3.1.4.41	evolution	the enzyme belongs to the the family of phospholipases D, PLD	731005	
3.1.4.41	additional information	active site structure, the highly conserved residue Trp230 is important in substrate binding, overview	714061	
3.1.4.41	additional information	highly conserved amino acids of the glycerophosphoryl diester phosphodiesterase domain of the recombinant enzyme interact with the substrate sphingomyelin and are involved in substrate recognition. Residues D259 and S262 form part of the catalytic pocket, and they have an important role in substrate recognition and maintenance of the electronegative net charge which sustains the interaction with sphingomyelin	731005	
3.1.4.41	physiological function	Arcanobacterium haemolyticum utilizes phospholipase D to mediate its uptake into non-phagocytic cell. The sphingomyelinase activity of phospholipase D is necessary to increase bacterial adherence to Detroit 562 cells	750742	
3.1.4.41	physiological function	in loxoscelism, the enzyme increases the expression/secretion of matrix metalloproteinases MMP2 and MMP9 and also stimulates the expression of MMP7 (matrilysin-1), which is associated with keratinocyte cell death	751945	
3.1.4.41	physiological function	phospholipases D are the major dermonecrotic component of Loxosceles intermedia venom and catalyze the hydrolysis of phospholipids, resulting in the formation of lipid mediators such as ceramide-1-phosphate and lysophosphatidic acid which can induce pathological and biological responses	713659	
3.1.4.41	physiological function	SMase D is a potent insecticidal toxin, comparison of toxic insecticidal activity, paralytic doses, against Acheta domestica of enzyme in crude spider venom with purified recombinanat enzyme, overview. Purified SMase D is more toxic to crickets than crude venom	731002	
3.1.4.41	physiological function	the activity of sphingomyelinase D is clearly influenced by the supramolecular organization of its substrate in membranes and, in situ ceramide-1-phosphate generation by enzymatic activity profoundly alters the lateral structure and morphology of the target membranes	730697	
3.1.4.41	physiological function	the endogenous metalloprotease of the adamalysin (ADAM) family is activated by the sphingomyelinase D in the venom, the metalloprotease induces the activation of cleavage of pro-inflammatory agent C5a at two sites, resulting in the release of the extracellular N-terminus. That way the spider venom reduces expression and function of the C5a receptor, a component of the complement system, overview	729815	
3.1.4.41	physiological function	the enzymatic activity of phospholipase D is necessary to promote hemolysis by arcanolysin, produced by the human pathogen Arcanobacterium haemolyticum. Incubating phospholipase D with erythrocytes corresponds with an increase in the amount of arcanolysin bound to host membranes	-, 752302	
3.1.4.41	physiological function	the enzyme activity is necessary to promote arcanolysin-mediated hemolysis of erythrocytes in both time- and concentration-dependent manners	-, 752303	
3.1.4.41	physiological function	the enzyme inhibits store-operated Ca2+ entry in T lymphocytes by suppressing ORAI current. Corynebacterium pseudotuberculosis has the ability to suppress the activity of the store-operated Ca2+ entry channel Orai1 with the enzyme to create an acquired, chronic severe combined immunodeficiency-like condition that allows persistent infection	751246	
3.1.4.41	physiological function	the enzyme is a toxic component of Loxosceles venom that activates human blood leukocytes in a partially complement-dependent manner, which can contribute to the systemic inflammation that follows envenomation by the spider	751580	
3.1.4.41	physiological function	the enzyme is responsible for the dermonecrosis and systemic effects observed in loxoscelism	750196	
3.1.4.41	physiological function	the reaction products of the enzyme promote cell migration and inflammation	752304	
3.1.4.41	physiological function	toxin phospholipases-D in the venom of Loxosceles spiders is the main responsible for local and systemic effects observed in the loxoscelism	715398