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Results 1 - 10 of 109 > >>
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EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - 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 736482
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - 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 736482
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - 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 736482
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - 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 736482
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - Avicel Km-value 1.8 g/l, pH 5, 25°C 735810
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - more - 664883
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - more bacterial cellulose binding at low nanomolar free enzyme concentrations is exclusively active site-mediated and is consistent with Langmuir's one binding site model, strongest binding observed with non-complexed cellulases, productive binding of te enzyme to cellulose chain ends on the hydrophobic face of bacterial cellulose microfibril. With increasing free TrCel7A concentrations the isotherm gradually deviates from the Langmuir's one binding site model caused by the increasing contribution of lower affinity binding modes that included both active site-mediated binding and non-productive binding with active site free from cellulose chain. The binding of enzyme to bacterial cellulose is only partially reversible. Measurement of binding kinetics and modelling, overview 732771
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - more comparative analysis of steady-state kinetics, adsorption, and processivity for wild-type enzyme and the W38A variant, full-length enzymes and catalytic domains with substrate Avicel PH 101, detailed overiew 732157
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - more detailed kinetic analysis of wild-type enzyme and mutants E212Q, D214N, and E217Q 663575
Show all pathways known for 3.2.1.176Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.176-999 - more Michaelis-Menten kinetic 732095
Results 1 - 10 of 109 > >>
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