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首页> 外文期刊>Biochemistry >Sbi00515, a Protein of Unknown Function from Streptomyces bingchenggensis, Highlights the Functional Versatility of the Acetoacetate Decarboxylase Scaffold
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Sbi00515, a Protein of Unknown Function from Streptomyces bingchenggensis, Highlights the Functional Versatility of the Acetoacetate Decarboxylase Scaffold

机译：Sbi00515，宾城链霉菌功能未知的蛋白质，突出了乙酰乙酸脱羧酶支架的功能多功能性

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摘要

The acetoacetate decarboxylase-like superfamily (ADCSF) is a group of similar to 4000 enzymes that, until recently, was thought to be homogeneous in terms of the reaction catalyzed. Bioinformatic analysis shows that the ADCSF consists of up to seven families that differ primarily in their active site architectures. The soil-dwelling bacterium Streptomyces bingchenggensis BCW-1 produces an ADCSF enzyme of unknown function that shares a low level of sequence identity (similar to 20%) with known acetoacetate decarboxylases (ADCs). This enzyme, Sbi00.515, belongs to the MppR-like family of the ADCSF because of its similarity to the mannopeptimycin biosynthetic protein MppR from Streptomyces hygroscopicus. Herein, we present steady state kinetic data that show Sbi00515 does not catalyze the decarboxylation of any alpha- or beta-keto acid tested. Rather, we show that Sbi00515 catalyzes the condensation of pyruvate with a number of aldehydes, followed by dehydration of the presumed aldol intermediate: Thus, Sbi00515 is a pyruvate aldolase-dehydratase and not an acetoacetate decarboxylase. We have also determined the X-ray crystal structures of Sbi00515 in complexes with formate and pyruvate. The structures show that the overall fold of Sbi00515 is nearly identical to those of both ADC and MppR The pyruvate complex is trapped as the Schiff base, providing evidence that the Schiff base chemistry that drives the acetoacetate decarboxylases has been co-opted to perform a new function, and that this core chemistry may be conserved across the superfamily. The structures also suggest possible catalytic roles for several active site residues.
机译：乙酰乙酸脱羧酶样超家族（ADCSF）是类似于4000种酶的组，直到最近，就催化的反应而言，它们被认为是均相的。生物信息学分析表明，ADCSF由多达七个家族组成，这些家族的主要区别在于其活动站点架构。土壤寄居细菌炳城链霉菌BCW-1产生一种功能未知的ADCSF酶，该酶与已知的乙酰乙酸脱羧酶（ADC）共有低水平的序列同一性（约20％）。该酶Sbi00.515属于ADCSF的MppR样家族，因为它与来自吸水链霉菌的甘露肽霉素生物合成蛋白MppR相似。本文中，我们提供的稳态动力学数据表明Sbi00515不会催化任何测试的α-或β-酮酸的脱羧反应。相反，我们表明Sbi00515催化丙酮酸与许多醛的缩合，然后使假定的羟醛中间产物脱水：因此，Sbi00515是一种丙酮酸醛缩酶脱水酶，而不是乙酰乙酸酯脱羧酶。我们还确定了Sbi00515与甲酸和丙酮酸的配合物的X射线晶体结构。结构表明，Sbi00515的总体折叠几乎与ADC和MppR相同。丙酮酸酯络合物被捕获为席夫碱，提供了证据表明驱动乙酰乙酸脱羧酶的席夫碱化学已被共同选择用于执行新的功能，并且这种核心化学物质可能在整个超家族中得以保留。该结构还暗示了几个活性位点残基的可能催化作用。

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