The substrate specificity of phospholipase D (PLO) from Streptomyces antibioticus (SaPLD) has been altered through protein engineering techniques. The mutant enzyme, namely TNYR SaPLD, is capable of producing phosphatidylinositol (Pl) using phosphatidylcholine (PC) and myo-inositol as substrates. TNYR SaPLD has been expressed, purified and crystallised for structural determination by X-ray crystallography to gain a better understanding of the substrate binding features of the mutant enzyme. The work gave insight into the role of the enzyme's catalytic residues and the mutated residues. The structure of the enzyme as well as its conformational changes during substrate binding also have been described.
|Qualification||Doctor of Philosophy|
|Award date||23 Jan 2019|
|Publication status||Unpublished - 2019|