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Literature summary for 3.1.4.4 extracted from

  • Uesugi, Y.; Arima, J.; Iwabuchi, M.; Hatanaka, T.
    C-terminal loop of Streptomyces phospholipase D has multiple functional roles (2007), Protein Sci., 16, 197-207.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.4

Protein Variants

Protein Variants Comment Organism
A426F/L438H mutation in residues located in the c-terminal flexible loop. Increase in activities and increase in thermotolerance and tolerance against organic solvents Streptomyces septatus
additional information isolation of mutants with higher activities, higher thermostability and tolerance against organic solvents, and with improved selectivity of the transphosphatidylation activity Streptomyces septatus

Organic Solvent Stability

Organic Solvent Comment Organism
benzene isolation of mutants that maintain their activites after 1 h incubation in benzene Streptomyces septatus
Ethyl acetate isolation of mutants that maintain 85% of activites after 1 h incubation in ethyl acetate Streptomyces septatus

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information G188 and D191 are the key amino acids involved in recognition of phospholipids. A426 and L438 enhance transphosphatidylation activities regardless of the substrate form Streptomyces septatus ?
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 ?
additional information G188 and D191 are the key amino acids involved in recognition of phospholipids. A426 and L438 enhance transphosphatidylation activities regardless of the substrate form Streptomyces septatus TH-2 ?
-
 ?
phosphatidyl-p-nitrophenol + H2O
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 Streptomyces septatus phosphatidic acid + p-nitrophenol
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 ?
phosphatidyl-p-nitrophenol + H2O
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 Streptomyces septatus TH-2 phosphatidic acid + p-nitrophenol
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 ?