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Literature summary for 3.1.1.4 extracted from

  • Kanaujia, S.P.; Sekar, K.
    Structures and molecular-dynamics studies of three active-site mutants of bovine pancreatic phospholipase A2 (2008), Acta Crystallogr. Sect. D, 64, 1003-1011.
    View publication on PubMed

Crystallization (Commentary)

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

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

Localization Comment Organism GeneOntology No. Textmining
extracellular
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Bos taurus
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-

Metals/Ions

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/ Products (Substrates)

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 ?
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?

Organism

Organism UniProt Comment Textmining
Bos taurus P00593
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-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
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Bos taurus
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Substrates and Products (Substrate)

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 ?
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?
additional information the secretory isozyme has a catalytic dyad formed by Asp99 and His48 Bos taurus ?
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?

Subunits

Subunits Comment Organism
More wild-type and mutant structure analysis and comparison, molecular-dynamics simulation, overview Bos taurus

Synonyms

Synonyms Comment Organism
PLA2
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Bos taurus
secretory PLA2s
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Bos taurus