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3.1.1.74: cutinase

This is an abbreviated version!
For detailed information about cutinase, go to the full flat file.

Word Map on EC 3.1.1.74

Reaction

cutin
+
H2O
= 2 cutin monomers

Synonyms

acidic cutinase, CcCUT1, CDEF1, CLE, Cut 5a, cut-2.KW3, Cut1, Cut11, Cut190, Cut2, Cut5a, CUTAB1, CutB, cuticle destructing factor 1, cutin esterase, cutin hydrolase, cutinase, cutinase 1, cutinase 2, cutinase-1, cutinase-like enzyme, cutinolytic polyesterase, CutL, CutL1, FspC, fungal cutinase, HIc, LC-cutinase, More, MYCTH_2110987, PET hydrolase, Tfu_0883, Thcut1, THCUT1 protein, Thc_Cut1, Thc_Cut2, TRIREDRAFT_60489

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.74 cutinase

Purification

Purification on EC 3.1.1.74 - cutinase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity purification
-
by centrifugation, ultrafiltration and on Ni2+ column
-
by immobilized metal affinity chromatography exploiting a C-terminal His-tag
by ion-exchange chromatography
by nickel-affinity chromatography
His-tagged protein, expressed in Pichia pastoris
native extracellular enzyme 1.42fold to homogeneity by ammoium sulfate fractionation, cation exchange chromatography, and two steps of gel filtration
-
non-tagged and the C-terminal tagged cutinases, by diafiltration
on Ni2+ affinity column
optimization and evaluation of foam fractionation as purification method to purify an extracellular cutinase from untreated supernatant of mycelium of submerged cultures of the basidiomycete Coprinopsis cinerea as a model enzyme, detailed overview
-
osmotic shock, acid precipitation, dialysis and two sequential anion exchange chromatographic steps, followed by a final dialysis and subsequently freeze-dried. Cutinase purity is confirmed by 12.5% SDS-PAGE
-
purification includes cationic Expanded Bed Adsorption (EBA) followed by hydrophobic interaction chromatography (HIC)
-
purification of his-tagged protein using Ni2+-affinity chromatography
-
recombinant C-terminally His-tagged enzyme from Pichia pastoris by nickel affinity chromatography
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
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) culture supernatant by nickel affinity chromatography to homogeneity
recombinant cutinase FspC from Bacillus subtilis
-
recombinant cutinase isozymes Tfu 0882 and Tfu 0883 from Escherichia coli strain BL21(DE3)
-
recombinant enzyme
recombinant enzyme from Escherichia coli strain BL21-Gold(DE3)
recombinant enzyme from Pichia pastoris strain X-33culture supernatant by tangential flow filtration and filter cell-based ultrafiltration
-
recombinant enzyme partially 293fold from Pichia pastoris strain X-33 by ultrafiltration
-
recombinant extracellular enzyme 2.0fold from culture supernatant by ammonium sulfate precipitation and two different steps of anion exchange chromatography
-
recombinant extracellular wild-type and mutant enzymes without a putative N-terminal signal peptide (Met1-Ala34) and Gln35 from Escherichia coli
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity and anion exchange chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Origami B (DE3) by nickel affinity chromatography, tag cleavage by recombinant enterokinase, and anion exchange chromatography
study of enzyme partition in a 20% polyethylene glykol/15% phosphate two-phase system. Specific interaction of butyrate to the active site of enzyme, enzyme-butyrate complex is over two times the size of the free enzyme
-
wild-type and mutants purified by ultrafiltration, wild-type further purified by hydrophobic interaction chromatography and ammonium sulfate precipitation, 1.6fold with a yield of 70%