BRENDA - Enzyme Database

Improving phospholipase D activity and selectivity by bio-imprinting-immobilization to produce phosphatidylglycerol

Li, B.; Duan, D.; Wang, J.; Li, H.; Zhang, X.; Zhao, B.; J. Biotechnol. 281, 67-73 (2018)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
3.1.4.4
synthesis
hyperactivation of PLD by bio-imprinting and immobilization by adsorption and precipitation, followed by cross-linking results in increased catalytic activity. The maximum activity of immobilized PLD reaches 166953 U/g protein, compared to 11922 U/mg protein for the free form. The selectivity of PLD is significantly enhanced after immobilization. The yield of phosphatidylglycerol and phosphatidic acid reaches 94.0% and 5.96%, respectively
Streptomyces sp.
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.4.4
Streptomyces sp.
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.4.4
commercial preparation
-
Streptomyces sp.
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.1.4.4
11.92
-
free enzyme, pH 5.5, temperature not specified in the publication
Streptomyces sp.
3.1.4.4
166.9
-
bio-imprinted immobilized enzyme, pH 6.0, temperature not specified in the publication
Streptomyces sp.
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.4.4
phosphatidylcholine + H2O
-
751163
Streptomyces sp.
choline + phosphatidate
-
-
-
?
3.1.4.4
phosphatidylethanolamine + H2O
-
751163
Streptomyces sp.
ethanolamine + phosphatidate
-
-
-
?
3.1.4.4
phosphatidylglycerol + H2O
-
751163
Streptomyces sp.
glycerol + phosphatidate
-
-
-
?
Application (protein specific)
EC Number
Application
Commentary
Organism
3.1.4.4
synthesis
hyperactivation of PLD by bio-imprinting and immobilization by adsorption and precipitation, followed by cross-linking results in increased catalytic activity. The maximum activity of immobilized PLD reaches 166953 U/g protein, compared to 11922 U/mg protein for the free form. The selectivity of PLD is significantly enhanced after immobilization. The yield of phosphatidylglycerol and phosphatidic acid reaches 94.0% and 5.96%, respectively
Streptomyces sp.
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.4.4
commercial preparation
-
Streptomyces sp.
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.1.4.4
11.92
-
free enzyme, pH 5.5, temperature not specified in the publication
Streptomyces sp.
3.1.4.4
166.9
-
bio-imprinted immobilized enzyme, pH 6.0, temperature not specified in the publication
Streptomyces sp.
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.4.4
phosphatidylcholine + H2O
-
751163
Streptomyces sp.
choline + phosphatidate
-
-
-
?
3.1.4.4
phosphatidylethanolamine + H2O
-
751163
Streptomyces sp.
ethanolamine + phosphatidate
-
-
-
?
3.1.4.4
phosphatidylglycerol + H2O
-
751163
Streptomyces sp.
glycerol + phosphatidate
-
-
-
?