| Literature DB >> 26976751 |
Qiongying Huang1, Anne Gershenson2, Mary F Roberts3.
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. Published by Elsevier B.V.Entities:
Keywords: Acidic pH optimum; Listeria monocytogenes; Mutagenesis; Phospholipase C; Vesicle binding
Mesh：
Substances：
Year: 2016 PMID： 26976751 PMCID： PMC4829451 DOI： 10.1016/j.bbapap.2016.03.008
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002