title: The PLD superfamily: insights into catalysis.
abstract: Knowledge of the PLD superfamily is rapidly expanding and new insights into the mechanism and regulation of the superfamily are rapidly emerging. The recent structural analysis and use of mutant proteins suggest a mechanism that involves two active sites acting in concert. While a number of residues are required for activity, it appears most likely that a histidine is the residue that becomes covalently linked to phosphatidate in catalysis. Evidence for these proposals is covered in this article.
authors.affiliation: Department of Biochemistry, Wake Forest University School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157, USA. mwaite@wfubmc.edu
authors.forename: M
authors.initials: M
authors.lastname: Waite
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010739:Phospholipase D / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D010739:Phospholipase D