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首页> 外文期刊>Biochemistry >STEREOCHEMISTRY OF CHITIN HYDROLYSIS BY A PLANT CHITINASE LYSOZYME AND X-RAY STRUCTURE OF A COMPLEX WITH ALLOSAMIDIN - EVIDENCE FOR SUBSTRATE ASSISTED CATALYSIS
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STEREOCHEMISTRY OF CHITIN HYDROLYSIS BY A PLANT CHITINASE LYSOZYME AND X-RAY STRUCTURE OF A COMPLEX WITH ALLOSAMIDIN - EVIDENCE FOR SUBSTRATE ASSISTED CATALYSIS

机译：植物几丁质酶溶菌酶对几丁质水解的立体化学和具有异源沙丁胺的复合物的X射线结构-基质辅助催化的证据

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摘要

The plant enzyme hevamine has both chitinase and lysozyme activity. HPLC analysis of the products of the hydrolysis of chitopentaose shows that hevamine acts with retention of the configuration, despite the absence of a nucleophilic or stabilizing carboxylate. To analyze the stabilization of a putative oxocarbonium ion intermediate, the X-ray structure of hevamine complexed with the inhibitor allosamidin was determined at 1.85 Angstrom resolution. This structure supports the role of Glu127 as a proton donor. The allosamizoline group binds in the center of the active site, mimicking a reaction intermediate in which a positive charge at Cl is stabilized intramolecularly by the carbonyl oxygen of the N-acetyl group at C2.
机译：植物酶七胺具有几丁质酶和溶菌酶的活性。壳多糖的水解产物的HPLC分析表明，尽管不存在亲核或稳定的羧酸盐，但七胺仍保留构型。为了分析推定的氧碳鎓离子中间体的稳定性，在1.85埃的分辨率下测定了与抑制剂异蒜素结合的七胺的X射线结构。这种结构支持Glu127作为质子供体的作用。别甲唑啉基团结合在活性位点的中心，模仿了反应中间体，其中C1上的正电荷通过C2处N-乙酰基的羰基氧分子内稳定。

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