酵母磷酸二酯酶-1 水解第二信使环腺苷酸和鸟苷 3',5'-环单磷酸的双重特异性和新颖结构折叠。
Dual specificity and novel structural folding of yeast phosphodiesterase-1 for hydrolysis of second messengers cyclic adenosine and guanosine 3',5'-monophosphate.
机构信息
Beijing Laboratory for Food Quality and Safety and Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University , Beijing 100048, P. R. China.
出版信息
Biochemistry. 2014 Aug 5;53(30):4938-45. doi: 10.1021/bi500406h. Epub 2014 Jul 22.
Cyclic nucleotide phosphodiesterases (PDEs) decompose second messengers cAMP and cGMP that play critical roles in many physiological processes. PDE1 of Saccharomyces cerevisiae has been subcloned and expressed in Escherichia coli. Recombinant yPDE1 has a KM of 110 μM and a kcat of 16.9 s(-1) for cAMP and a KM of 105 μM and a kcat of 11.8 s(-1) for cGMP. Thus, the specificity constant (kcat/KM(cAMP))/(kcat/KM(cGMP)) of 1.4 indicates a dual specificity of yPDE1 for hydrolysis of both cAMP and cGMP. The crystal structures of unliganded yPDE1 and its complex with GMP at 1.31 Å resolution reveal a new structural folding that is different from those of human PDEs but is partially similar to that of some other metalloenzymes such as metallo-β-lactamase. In spite of their different structures and divalent metals, yPDE1 and human PDEs may share a common mechanism for hydrolysis of cAMP and cGMP.
环核苷酸磷酸二酯酶（PDEs）分解第二信使 cAMP 和 cGMP，它们在许多生理过程中发挥着关键作用。酿酒酵母的 PDE1 已被亚克隆并在大肠杆菌中表达。重组 yPDE1 对 cAMP 的 KM 为 110 μM，kcat 为 16.9 s(-1)，对 cGMP 的 KM 为 105 μM，kcat 为 11.8 s(-1)。因此，特异性常数（kcat/KM(cAMP))/(kcat/KM(cGMP))为 1.4，表明 yPDE1 对 cAMP 和 cGMP 的水解具有双重特异性。未配体结合的 yPDE1 及其与 GMP 的复合物的晶体结构在 1.31 Å 分辨率下揭示了一种新的结构折叠，与人类 PDEs 的结构折叠不同，但与一些其他金属酶（如金属β-内酰胺酶）的结构折叠部分相似。尽管它们的结构和二价金属不同，但 yPDE1 和人类 PDEs 可能共享 cAMP 和 cGMP 水解的共同机制。
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