Structural highlights
Function
[PDE1_YEAST] Controls the level of cAMP in yeast cells, together with the high-affinity cAMP phosphodiesterase (PDE2).
Publication Abstract from PubMed
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 muM and a kcat of 16.9 s(-1) for cAMP and a KM of 105 muM 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 A 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-beta-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.
Dual specificity and novel structural folding of yeast phosphodiesterase-1 for hydrolysis of second messengers cyclic adenosine and guanosine 3',5'-monophosphate.,Tian Y, Cui W, Huang M, Robinson H, Wan Y, Wang Y, Ke H Biochemistry. 2014 Aug 5;53(30):4938-45. doi: 10.1021/bi500406h. Epub 2014 Jul, 22. PMID:25050706[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tian Y, Cui W, Huang M, Robinson H, Wan Y, Wang Y, Ke H. Dual specificity and novel structural folding of yeast phosphodiesterase-1 for hydrolysis of second messengers cyclic adenosine and guanosine 3',5'-monophosphate. Biochemistry. 2014 Aug 5;53(30):4938-45. doi: 10.1021/bi500406h. Epub 2014 Jul, 22. PMID:25050706 doi:http://dx.doi.org/10.1021/bi500406h
