Cloned (Comment) | Organism |
---|---|
recombinant enzyme expression | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces albidoflavus | K0J3J2 | - |
- |
Streptomyces albidoflavus NA297 | K0J3J2 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme by ammonium sulfate fractionation, hydrophobic interaction and cation exchange chromatography, followed by anion exchange chromatography | Streptomyces albidoflavus |
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 | Comment | Organism |
---|---|---|
PLA1 | - |
Streptomyces albidoflavus |
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 |