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Literature summary extracted from

  • Kingma, R.L.; Snijder, H.J.; Dijkstra, B.W.; Dekker, N.; Egmond, M.R.
    Functional importance of calcium binding sites in outer membrane phospholipase A (2002), Biochim. Biophys. Acta, 1561, 230-237.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.32
-
 Escherichia coli
3.1.1.32 expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.32
-
 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.32 D148N 100% of wild-type activity Escherichia coli
3.1.1.32 D149A 100% of wild-type activity Escherichia coli
3.1.1.32 D149N approx. 85% of wild-type activity Escherichia coli
3.1.1.32 D184A approx. 30% of wild-type activity Escherichia coli
3.1.1.32 H26C introduced cysteine covalently links 2 OMPLA monomers to an active dimer via disulfide bond Escherichia coli
3.1.1.32 S152N approx. 6% of wild-type activity Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.32 EDTA no activity in the presence of EDTA Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.32 integral to membrane
-
 Escherichia coli
-
-
3.1.1.32 outer membrane
-
 Escherichia coli 19867
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.32 Ca2+ required for actiivty, one Ca2+ per monomer bound at the dimer interface Escherichia coli
3.1.1.32 Ca2+ required for activity, only in dimeric OMPLA high affinity Ca2+-sites are formed that are essential for catalysis Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.32 27000
-
 2 * 27000, SDS-PAGE, OMPLA is only active in the dimeric state Escherichia coli
3.1.1.32 31000
-
 2 * 31000, OMPLA is only active as a dimer Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.32 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.32 recombinant OMPLA Escherichia coli
3.1.1.32 recombinant phospholipase A Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.32 84
-
 substrate hexadecanoylthioethane-1-phosphocholine Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.32 1,2-dioctadecenoylthio-sn-glycero-3-phosphocholine + H2O
-
 Escherichia coli 1-thio-2-octadecenoylthio-sn-glycero-3-phosphocholine + octadecenoate
-
 ?
3.1.1.32 1,2-dioctadecenoylthio-sn-glycero-3-phosphoethanolamine + H2O
-
 Escherichia coli 1-thio-2-octadecenoylthio-sn-glycero-3-phosphoethanolamine + octadecenoate
-
 ?
3.1.1.32 1,2-dioctadecenoylthio-sn-glycero-3-phosphoglycerol + H2O
-
 Escherichia coli 1-thio-2-octadecenoylthio-sn-glycero-3-phosphoglycerol + octadecenoate
-
 ?
3.1.1.32 2-hexadecanoylthio-ethane-1-phosphocholine + H2O
-
 Escherichia coli thio-ethane-1-phosphocholine + hexadecanoate
-
 ?
3.1.1.32 hexadecanoylthioethane-1-phosphocholine + H2O
-
 Escherichia coli hexadecanoate + thioethane-1-phosphocholine
-
 ?
3.1.1.32 phosphatidylcholine + H2O
-
 Escherichia coli 2-acylglycerophosphocholine + a carboxylate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.32 dimer 2 * 27000, SDS-PAGE, OMPLA is only active in the dimeric state Escherichia coli
3.1.1.32 dimer 2 * 31000, OMPLA is only active as a dimer Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.1.1.32 OMPLA
-
 Escherichia coli
3.1.1.32 outer membrane phospholipase A
-
 Escherichia coli