The specificity of prolyl endopeptidase from Flavobacterium meningoseptum:: Mapping the S′ subsites by positional scanning via acyl transfer
The specificity of prolyl endopeptidase from Flavobacterium meningoseptum:: Mapping the S′ subsites by positional scanning via acyl transfer
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DOI：
10.1016/s0968-0896(98)00145-x
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发表时间：
1998-10-01
影响因子：
3.5
通讯作者：
Jakubke, HD
中科院分区：
文献类型：
--
作者：
Bordusa, F;Jakubke, HD
用酰基转移法研究了脑膜隔膜黄杆菌脯氨酰内肽酶的S-1 '-S-3'亚位点特异性。而S-1'和S-3'亚位点对氨基组分的特异性的影响约为一个数量级，S-2'亚位点具有明显更高的特异性。除了对P-1 ′-P-3 ′上的疏水残基具有高度特异性外，脯氨酸还能有效地与酶的S-2 ′和S-3 ′亚位点结合。相反，没有观察到含P-1'脯氨酸的肽的结合。可以证明S'亚位点的特异性不限于L-氨基酸。还发现β-和γ-氨基酸的有效P '-S'相互作用，表明该酶不与P-1'和P-2'氨基酸残基的骨架形成紧密接触。(C)1998爱思唯尔科技有限公司版权所有。
The S-1'-S-3' subsite specificity of prolyl endopeptidase from Flavobacterium meningoseptum was studied by acyl transfer to libraries of amino acid amides and peptides. Whereas the S-1' and S-3' subsites influence the specificity for the amino component by approximately one order of magnitude, the S-2' subsite possesses a markedly higher specificity. Besides the high specificity for hydrophobic residues at P-1'-P-3', proline was efficiently bound by the S-2' and S-3' subsites of the enzyme. In contrast, no binding of P-1' proline-containing peptides was observed. It could be demonstrated that the specificity of the S' subsite is not restricted to L-amino acids. Effective P'-S' interactions were also found for beta- and gamma-amino acids indicating that the enzyme does not form close contacts to the backbone of P-1' and P-2' amino acid residues. (C) 1998 Elsevier Science Ltd. All rights reserved.