Literature summary for 3.1.1.32 extracted from

Murayama, K.; Kano, K.; Matsumoto, Y.; Sugimori, D.
Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297 (2013), J. Struct. Biol., 182, 192-196.

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant enzyme expression	Streptomyces albidoflavus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, hanging drop vapour diffusion method, by equilibrating a mixture containing 0.001 ml of 1.0 mg/ml protein solution containing 20 mM Tris-HCl, pH 9.0, and 20 mM NaCl, and 0.001 ml of reservoir solution containing 1.8 M ammonium sulfate, 3% PEG monomethyl ether 2000, and 0.1 M HEPES, pH 7.5, a few days, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular replacement	Streptomyces albidoflavus

Crystallization (Comment)

Organism

purified recombinant enzyme, hanging drop vapour diffusion method, by equilibrating a mixture containing 0.001 ml of 1.0 mg/ml protein solution containing 20 mM Tris-HCl, pH 9.0, and 20 mM NaCl, and 0.001 ml of reservoir solution containing 1.8 M ammonium sulfate, 3% PEG monomethyl ether 2000, and 0.1 M HEPES, pH 7.5, a few days, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular replacement

Streptomyces albidoflavus

Organism

Organism	UniProt	Comment	Textmining
Streptomyces albidoflavus	K0J3J2	-	-
Streptomyces albidoflavus NA297	K0J3J2	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme by ammonium sulfate fractionation, hydrophobic interaction and cation exchange chromatography, followed by anion exchange chromatography	Streptomyces albidoflavus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme preferentially hydrolyzes the sn-1 acyl ester in glycerophospholipids, yielding a fatty acid and 2-acyl-lysophospholipid, molecular mechanism underlying the substrate binding by the enzyme, overview	Streptomyces albidoflavus	?	-	?
additional information	the enzyme preferentially hydrolyzes the sn-1 acyl ester in glycerophospholipids, yielding a fatty acid and 2-acyl-lysophospholipid, molecular mechanism underlying the substrate binding by the enzyme, overview	Streptomyces albidoflavus NA297	?	-	?

Synonyms

Synonyms	Comment	Organism
PLA1	-	Streptomyces albidoflavus

General Information

General Information	Comment	Organism
additional information	the enzyme's active site is composed of a Ser-His dyad (Ser11 and His218), whereby stabilization of the imidazole is provided by the main-chain carbonyl oxygen of Ser216, a common variation of the catalytic triad in many serine hydrolases, where this carbonyl maintains the orientation of the active site histidine residue. The hydrophobic pocket and cleft for lipid binding are adjacent to the active site, and are approximately 13-15 A deep and 14-16 A long	Streptomyces albidoflavus