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Literature summary for 3.1.4.4 extracted from

  • Uesugi, Y.; Mori, K.; Arima, J.; Iwabuchi, M.; Hatanaka, T.
    Recognition of phospholipids in Streptomyces phospholipase D (2005), J. Biol. Chem., 280, 26143-26151.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of chimeras between TH-2PLD and PLD from a distict Streptomyces sp. Streptomyces septatus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km-values of chimeric enzymes Streptomyces septatus
0.075
-
phosphatidyl-p-nitrophenol pH 5.5, hydrolysis Streptomyces septatus
1.16
-
phosphatidyl-p-nitrophenol pH 5.5, transphosphatidylation Streptomyces septatus

Organism

Organism UniProt Comment Textmining
Streptomyces septatus
-
recombinant enzyme
-
Streptomyces septatus TH-2
-
recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme expressed in Escherichia coli Streptomyces septatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphatidyl-p-nitrophenol + H2O the N-terminal HKD motif contains the catalytic nucleophile, which attacks the phosphatidyl group of the substrate Streptomyces septatus phosphatidate + p-nitrophenol
-
?
phosphatidyl-p-nitrophenol + H2O the N-terminal HKD motif contains the catalytic nucleophile, which attacks the phosphatidyl group of the substrate Streptomyces septatus TH-2 phosphatidate + p-nitrophenol
-
?

Synonyms

Synonyms Comment Organism
TH-2PLD
-
Streptomyces septatus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information turnover-numbers of chimeric enzymes Streptomyces septatus
68.8
-
phosphatidyl-p-nitrophenol pH 5.5, hydrolysis Streptomyces septatus
174.8
-
phosphatidyl-p-nitrophenol pH 5.5, transphosphatidylation Streptomyces septatus