Alic M, Akileswaran L, Gold M H
Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000, USA.
Biochim Biophys Acta. 1997 Mar 7;1338(1):1-7. doi: 10.1016/s0167-4838(96)00235-x.
The gene encoding manganese peroxidase isozyme 3 (MnP3) from the white-rot basidiomycete Phanerochaete chrysosporium was cloned and sequenced. The mnp3 gene encodes a mature protein of 357 amino acids with a 25 amino-acid signal peptide. The amino acids involved in peroxidase function, as well as those forming the MnII binding site and those involved in disulfide bond formation, are conserved in the MnP3 sequence. The mnp3 gene has six introns, indicating that the sequenced P. chrysosporium mnp genes can be divided into three subfamilies on the basis of intron-exon structure. The mnp3 gene promoter contains putative metal response elements and heat shock elements which may be involved in the regulation of mnp gene transcription by Mn, the substrate for the enzyme, and by heat shock.
克隆并测序了来自白腐担子菌黄孢原毛平革菌的编码锰过氧化物酶同工酶3（MnP3）的基因。mnp3基因编码一个由357个氨基酸组成的成熟蛋白，并带有一个25个氨基酸的信号肽。在MnP3序列中，参与过氧化物酶功能的氨基酸、形成MnII结合位点的氨基酸以及参与二硫键形成的氨基酸都是保守的。mnp3基因有六个内含子，这表明根据内含子-外显子结构，已测序的黄孢原毛平革菌mnp基因可分为三个亚家族。mnp3基因启动子含有假定的金属反应元件和热休克元件，它们可能参与了该酶的底物锰以及热休克对mnp基因转录的调控。
