A new versatile peroxidase from Pleurotus.
A new versatile peroxidase from Pleurotus.
复制标题
来自侧耳属的新型多功能过氧化物酶。
DOI：
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发表时间：
2001
影响因子：
3.9
通讯作者：
Angel T. Martı́nez
中科院分区：
文献类型：
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作者：
F. J. Ruiz;S. Camarero;Marta Pérez;M. Martínez;Angel T. Martı́nez
对黄孢原毛平革菌的木质素过氧化物酶(LIP)和锰过氧化物酶(MNP)进行了研究。第三种木质素分解过氧化物酶已在侧耳和侧耳中被描述。其中两种多功能过氧化物酶(VPs)已被克隆、测序和鉴定。它们对Mn(2+)、对苯二酚和染料有很高的亲和力，也能氧化藜芦醇、二甲氧基苯和木质素二聚体。所推导的序列与黄孢链霉菌LIP的同源性高于与MNP的同源性，但所得到的分子模型包含了一个Mn(2+)结合部位。关于芳香族底物的氧化，Pl。Eryngii VP显示了一条假定的从暴露的酪氨酸到血红素的远程电子转移途径。该色氨酸和形成Mn(2+)结合部位的酸性残基的诱变和化学修饰证实了它们在催化中的作用。生化证据进一步支持了几个底物氧化点的存在。讨论了在其他真菌过氧化物酶中的残基保守。
Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanerochaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn(2+), hydroquinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and lignin dimers. The deduced sequences show higher identity with Ph. chrysosporium LiP than MnP, but the molecular models obtained include a Mn(2+)-binding site. Concerning aromatic substrate oxidation, Pl. eryngii VP shows a putative long-range electron transfer pathway from an exposed trytophan to haem. Mutagenesis and chemical modification of this tryptophan and the acidic residues forming the Mn(2+)-binding site confirmed their role in catalysis. The existence of several substrate oxidation sites is supported further by biochemical evidence. Residue conservation in other fungal peroxidases is discussed.