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首页> 外文期刊>Biochemistry >Characterization of the Monomer-Dimmer Equilibrium of Human Cytomegalovirus Protease by Kinetic Methods
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Characterization of the Monomer-Dimmer Equilibrium of Human Cytomegalovirus Protease by Kinetic Methods

机译：动力学方法表征人巨细胞病毒蛋白酶的单体-二聚体平衡

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摘要

Herpesviruses encode a serine protease that is essential for the maturation of infectious virions.This protease has a unique polypeptide backbone fold and contains a novel Ser-His-His catalytic triad.It exists in a monomer-dimer equilibrium in solution,but only the dimer form of the enzyme is catalytically active.The stability of this dimmer is affected by the presence of anti-chaotropic agents.Most of the reported Kd values for this dimer (between 0.6 and 6muM) are inconsistent with the fact that the protease is routinely assayed at 20-50 nM concentrations,as only monomeric species would be expected with such K_d values.We have characterized the monomer-dimer equilibrium of HCMV protease using a new method,which observes the exchange between dimmers of the wild-type enzyme and the active-site Ser132Ala mutant in a titration experiment.The K_d of the dimmer was determined to be 8 muM and 31 nM in the absence or presence of anti-chaotropic agents (10% glycerol and 0.5 M Na_2SO_4),respectively.Detailed kinetic analysis also showed that,in addition to the 260-fold stabilization of the dimmer,the anti-chaotropic agents produced a 7-fold enhancement in the catalytic activity of the dimmer.
机译：疱疹病毒编码一种丝氨酸蛋白酶，对感染性病毒粒子的成熟至关重要。这种蛋白酶具有独特的多肽骨架折叠，并含有新型的Ser-His-His催化三联体。它以单体-二聚体的平衡存在于溶液中，但只有二聚体该酶的形式具有催化活性。该二聚体的稳定性受抗离液剂的影响。该二聚体的大多数报道的Kd值（0.6至6μM之间）与常规检测该蛋白酶的事实不一致在20-50 nM的浓度下，因为只有单体物种才具有这样的K_d值。滴定实验中的Ser132Ala突变位点。在不存在或存在抗离液剂（10％甘油和0.5 M Na_2SO_4）的情况下，确定二聚体的K_d为8μM和31 nM详细的动力学分析还表明，除了调光器具有260倍的稳定性外，抗离液剂还使调光器的催化活性提高了7倍。

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