Karthik L, Nachiappan M, Velmurugan D, Jeyakanthan J, Gunasekaran K
CAS in Crystallography and Biophysics, University of Madras, Maraimalai Campus, Chennai, 600 025, Tamil Nadu, India.
J Struct Funct Genomics. 2013 Jun;14(2):59-70. doi: 10.1007/s10969-013-9156-8. Epub 2013 Jun 7.
Fuculose phosphate aldolase catalyzes the reversible cleavage of fuculose-1-phosphate to dihydroxyacetone phosphate and L-lactaldehyde. A tetramer by nature, this enzyme from Thermus thermophilus HB8 represents the group of Class II aldolases. The structure was solved in two different space groups using the crystals obtained from slow evaporation vapour-diffusion and microbatch techniques. The detailed crystallization description has been reported previously. In this study, the structural features of fuculose phosphate aldolase from T. thermophilus have been explored extensively through sequence and structure comparisons with fuculose phosphate aldolases of different species. Finally, an in silico analysis using induced fit docking was attempted to deduce the binding mode of fuculose phosphate aldolase with its natural substrate fuculose-1-phosphate along with a substrate analog dihydroxyacetone phosphate and phosphoglycolohydroxymate--a potential aldolase inhibitor. The results show the mechanism of action may be similar to that of Escherichia coli fuculose aldolase.
岩藻糖磷酸醛缩酶催化1-磷酸岩藻糖可逆地裂解为磷酸二羟丙酮和L-乳醛。这种来自嗜热栖热菌HB8的酶本质上是一种四聚体，属于II类醛缩酶。利用通过缓慢蒸发气相扩散和微量分批技术获得的晶体，在两种不同的空间群中解析了其结构。详细的结晶描述先前已有报道。在本研究中，通过与不同物种的岩藻糖磷酸醛缩酶进行序列和结构比较，广泛探索了嗜热栖热菌岩藻糖磷酸醛缩酶的结构特征。最后，尝试使用诱导契合对接进行计算机模拟分析，以推断岩藻糖磷酸醛缩酶与其天然底物1-磷酸岩藻糖以及底物类似物磷酸二羟丙酮和磷酸乙醇酸羟肟酸（一种潜在的醛缩酶抑制剂）的结合模式。结果表明其作用机制可能与大肠杆菌岩藻糖醛缩酶相似。
