Literature summary for 3.1.4.41 extracted from

Ullah, A.; de Giuseppe, P.O.; Murakami, M.T.; Trevisan-Silva, D.; Wille, A.C.; Chaves-Moreira, D.; Gremski, L.H.; da Silveira, R.B.; Sennf-Ribeiro, A.; Chaim, O.M.; Veiga, S.S.; Arni, R.K.
Crystallization and preliminary X-ray diffraction analysis of a class II phospholipase D from Loxosceles intermedia venom (2011), Acta Crystallogr. Sect. F, 67, 234-236.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of His6-tagged wild-type and mutant H12A phospholipase Ds in Escherichia coli strain BL21(DE3)	Loxosceles intermedia

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant wild-type and H12A mutant enzymes, 0.002 ml of protein solution containing 17 mg/ml wild type enzyme and 9 mg/ml H12A mutant, respectively, are mixed with 0.002 ml of reservoir solution containing 0.1 M Tris-HCl, pH 7.5, 40% v/v PEG 200 for the wild-type enzyme, and 0.1 M Tris-HCl, pH 7.5 and 35% v/v PEG 200 for the H12A mutant, equilibration over 1 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.95 and 1.6 A resolution, respectively	Loxosceles intermedia

Crystallization (Comment)

Organism

purified recombinant wild-type and H12A mutant enzymes, 0.002 ml of protein solution containing 17 mg/ml wild type enzyme and 9 mg/ml H12A mutant, respectively, are mixed with 0.002 ml of reservoir solution containing 0.1 M Tris-HCl, pH 7.5, 40% v/v PEG 200 for the wild-type enzyme, and 0.1 M Tris-HCl, pH 7.5 and 35% v/v PEG 200 for the H12A mutant, equilibration over 1 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.95 and 1.6 A resolution, respectively

Loxosceles intermedia

Protein Variants

Protein Variants	Comment	Organism
H12A	site-directed mutagenesis	Loxosceles intermedia

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Loxosceles intermedia	-	-

Organism

Organism	UniProt	Comment	Textmining
Loxosceles intermedia	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged wild-type and mutant H12A phospholipase Ds from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Loxosceles intermedia

Source Tissue

Source Tissue	Comment	Organism	Textmining
venom	-	Loxosceles intermedia	-

Synonyms

Synonyms	Comment	Organism
class II phospholipase D	-	Loxosceles intermedia

General Information

General Information	Comment	Organism
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	Loxosceles intermedia