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Literature summary for 3.1.1.32 extracted from

  • Snijder, H.J.; Van Eerde, J.H.; Kingma, R.L.; Kalk, K.H.; Dekker, N.; Egmond, M.R.; Dijkstra, B.W.
    Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: Function of the Asn-His interaction in the catalytic triad (2001), Protein Sci., 10, 1962-1969.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of N156A mutant Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
N156A mutant OMPLA is crystallized by hanging drop vapor-diffusion, drops consisting of 0.003 ml of protein solution and 0.002 ml reservoir solution are suspended over a 1 ml reservoir containing 27% 2-methyl-2,4-pentanediol, 0.4-1 mM CaCl2 and 100 mM Bis-Tris buffer, pH 6.0-6.3, the initial protein solution contained 10 mg/ml N156A OMPLA, 10 mM KCl, 1% 1-O-n-octyl-beta-D-glucopyranoside and 0.2 mM Tris-HCl at pH 6.6, crystals diffract to 2.5-3 A Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
outer membrane
-
Escherichia coli 19867
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required for activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphatidylcholine + H2O Escherichia coli
-
2-acylglycerophosphocholine + a carboxylate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
N156A mutant Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphatidylcholine + H2O
-
Escherichia coli 2-acylglycerophosphocholine + a carboxylate
-
?

Synonyms

Synonyms Comment Organism
OMPLA
-
Escherichia coli
outer membrane phospholipase A
-
Escherichia coli