Literature summary for 3.1.1.4 extracted from

Guy, J.E.; Stahl, U.; Lindqvist, Y.
Crystal structure of a class XIB phospholipase A2 (PLA2): rice (oryza sativa) isoform-2 pla2 and an octanoate complex (2009), J. Biol. Chem., 284, 19371-19379.

Cloned(Commentary)

Cloned (Comment)	Organism
cDNA coding for the predicted mature PLA2 protein, amino acids 1-128 without the signal peptide, designed with optimized codons for high level expression in Escherichia coli strain Tuner (DE3) LacI	Oryza sativa

Crystallization (Commentary)

Crystallization (Comment)	Organism
isoform 2 phospholipase A2, by the sitting drop, vapor-diffusion method, to 2.0 A resolution. The N-terminal half of the chain contains mainly loop structure, including the conserved Ca2+-binding loop, but starts with a short 3(10)-helix and also includes two short anti-parallel beta-strands. The C-terminal half is folded into three anti-parallel alpha-helices, of which the two first contain the conserved catalytic histidine and calcium liganding aspartate residues. The structure is stabilized by six disulfide bonds. The water structure around the calcium ion binding site suggests the involvement of a second water molecule in the mechanism for hydrolysis, the water-assisted calcium-coordinate oxyanion mechanism. The octanoate molecule in the complex structure is bound in a hydrophobic pocket, which extends to the likely membrane interface and is proposed to model the binding of the product fatty acid	Oryza sativa

Crystallization (Comment)

Organism

isoform 2 phospholipase A2, by the sitting drop, vapor-diffusion method, to 2.0 A resolution. The N-terminal half of the chain contains mainly loop structure, including the conserved Ca2+-binding loop, but starts with a short 3(10)-helix and also includes two short anti-parallel beta-strands. The C-terminal half is folded into three anti-parallel alpha-helices, of which the two first contain the conserved catalytic histidine and calcium liganding aspartate residues. The structure is stabilized by six disulfide bonds. The water structure around the calcium ion binding site suggests the involvement of a second water molecule in the mechanism for hydrolysis, the water-assisted calcium-coordinate oxyanion mechanism. The octanoate molecule in the complex structure is bound in a hydrophobic pocket, which extends to the likely membrane interface and is proposed to model the binding of the product fatty acid

Oryza sativa

Protein Variants

Protein Variants	Comment	Organism
additional information	construct A (Leu-1 mutated to an alanine) and construct B (extra glycine inserted between the start methionine and Leu-1), both variants show similar specific activity after refolding	Oryza sativa

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	Ca2+-binding loop	Oryza sativa

Organism

Organism	UniProt	Comment	Textmining
Oryza sativa	Q9XG81	-	-

Purification (Commentary)

Purification (Comment)	Organism
by centrifugation, sonication and gel filtration	Oryza sativa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
33	-	construct A (Leu-1 mutated to an alanine) and construct B (extra glycine inserted between the start methionine and Leu-1)	Oryza sativa

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1-palmitoyl-2-oleoylglycerophosphocholine + H2O	-	Oryza sativa	?	-	?

Synonyms

Synonyms	Comment	Organism
class XIB phospholipase A2	-	Oryza sativa
sPLA2	-	Oryza sativa