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Literature summary for 3.1.4.4 extracted from

  • Matsumoto, Y.; Sugimori, D.
    Substrate recognition mechanism of Streptomyces phospholipase D and enzymatic measurement of plasmalogen (2015), J. Biosci. Bioeng., 120, 372-379 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Triton X-100 in the presence of 0.05-0.5% and 0.1-0.2% (wt/vol) Triton X-100, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and choline plasmalogen are efficiently hydrolyzed, respectively. Hydrolysis of lysophosphatidylcholine and choline lysoplasmalogen does not require Triton X-100, the hydrolytic activity is inhibited by more than 0.05% (wt/vol) Triton X-100 Streptomyces sp. NA684

Application

Application Comment Organism
analysis enzymatic measurement of choline plasmalogen using PLD684 and phospholipase B Streptomyces sp. NA684

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0513
-
L-alpha-lysophosphatidylcholine pH 5.0, 37°C Streptomyces sp. NA684
0.271
-
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine pH 5.0, 37°C Streptomyces sp. NA684

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Streptomyces sp. NA684
-
-

Organism

Organism UniProt Comment Textmining
Streptomyces sp. NA684 A0A0E4B8Q4 bifunctional enzyme, displays activities of EC 3.1.4.3 and EC 3.1.4.4
-

Purification (Commentary)

Purification (Comment) Organism
from culture supernatant Streptomyces sp. NA684

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O the enzyme hydrolyzes 98.4% of mixed micelle 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine in 1 h Streptomyces sp. NA684 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphate + choline
-
?
choline plasmalogen + H2O substrate of EC 3.1.4.3 Streptomyces sp. NA684 ?
-
?
L-alpha-lysophosphatidylcholine + H2O substrate of EC 3.1.4.3 Streptomyces sp. NA684 ?
-
?
additional information the enzyme prefers mixed micelle substrates to liposomal substrates. The rate-limiting steps of hydrolysis of mixed micelle 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and emulsified lysophosphatidylcholine are the bulk step and the surface step, respectively Streptomyces sp. NA684 ?
-
?

Subunits

Subunits Comment Organism
? x * 54000, SDS-PAGE Streptomyces sp. NA684

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
243
-
L-alpha-lysophosphatidylcholine pH 5.0, 37°C Streptomyces sp. NA684
4000
-
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine pH 5.0, 37°C Streptomyces sp. NA684

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4740
-
L-alpha-lysophosphatidylcholine pH 5.0, 37°C Streptomyces sp. NA684
14800
-
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine pH 5.0, 37°C Streptomyces sp. NA684