ISOZYMES OF LIGNIN PEROXIDASE AND MANGANESE(II) PEROXIDASE FROM THE WHITE-ROT BASIDIOMYCETE TRAMETES-VERSICOLOR .2. PARTIAL SEQUENCES, PEPTIDE MAPS, AND AMINO-ACID AND CARBOHYDRATE COMPOSITIONS
ISOZYMES OF LIGNIN PEROXIDASE AND MANGANESE(II) PEROXIDASE FROM THE WHITE-ROT BASIDIOMYCETE TRAMETES-VERSICOLOR .2. PARTIAL SEQUENCES, PEPTIDE MAPS, AND AMINO-ACID AND CARBOHYDRATE COMPOSITIONS
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DOI：
10.1006/abbi.1993.1008
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发表时间：
1993-01-01
影响因子：
3.9
通讯作者：
NYMAN, PO
中科院分区：
文献类型：
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作者：
JOHANSSON, T;WELINDER, KG;NYMAN, PO
担子菌 Trametes versicolor 是一种白腐真菌和木质素的有效降解剂，可产生多种形式的细胞外过氧化物酶。其中九种形式，即六种木质素过氧化物酶和三种锰 (II) 过氧化物酶，按照前一篇论文中所述进行纯化，并通过氨基末端测序、氨基酸分析、碳水化合物分析或肽图谱进行了表征。对于两种木质素过氧化物酶形式，胰蛋白酶肽被分离并测序至分别对应于一级结构的约40%和30%的程度。研究发现，九种过氧化物酶中有八种具有独特的氨基末端区域。序列比较显示 57% 的残基相同，表明木质素过氧化物酶和锰 (II) 过氧化物酶具有共同的祖先。五种木质素过氧化物酶之间的同一性约为80%，三种锰(II)过氧化物酶之间的同一性约为70%。序列的成对比较揭示了一些木质素过氧化物酶非常密切相关，或者相同或者仅在所研究的三十五个木质素过氧化物酶中的单个氨基酸残基上不同。这些密切关系也得到肽图谱和氨基酸组成相似性的支持。所有同工酶中均不存在酪氨酸。木质素和锰(II)过氧化物酶显示存在葡萄糖胺和甘露糖，其量相当于蛋白质分子质量的3%至6%。碳水化合物组合物与1、2和3个N-糖基化位点的存在相容。获得的结果强烈表明真菌所表现出的过氧化物酶模式的复杂性（T. Johansson 和 P.O. Nyman,Arch. Biochem. Biophys.300, 49-56, 1993）在很大程度上可以通过基因水平的异质性来解释，可能以多个结构基因的形式。最近发表的两个来自 T 基因组克隆的基因。 versicolor 与此处表征的两种木质素过氧化物酶的序列相同。
The basidiomyceteTrametes versicolor, a white-rot fungus and potent degrader of lignin, produces multiple forms of extracellular peroxidases. Nine of these forms, six lignin peroxidases and three manganese(II) peroxidases, purified as described in the preceding paper, were characterized by amino-terminal sequencing, amino acid analyses, carbohydrate analyses, or peptide mapping. For two of the lignin peroxidase forms, tryptic peptides were isolated and sequenced to an extent corresponding to about 40 and 30%, respectively, of the primary structure. Eight of the nine peroxidases investigated were found to possess unique amino-terminal regions. A comparison of the sequences shows 57% of the residues to be identical, indicating a common ancestry for the lignin peroxidase and the manganese(II) peroxidase. The degree of identity among the five lignin peroxidases is about 80% and among the three manganese(II) peroxidases about 70%. Pairwise comparisons of the sequences disclosed that some of the lignin peroxidases are very closely related, either identical or differing only in a single amino acid residue of the thirty-five investigated. These close relationships are also supported by peptide mapping and by similarities in amino acid compositions. Tyr is absent in all isozymes. Lignin and manganese(II) peroxidases showed the presence of glucosamine and mannose in an amount corresponding to 3 to 6% of the molecular mass of the proteins. The carbohydrate compositions are compatible with the presence of 1, 2, and 3 sites of N-glycosylation. The results obtained strongly suggest that the complexity in the peroxidase pattern displayed by the fungus (T. Johansson and P.O. Nyman,Arch. Biochem. Biophys.300, 49-56, 1993) can largely be accounted for by a heterogeneity at the gene level, probably in the form of multiple structural genes. Two recently published genes from genomic clones ofT. versicolorare identical in sequence to two of the lignin peroxidases characterized here.