来自单核细胞增生李斯特菌的重组广谱磷脂酶C在酸性pH值下表现出最佳活性。
Recombinant broad-range phospholipase C from Listeria monocytogenes exhibits optimal activity at acidic pH.
作者信息
Huang Qiongying, Gershenson Anne, Roberts Mary F
机构信息
Department of Chemistry, Boston College, Chestnut Hill, MA, United States.
Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, United States.
出版信息
Biochim Biophys Acta. 2016 Jun;1864(6):697-705. doi: 10.1016/j.bbapap.2016.03.008. Epub 2016 Mar 11.
Abstract
The broad-range phospholipase C (PLC) from Listeria monocytogenes has been expressed using an intein expression system and characterized. This zinc metalloenzyme, similar to the homologous enzyme from Bacillus cereus, targets a wide range of lipid substrates. With monomeric substrates, the length of the hydrophobic acyl chain has significant impact on enzyme efficiency by affecting substrate affinity (Km). Based on a homology model of the enzyme to the B. cereus protein, several active site residue mutations were generated. While this PLC shares many of the mechanistic characteristics of the B. cereus PLC, a major difference is that the L. monocytogenes enzyme displays an acidic pH optimum regardless of substrate status (monomer, micelle, or vesicle). This unusual behavior might be advantageous for its role in the pathogenicity of L. monocytogenes.
摘要
利用内含肽表达系统表达并鉴定了单核细胞增生李斯特菌的广谱磷脂酶C（PLC）。这种锌金属酶与蜡样芽孢杆菌的同源酶相似，可作用于多种脂质底物。对于单体底物，疏水酰基链的长度通过影响底物亲和力（Km）对酶效率有显著影响。基于该酶与蜡样芽孢杆菌蛋白的同源模型，产生了几个活性位点残基突变。虽然这种PLC与蜡样芽孢杆菌PLC具有许多机制特征，但一个主要区别是，无论底物状态（单体、胶束或囊泡）如何，单核细胞增生李斯特菌酶的最适pH值均呈酸性。这种不寻常的行为可能对其在单核细胞增生李斯特菌致病性中的作用具有优势。
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