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Literature summary for 3.1.4.4 extracted from

  • Yang, H.; Roberts, M.F.
    Phosphohydrolase and transphosphatidylation reactions of two Streptomyces phospholipase D enzymes: Covalent versus noncovalent catalysis (2003), Protein Sci., 12, 2087-2098.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
phosphatidic acid up to 2fold Streptomyces chromofuscus

Cloned(Commentary)

Cloned (Comment) Organism
-
Streptomyces chromofuscus

Protein Variants

Protein Variants Comment Organism
C123A enzymatically inactive, secondary structure and thermostability similar to wild type Streptomyces chromofuscus
C123S enzymatically inactive, secondary structure and thermostability similar to wild type Streptomyces chromofuscus
H171A 17% of wild type activity Streptomyces chromofuscus
H187A dramatic decrease in activity Streptomyces chromofuscus
H200A dramatic decrease in activity Streptomyces chromofuscus
H266A 17% of wild type activity, activation by phosphatidic acid up to 12fold Streptomyces chromofuscus
additional information truncation of C-terminal 530 bp, no enzymic activtiy probably due o misfolding Streptomyces chromofuscus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.16
-
1,2-dibutyl-sn-glycero-3-phosphocholine pH 7.5, in presence of 5 mM Ca2+ Streptomyces chromofuscus

Organism

Organism UniProt Comment Textmining
Streptomyces chromofuscus Q8KRU5 ATCC type strain
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Streptomyces chromofuscus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
13
-
pH 7.5, in presence of 5 mM Ca2+ Streptomyces chromofuscus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-dibutyl-sn-glycero-3-phosphocholine + H2O
-
Streptomyces chromofuscus choline + ?
-
?