Raices M, Paifer E, Cremata J, Montesino R, Ståhlberg J, Divne C, Szabó I J, Henriksson G, Johansson G, Pettersson G
Centro de Ingeniéria Genética y Biotecnologia, Havana, Cuba.
FEBS Lett. 1995 Aug 7;369(2-3):233-8. doi: 10.1016/0014-5793(95)00758-2.
The cDNA of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium has been cloned and sequenced. The 5' end was obtained by PCR amplification. The cDNA contains 2310 translated bases excluding the poly(A) tail. The deduced mature protein contains 770 amino acid residues and is preceded by a 18 residue long signal peptide. The regions of the amino acid sequence corresponding to the heme and FAD domains of CDH were identified as well as the nucleotide-binding motif, the disulfide pairing and a methionine residue chelating the heme iron. No homologous sequences were found for the heme domain, however, the FAD domain appears to be distantly related to the GMC oxidoreductase family.
已克隆并测序了来自黄孢原毛平革菌的纤维二糖脱氢酶(CDH)的cDNA。其5'端通过PCR扩增获得。该cDNA包含2310个可翻译碱基,不包括聚腺苷酸尾。推导的成熟蛋白含有770个氨基酸残基,前面有一个18个残基长的信号肽。确定了与CDH的血红素和FAD结构域相对应的氨基酸序列区域,以及核苷酸结合基序、二硫键配对和一个螯合血红素铁的甲硫氨酸残基。在血红素结构域未发现同源序列,然而,FAD结构域似乎与GMC氧化还原酶家族有远缘关系。