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Literature summary for 3.1.4.4 extracted from

  • Khatoon, H.; Talat, S.; Younus, H.
    Phospholipase D from Allium sativum bulbs: A highly active and thermal stable enzyme (2008), Int. J. Biol. Macromol., 42, 380-385.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
phosphatidylinositol 4,5-bisphosphate
-
Allium sativum

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ maximal activity at 70 mM Ca2+ concentration. However, Ca2+ is not mandatory for enzymatic activity Allium sativum

Organism

Organism UniProt Comment Textmining
Allium sativum
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
bulb
-
Allium sativum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphatidylcholine + ethanol enzyme shows also transphosphatidylation activity Allium sativum phosphatidylethanol + choline
-
?
phosphatidylcholine + H2O
-
Allium sativum phosphatidate + choline
-
?

Synonyms

Synonyms Comment Organism
phospholipase D
-
Allium sativum
PLDGB
-
Allium sativum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Allium sativum
70
-
maximal activity Allium sativum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 80 enzyme shows more than 65% of maximal activity Allium sativum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
the crude enzyme retains almost 100% activity after incubation for 30 min at 60°C, after which the activity increases and is about 119% and 139% after incubation for 30 min at 70 and 80°C, respectively Allium sativum
80
-
enzyme shows 90% activity Allium sativum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
assay at Allium sativum