钙对粗糙脉孢菌中一种热稳定的环核苷酸磷酸二酯酶的抑制作用。
Calcium inhibition of a heat-stable cyclic nucleotide phosphodiesterase from Neurospora crassa.
作者信息
Shaw N M, Harding R W
出版信息
FEBS Lett. 1983 Feb 21;152(2):295-9. doi: 10.1016/0014-5793(83)80399-8.
Neurospora crassa had a heat-stable (up to 95 degrees C), soluble cyclic nucleotide phosphodiesterase (PDE). Both unheated and heat-stable PDE activities were inhibited by micromolar concentrations of Ca2+. This inhibition was reversed by EGTA or EDTA in molar excess of the Ca2+ concentration. Calmodulin was not involved in the Ca2+ inhibition, nor was Ca2+ inhibition of the heat-stable PDE due to cleavage inactivation of the enzyme by a Ca2+-stimulated protease. In addition to Ca2+, several other cations inhibited the activity of the heat-stable enzyme. Cyclic AMP and cGMP, but not 2'3' cAMP were substrates for both unheated and heat-stable PDEs. This is the first report of a PDE which is inhibited by micromolar concentrations of Ca2+.
粗糙脉孢菌有一种热稳定（高达95摄氏度）的可溶性环核苷酸磷酸二酯酶（PDE）。未加热和热稳定的PDE活性均受到微摩尔浓度的Ca2+抑制。这种抑制作用可被摩尔浓度超过Ca2+浓度的EGTA或EDTA逆转。钙调蛋白不参与Ca2+抑制作用，热稳定PDE的Ca2+抑制作用也不是由于Ca2+刺激的蛋白酶对该酶的切割失活所致。除Ca2+外，其他几种阳离子也抑制热稳定酶的活性。环磷酸腺苷（cAMP）和环磷酸鸟苷（cGMP）是未加热和热稳定PDE的底物，但2',3'-环磷酸腺苷不是。这是关于一种受微摩尔浓度Ca2+抑制的PDE的首次报道。
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