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Literature summary for 3.2.1.176 extracted from

  • Sorensen, T.H.; Cruys-Bagger, N.; Windahl, M.S.; Badino, S.F.; Borch, K.; Westh, P.
    Temperature effects on kinetic parameters and substrate affinity of Cel7A cellobiohydrolases (2015), J. Biol. Chem., 290, 22193-22202.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.176

Protein Variants

Protein Variants Comment Organism
additional information the carbohydrate-binding module has a dual effect on the activity, it diminishes the tendency of heat-induced desorption, but also has a pronounced negative effect on the maximal rate, which was 2fold larger in variants without carbohydrate-binding module throughout the investigated temperature range. Although the carbohydrate-binding module is beneficial for affinity it slows down the catalytic process Trichoderma reesei
additional information the carbohydrate-binding module has a dual effect on the activity, it diminishes the tendency of heat-induced desorption, but also has a pronounced negative effect on the maximal rate, which was 2fold larger in variants without carbohydrate-binding module throughout the investigated temperature range. Although the carbohydrate-binding module is beneficial for affinity it slows down the catalytic process Rasamsonia emersonii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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 Avicel Km value of the full-length enzyme increases from 2.8 g/l, pH 5.0, 10°C, to 19 g/l, pH 5.0, 50°C Trichoderma reesei
additional information
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 Avicel Km value of the full-length enzyme increases from 2.8 g/l, pH 5.0, 10°C, to 29 g/l, pH 5.0, 50°C Rasamsonia emersonii
additional information
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 Avicel Km value of the isolated catalytic domain increases from 4.9 g/l, pH 5.0, 10°C, to 76 g/l, pH 5.0, 50°C Rasamsonia emersonii
additional information
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 Avicel Km value of the isolated catalytic domain increases from 7.1 g/l, pH 5.0, 10°C, to 122 g/l, pH 5.0, 50°C Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Rasamsonia emersonii Q8TFL9
-
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Trichoderma reesei G0RVK1
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Trichoderma reesei QM6a G0RVK1
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
avicel + H2O
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 Trichoderma reesei cellobiose + ?
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 ?
avicel + H2O
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 Rasamsonia emersonii cellobiose + ?
-
 ?
avicel + H2O
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 Trichoderma reesei QM6a cellobiose + ?
-
 ?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
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 the maximal rate increases strongly with temperature, whereas the affinity for the insoluble substrate decreases, and as a result, the effect of temperature depends strongly on the substrate load. Temperature has little or no effect on the hydrolytic rate in dilute substrate suspensions, whereas strong temperature activation is observed at saturating substrate loads Trichoderma reesei
additional information
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 the maximal rate increases strongly with temperature, whereas the affinity for the insoluble substrate decreases, and as a result, the effect of temperature depends strongly on the substrate load. Temperature has little or no effect on the hydrolytic rate in dilute substrate suspensions, whereas strong temperature activation is observed at saturating substrate loads Rasamsonia emersonii