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首页> 外文期刊>Biochemistry >ORIGIN OF CARBOHYDRATE RECOGNITION SPECIFICITY OF HUMAN LYSOZYME REVEALED BY AFFINITY LABELING
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ORIGIN OF CARBOHYDRATE RECOGNITION SPECIFICITY OF HUMAN LYSOZYME REVEALED BY AFFINITY LABELING

机译：亲和力标签揭示的人类溶菌酶的碳水化合物识别特异性起源

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Ln order to reveal the origin of carbohydrate recognition specificity of human lysozyme by clarifying the difference in the binding mode of ligands in the active site, the inactivation of human lysozyme by 2',3'-epoxypropyl beta-glycoside derivatives of the disaccharides, N,N'-diacetylchitobiose [GlcNAc-beta-(1-->4)-GlcNAc] and N-acetyllactosamine [Gal-beta-(1-->4)-GlcNAc], was investigated and the three-dimensional structures of the affinity-labeled enzymes were determined by X-ray crystallography at 1.7 Angstrom resolution. Under the conditions comprising 2.0 x 10(-3) M labeling reagent and 1.0 x 10(-5) M human lysozyme at pH 5.4, 37 degrees C, the reaction time required to reduce the lytic activity against Micrococcus luteus cells to 50% of its initial activity was lengthened by 3.7 times through the substitution of the nonreducing end sugar residue, GlcNAc to Gal. The refined structure of human lysozyme labeled by 2',3'-epoxypropyl beta-glycoside derivatives of N,N'-diacetylchitobiose (HL/NAG-NAG-EPO complex) indicated that the interaction mode of the N,N-diacetylchitobiose moiety in substites B and C in this study was essentially the same as in the case of the complex of human lysozyme with the free ligand. On the other hand, the hydrogen-bonding pattern acid the stacking interaction at subsite B were remarkably different between the HL/NAG-NAG-EPO complex and human lysozyme labeled by the 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine (HL/GAL-NAG-EPO complex). The reduced number of possible hydrogen bonds as well as the less favorable stacking between the side chain of Tyr63 in human lysozyme and the galactose residue in the HL/GAL-NAG-EPO complex reasonably explained the less efficient ability of the 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine as compared to that of N,N'-diacetylchitobiose as an affinity labeling reagent toward human lysozyme.
机译：Ln为了阐明人溶菌酶对碳水化合物的识别特异性的起源，是通过阐明活性位点中配体的结合方式的差异，二糖的2'，3'-环氧丙基β-糖苷衍生物对人溶菌酶的失活，N ，N'-二乙酰壳聚糖二糖[GlcNAc-β-（1-> 4）-GlcNAc]和N-乙酰基乳糖胺[Gal-β-（1-> 4）-GlcNAc]进行了研究，其三维结构亲和标记的酶是通过X射线晶体学在1.7埃分辨率下确定的。在pH值为5.4、37摄氏度，包含2.0 x 10（-3）M标记试剂和1.0 x 10（-5）M人类溶菌酶的条件下，将针对微球菌的裂解活性降低至50％的黄腐球菌所需的反应时间通过将非还原性末端糖残基GlcNAc替换为Gal，其初始活性延长了3.7倍。 N，N'-二乙酰基壳二糖（HL / NAG-NAG-EPO配合物）的2'，3'-环氧丙基β-糖苷衍生物标记的人溶菌酶的精制结构表明，N，N'-二乙酰基壳二糖部分的相互作用模式为这项研究中的B和C取代基基本上与人溶菌酶与游离配体的复合物相同。另一方面，HL / NAG-NAG-EPO配合物与被N-乙酰基乳糖胺的2'，3'-环氧丙基β-糖苷标记的人溶菌酶之间的氢键结合酸在B位点的堆积相互作用显着不同。 （HL / GAL-NAG-EPO复合物）。可能的氢键数量减少以及人溶菌酶中Tyr63的侧链与HL / GAL-NAG-EPO复合物中的半乳糖残基之间的堆叠性降低，这可以合理地解释2'，3'的低效能力与N，N'-二乙酰基壳二糖相比，N-乙酰基乳糖胺的-环氧丙基β-糖苷作为对人溶菌酶的亲和标记试剂。

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