes from another white-rot fungus, Phanerochaete chrysosporium. The gene structure of PG V appears to be primarily related to known lignin peroxidase genes, while the encoded mature 339-residue protein has several characteristics in common with manganese peroxidases. Analyses further indicate that PG V encodes a Ser instead of an Asn at a position regarded as invariant within the enzyme superfamily, with the side chain involved in hydrogen bonding with the distal His.
木腐真菌云芝分泌大量过氧化物酶同工酶，推测其参与木质素的降解。通过酶学研究，已区分出两种类型的过氧化物酶：木质素过氧化物酶和锰过氧化物酶。我们在此报告发现了云芝过氧化物酶基因PG V，它具有一些在先前研究的白腐真菌过氧化物酶基因中未观察到的特征，例如内含子数量众多（12个）。12个内含子中的8个与另一种白腐真菌黄孢原毛平革菌过氧化物酶基因的内含子位置相当。PG V的基因结构似乎主要与已知的木质素过氧化物酶基因相关，而编码的成熟339个残基的蛋白质具有一些与锰过氧化物酶相同的特征。进一步分析表明，PG V在酶超家族中一个被认为不变的位置编码的是丝氨酸而非天冬酰胺，其侧链参与与远端组氨酸的氢键形成。
