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Literature summary for 3.1.1.74 extracted from

  • Park, J.S.; Han, K.Y.; Lee, J.H.; Song, J.A.; Ahn, K.Y.; Seo, H.S.; Sim, S.J.; Kim, S.W.; Lee, J.
    Solubility enhancement of aggregation-prone heterologous proteins by fusion expression using stress-responsive Escherichia coli protein, RpoS (2008), BMC Biotechnol., 8, 15.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
industry Cutinase is used as a lipolytic enzyme in the composition of laundry and dishwashing detergents to more efficiently remove immobilized fats. The oleochemistry industries and pollutant degradation represent other potential uses of cutinase. Pseudomonas putida

Cloned(Commentary)

Cloned (Comment) Organism
Expression of aggregation-prone cutinase protein using RNA polymerase sigma factor (RpoS) or glutathione transferase as fusion partners in Escherichia coli strain BL21 (DE3). Pseudomonas putida

General Stability

General Stability Organism
Using RNA polymerase sigma factor (RpoS) or glutathione transferase as fusion expression partners, the solubility of cutinase significantly increases. Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas putida Cutinase is known for its hydrolytic activity for a variety of esters ranging from soluble p-nitrophenyl esters to insoluble long-chain triglycerides. The hydrolytic activity of cutinase, especially on p-nitrophenyl esters of fatty acids, is extremely sensitive to fatty acid chain length. ?
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?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
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-
-

Purification (Commentary)

Purification (Comment) Organism
purification of his-tagged protein using Ni2+-affinity chromatography Pseudomonas putida

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
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Pseudomonas putida
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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Assay of enzymatic activity of the fusion mutant of cutinase (RpoS-CUT) shows the same selective bioactivity as native cutinase to degrade p-nitrophenyl butyrate (PNB) but not to degrade p-nitrophenyl butyrate. Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Cutinase is known for its hydrolytic activity for a variety of esters ranging from soluble p-nitrophenyl esters to insoluble long-chain triglycerides. The hydrolytic activity of cutinase, especially on p-nitrophenyl esters of fatty acids, is extremely sensitive to fatty acid chain length. Pseudomonas putida ?
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?

Synonyms

Synonyms Comment Organism
cutinase
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Pseudomonas putida

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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assay at Pseudomonas putida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Pseudomonas putida