Sandbox Reserved 655: Difference between revisions
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== '''Mechanism''' == | == '''Mechanism''' == | ||
[[Image:Mechanism. | [[Image:Endoglucanase Mechanism.jpeg]] | ||
The CBM facilitates the enzyme by binding the complex to the cellulose, thus maintaining the proximity of the enzyme and the substrate. It can also target areas of the cellulose that are specific to the enzyme complex. In addition, the CBM itself can disrupt the structure of the cellulose and thus expose the substrate more to the enzyme. The aromatic amino acid residues and planar architecture of the CBM binding sites are complementary to the hydrophobic sites of cellulose chains (hydrophobic 110 face). This exposes the beta-D-glucopyranose rings in the chair conformation, which have their alpha and beta faces having either two or three axial hydrogens exposed and ring hydroxyl groups in the equatorial position, allowing the CBMs to bind efficiently (Nimlos, et al., 2007). | The CBM facilitates the enzyme by binding the complex to the cellulose, thus maintaining the proximity of the enzyme and the substrate. It can also target areas of the cellulose that are specific to the enzyme complex. In addition, the CBM itself can disrupt the structure of the cellulose and thus expose the substrate more to the enzyme. The aromatic amino acid residues and planar architecture of the CBM binding sites are complementary to the hydrophobic sites of cellulose chains (hydrophobic 110 face). This exposes the beta-D-glucopyranose rings in the chair conformation, which have their alpha and beta faces having either two or three axial hydrogens exposed and ring hydroxyl groups in the equatorial position, allowing the CBMs to bind efficiently (Nimlos, et al., 2007). | ||
