Discovery of a cyclic phosphodiesterase that catalyzes the sequential hydrolysis of both ester bonds to phosphorus.
Discovery of a cyclic phosphodiesterase that catalyzes the sequential hydrolysis of both ester bonds to phosphorus.
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DOI：
10.1021/ja409376k
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发表时间：
2013-11-06
影响因子：
15
通讯作者：
Raushel FM
中科院分区：
文献类型：
--
作者：
Ghodge SV;Cummings JA;Williams HJ;Raushel FM
在磷酸盐饥饿条件下，细菌C-P裂解酶途径负责未激活的有机膦酸盐的代谢。自由基SAM酶PhnJ催化1-甲基磷酸-5-磷酸核糖中的C-P键裂解生成甲烷和5-磷酸-1,2-环磷酸（PRcP）。在大肠杆菌中，环磷酸产物被PhnP水解成核糖-1,5-二磷酸。在这项研究中，我们描述了一种酶的发现和表征，该酶可以将环磷酸二酯直接水解为邻二醇和无机磷酸盐。使用PRcP，这种酶水解核糖部分碳-1处的磷酸酯，形成核糖-2,5-二磷酸，然后这个中间体被水解成核糖-5-磷酸和无机磷酸。核糖-1,5-二磷酸既不是这种酶的中间产物，也不是底物。这种酶的同源物存在于人类病原体艰难梭状芽胞杆菌和长毛蛋菌中。我们建议将这种酶命名为环磷酸二氢酶（cPDH），并命名为PhnPP。
The bacterial C-P lyase pathway is responsible for the metabolism of unactivated organophosphonates under conditions of phosphate starvation. The cleavage of the C-P bond within ribose-1-methylphosphonate-5-phosphate to form methane and 5-phosphoribose-1,2-cyclic phosphate (PRcP) is catalyzed by the radical SAM enzyme PhnJ. In Escherichia coli the cyclic phosphate product is hydrolyzed to ribose-1,5-bisphosphate by PhnP. In this study, we describe the discovery and characterization of an enzyme that can hydrolyze a cyclic phosphodiester directly to a vicinal diol and inorganic phosphate. With PRcP, this enzyme hydrolyzes the phosphate ester at carbon-1 of the ribose moiety to form ribose-2,5-bisphosphate, and then this intermediate is hydrolyzed to ribose-5-phosphate and inorganic phosphate. Ribose-1,5-bisphosphate is neither an intermediate nor substrate for this enzyme. Orthologs of this enzyme are found in the human pathogens Clostridium difficile and Eggerthella lenta. We propose that this enzyme be called cyclic phosphate dihydrolase (cPDH) and be designated as PhnPP.
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