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Literature summary for 3.1.1.74 extracted from

  • Su, L.; Woodard, R.W.; Chen, J.; Wu, J.
    Extracellular location of Thermobifida fusca cutinase expressed in Escherichia coli BL21(DE3) without mediation of a signal peptide (2013), Appl. Environ. Microbiol., 79, 4192-4198.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.74

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally His-tagged wild-type and mutant cutinase lacking the signal peptide sequence in Escherichia coli strain BL21(DE3), the enzyme is mostly secreted to the medium. Compared to the cells expressing the inactive cutinase mutant S130A, the cells expressing the truncated cutinase show increased membrane permeability and irregular morphology Thermobifida fusca

Protein Variants

Protein Variants Comment Organism
S130A site-directed mutagenesis, catalytically inactive active site mutant, which is mostly located in the cytoplasm. Compared to the cells expressing the inactive cutinase mutant S130A, the cells expressing the truncated cutinase show increased membrane permeability and irregular morphology Thermobifida fusca

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Thermobifida fusca
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermobifida fusca the enzyme has hydrolytic activity toward phospholipids of the cell membrane, cf. EC 3.1.1.3 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermobifida fusca
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His-tagged wild-type and mutant cutinases lacking the signal peptide sequence 1.9fold from Escherichia coli strain BL21(DE3) culture supernatant by ammonium sulfate fractionation and nickel affinity chromatography Thermobifida fusca

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme has hydrolytic activity toward phospholipids of the cell membrane, cf. EC 3.1.1.3 Thermobifida fusca ?
-
 ?

General Information

General Information Comment Organism
additional information the enzyme has a Ser130-His208-Asp176 catalytic triad in which Ser130 is critical to the hydrolytic activity Thermobifida fusca