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Literature summary for 3.1.4.4 extracted from

  • Yang, H.; Roberts, M.F.
    Expression and characterization of a heterodimer of Streptomyces chromofuscus phospholipase D (2004), Biochim. Biophys. Acta, 1703, 43-51.
    View publication on PubMed
Search for more literature for 3.1.4.4

Activating Compound

Activating Compound Comment Organism Structure
Ca2+ inhibits the PLD37/18-catalyzed hydrolysis of dibutyroylphosphatidylcholine at basic pH values, but activates the enzyme more than twofold at pH 5.5. Addition of Ca2+ at pH 8.0 increases the transphosphatidylation activity 2.5- and 3.5fold with 5 and 20 mM Ca2+, respectively. At pH 9.0, Ca2+ inhibits both phosphohydrolase and transferase activities with much less inhibition to the latter Streptomyces chromofuscus

Cloned(Commentary)

Cloned (Comment) Organism
expression of PLD37/18 in Escherichia coli. PLD37 is the N-terminal fragment which contains the active site. PLD18 is the C-terminal fragment which is likely to play a regulatory role. The proteolytically clipped PLD37/18 is more active than the intact enzyme, but is no longer subject to product activation Streptomyces chromofuscus

Protein Variants

Protein Variants Comment Organism
additional information expression of PLD37/18 in Escherichia coli. PLD37 is the N-terminal fragment which contains the active site. PLD18 is the C-terminal fragment which is likely to play a regulatory role. The proteolytically clipped PLD37/18 is more active than the intact enzyme, but is no longer subject to product activation Streptomyces chromofuscus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 dibutyroylphosphatidylcholine reaction with PLD37/18 Streptomyces chromofuscus
0.23
-
 diheptanoylphosphatidylcholine reaction with PLD37/18 Streptomyces chromofuscus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ inhibits the PLD37/18-catalyzed hydrolysis of dibutyroylphosphatidylcholine at basic pH values, but activates the enzyme more than twofold at pH 5.5. Addition of Ca2+ at pH 8.0 increases the transphosphatidylation activity 2.5- and 3.5fold with 5 and 20 mM Ca2+, respectively. At pH 9.0, Ca2+ inhibits both phosphohydrolase and transferase activities with much less inhibition to the latter Streptomyces chromofuscus

Organism

Organism UniProt Comment Textmining
Streptomyces chromofuscus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Streptomyces chromofuscus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dibutyroylphosphatidylcholine + H2O
-
 Streptomyces chromofuscus dibutyroylglycerophosphate + choline
-
 ?
diheptanoylphosphatidylcholine + H2O
-
 Streptomyces chromofuscus diheptanoylglycerophosphate + choline
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8.5 hydrolysis of dibutyroylphosphatidylcholine, reaction with PLD37/18 Streptomyces chromofuscus