Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search General Information

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 16 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41evolution the enzyme belongs to the the family of phospholipases D, PLD 731005
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41more active site structure, the highly conserved residue Trp230 is important in substrate binding, overview 714061
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41more 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.41physiological 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
Results 1 - 10 of 16 > >>