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Literature summary for 3.1.1.32 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)

Cloned (Comment) Organism
-
Escherichia coli
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Protein Variants

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

Inhibitors

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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