Literature summary for 3.1.1.3 extracted from

Nardini, M.; Lang, D.A.; Liebeton, K.; Jaeger, K.E.; Dijkstra, B.W.
Crystal structure of Pseudomonas aeruginosa lipase in the open conformation. The prototype for family 1.1 of bacterial lipases (2000), J. Biol. Chem., 275, 31219-31225.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme in open conformation through complexion by inhibitor Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-(4-nitrophenyl) octylphosphonate, sitting drop vapour diffusion method, room temperature, 5 mg/ml protein in10 mM Tris-HCl, pH 8.0, 1% beta-octylpyranoside, equilibration against precipitation solution containing 25% 2-methyl-2,4-pentanediol, 20 mM CaCl2, 100 mM citrate, pH 5.6, several months, X-ray structure determination and analysis at 2.54 A resolution, structure scheme and modelling	Pseudomonas aeruginosa

Crystallization (Comment)

Organism

purified recombinant enzyme in open conformation through complexion by inhibitor Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-(4-nitrophenyl) octylphosphonate, sitting drop vapour diffusion method, room temperature, 5 mg/ml protein in10 mM Tris-HCl, pH 8.0, 1% beta-octylpyranoside, equilibration against precipitation solution containing 25% 2-methyl-2,4-pentanediol, 20 mM CaCl2, 100 mM citrate, pH 5.6, several months, X-ray structure determination and analysis at 2.54 A resolution, structure scheme and modelling

Pseudomonas aeruginosa

Inhibitors

Inhibitors	Comment	Organism	Structure
Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-(4-nitrophenyl) octylphosphonate	binding site structure, binding arrests the enzyme in the open conformation	Pseudomonas aeruginosa

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	stabilizes the loop containing the catalytic His251 residue, binding site structure	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	P26876	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
triacylglycerol + H2O = diacylglycerol + a carboxylate	the catalytic triad is formed by Ser82, Asp229, and His251, substrates bind first to Ser82, position of the oxyanion hole and the three pockets accomodating the sn-1, sn-2, and sn-3 fatty acid chains, reaction mechanism, tetrahedral intermediate during acylation step	Pseudomonas aeruginosa	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
triacylglycerol + H2O	-	Pseudomonas aeruginosa	diacylglycerol + a carboxylate	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme structure contains an unusual alpha/beta hydrolase fold lacking two beta-strands and one helix	Pseudomonas aeruginosa

Synonyms

Synonyms	Comment	Organism
lipase	-	Pseudomonas aeruginosa
More	the enzyme belongs to the family 1.1 of bacterial lipases	Pseudomonas aeruginosa