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Literature summary for 3.1.4.4 extracted from

  • Ben Ali, Y.; Carriere, F.; Abousalham, A.
    High-level constitutive expression in Pichia pastoris and one-step purification of phospholipase D from cowpea (Vigna unguiculata L. Walp) (2007), Protein Expr. Purif., 51, 162-169.
    View publication on PubMed
Search for more literature for 3.1.4.4

Application

Application Comment Organism
synthesis heterologous high-yield expression of enzyme in Pichia pastoris and purification by single calcium-dependent octyl-sepharose chromatography step gives 8 mg of pure recombinant protein from 1 l of yeast culture without proteolytic degradation of the N-terminal calcium-dependent C2 lipid binding domain Vigna unguiculata

Cloned(Commentary)

Cloned (Comment) Organism
high-yield expression in Pichia pastoris Vigna unguiculata

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
88110
-
 x * 90000, SDS-PAGE, x * 88110, mass spectrometry Vigna unguiculata
90000
-
 x * 90000, SDS-PAGE, x * 88110, mass spectrometry Vigna unguiculata

Organism

Organism UniProt Comment Textmining
Vigna unguiculata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification by single calcium-dependent octyl-sepharose chromatography step Vigna unguiculata

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
27
-
 pH 8.0, 37°C Vigna unguiculata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphatidylcholine + H2O
-
 Vigna unguiculata 1,2-diacylglycerophosphate + choline
-
 ?

Subunits

Subunits Comment Organism
? x * 90000, SDS-PAGE, x * 88110, mass spectrometry Vigna unguiculata

pI Value

Organism Comment pI Value Maximum pI Value
Vigna unguiculata isoelectric focusing
-
 4.7