Morya V K, Yadav Virendra K, Yadav Sangeeta, Yadav Dinesh
Department of Biological Engineering, Inha University, Incheon, 42-751, Republic of Korea.
Department of Molecular and Cellular Engineering, SHIATS, Allahabad, India.
Cell Biochem Biophys. 2016 Sep;74(3):327-35. doi: 10.1007/s12013-016-0750-9. Epub 2016 Jun 29.
A total of 129 proteases sequences comprising 43 serine proteases, 36 aspartic proteases, 24 cysteine protease, 21 metalloproteases, and 05 neutral proteases from different Aspergillus species were analyzed for the catalytically active site residues using MEROPS database and various bioinformatics tools. Different proteases have predominance of variable active site residues. In case of 24 cysteine proteases of Aspergilli, the predominant active site residues observed were Gln193, Cys199, His364, Asn384 while for 43 serine proteases, the active site residues namely Asp164, His193, Asn284, Ser349 and Asp325, His357, Asn454, Ser519 were frequently observed. The analysis of 21 metalloproteases of Aspergilli revealed Glu298 and Glu388, Tyr476 as predominant active site residues. In general, Aspergilli species-specific active site residues were observed for different types of protease sequences analyzed. The phylogenetic analysis of these 129 proteases sequences revealed 14 different clans representing different types of proteases with diverse active site residues.
使用MEROPS数据库和各种生物信息学工具，对来自不同曲霉属物种的总共129个蛋白酶序列进行了分析，这些序列包括43个丝氨酸蛋白酶、36个天冬氨酸蛋白酶、24个半胱氨酸蛋白酶、21个金属蛋白酶和5个中性蛋白酶，以确定其催化活性位点残基。不同的蛋白酶具有不同的活性位点残基优势。在曲霉属的24个半胱氨酸蛋白酶中，观察到的主要活性位点残基是Gln193、Cys199、His364、Asn384；而对于43个丝氨酸蛋白酶，经常观察到的活性位点残基分别是Asp164、His193、Asn284、Ser349以及Asp325、His357、Asn454、Ser519。对曲霉属的21个金属蛋白酶的分析表明，Glu298、Glu388、Tyr476是主要的活性位点残基。总体而言，在所分析的不同类型蛋白酶序列中观察到了曲霉属物种特异性的活性位点残基。对这129个蛋白酶序列的系统发育分析揭示了14个不同的家族，它们代表了具有不同活性位点残基的不同类型蛋白酶。
