Crystallization (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes, 0.005 ml of 15 mg/ml protein in 50 mM Tris-HCl buffer, pH 7.2, and 5.0 mM CaCl2, is mixed with 0.002 ml of 50% v/v 2-methyl-2,4-pentanediol and equilibrated against 60% v/v 2-methyl-2,4-pentanediol in 0.5 ml reservoir solution, hanging drop vapour diffusion method at room temperature, X-ray diffraction structure determination and analysis at 1.9 A resolution | Bos taurus |
Protein Variants | Comment | Organism |
---|---|---|
D49K | site-directed mutagenesis, the tertiary structures of the active site mutant is similar to that of the trigonal recombinant enzyme, but the mutant lacks a Ca2+ in the active site. Molecular-dynamics simulation, proton transfer is not possible from the catalytic water to the mutated residue | Bos taurus |
D49N | site-directed mutagenesis, the tertiary structures of the active site mutant is similar to that of the trigonal recombinant enzyme, but the mutant lacks a Ca2+ in the active site. Molecular-dynamics simulation, proton transfer is not possible from the catalytic water to the mutated residue | Bos taurus |
H48N | site-directed mutagenesis, the tertiary structures of the active site mutant is similar to that of the trigonal recombinant enzyme. Molecular-dynamics simulation, proton transfer is not possible from the catalytic water to the mutated residue | Bos taurus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Bos taurus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | residue Asp49 in the calcium-binding loop is essential for controlling binding of the calcium ion and catalytic action of phospholipase A2 | Bos taurus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Bos taurus | phospholipase A2 hydrolyzes phospholipids at the sn-2 position to cleave the fatty-acid ester bond of L-glycerophospholipids. The catalytic dyad, formed by residues Asp99 and His48, along with a nucleophilic water molecule is responsible for enzyme hydrolysis | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | P00593 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
pancreas | - |
Bos taurus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | phospholipase A2 hydrolyzes phospholipids at the sn-2 position to cleave the fatty-acid ester bond of L-glycerophospholipids. The catalytic dyad, formed by residues Asp99 and His48, along with a nucleophilic water molecule is responsible for enzyme hydrolysis | Bos taurus | ? | - |
? | |
additional information | the secretory isozyme has a catalytic dyad formed by Asp99 and His48 | Bos taurus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | wild-type and mutant structure analysis and comparison, molecular-dynamics simulation, overview | Bos taurus |
Synonyms | Comment | Organism |
---|---|---|
PLA2 | - |
Bos taurus |
secretory PLA2s | - |
Bos taurus |