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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

General Stability

General Stability on EC 3.1.1.74 - cutinase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ANS binds strongly to native cutinase as a noncompetitive inhibitor with up to 5 ANS per cutinase molecule. The first ANS molecule stabilizes cutinase. The last 4 ANS molecules decrease Tm by up to 7°C
encapsulation of enzyme in bis(2-ethylhexyl) sodium sulfosuccinate reverse micelles induces unfolding at room temperature, presence of 1-hexanol delays or even prevents unfolding
-
half-life time of cutinase at 35°C, pH 8, in a water bath with agitation, increases by 3.5fold with the addition of 15% N,N-dimethylacetamide and by 3fold with 1 M glycerol
-
in bis(2-ethylhexyl) sodium sulfosuccinate reverse micelles, enzyme unfolds with mono-exponential rates, indicating a two-state process. After unfolding in reverse micelles, enzyme is less destabilised than in guanidinium hydrochloride-denatured state, which is supported by fluorescence data. NMR studies indicate a molten globule structure
micelle-forming short-chain phospholipids significantly reduce cutinase stability (both below and above the critical micelle concentration) and rates of folding (only above critical micelle concentration), trapping cutinase in an inactive state which only regains activity over hours to days, rather than the few seconds required for refolding in the absence of detergent. Destabilization decreases with increasing chain length, and increases with critical micelle concentration, indicating that monomers and micelles cooperate in destabilizing cutinase
stability is regulated by Ca2+ binding. One Ca2+ binds to the enzyme, which induces large conformational changes in several loop regions to stabilize an open conformation
stable in presence of hexadecyltrimethyl-ammoniumbromide
-
the disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase
-
trehalose delays thermal unfolding, thus increasing the temperature at the mid-point of unfolding by 7.2°C
-
unfolding of enzyme induced by guanidinium hydrochloride shows a stable intermediate, molten globule
-
unstable in presence of sodium bis(2-ethylhexyl)ester sulfosuccinic acid, unfolding of protein structure
-
Using RNA polymerase sigma factor (RpoS) or glutathione transferase as fusion expression partners, the solubility of cutinase significantly increases.
-