Sandbox GGC14: Difference between revisions

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==== Mechanism ====

This a-Galactosidase, along with Human a-Galactosidase, reacts via a double displacement mechanism. Asp132 acts as the nucleophile while Asp226 functions as the acid/base catalyst.<ref>DOI 10.1016/j.jmb.2004.03.062</ref> a-Galactosidase is part of a group of enzymes known as glycoside hydrolases, which generally have 1 of 2 mechanisms. The 1st mechanism is a 1 step mechanism that induces the inversion of the stereochemistry of the substrate anomeric center, while the 2nd mechanism is a 2 step mechanism that preserves the stereochemistry. a-Galactosidase uses the 2-step mechanism.

This a-Galactosidase, along with Human a-Galactosidase, reacts via a double displacement mechanism. Asp132 acts as the nucleophile while Asp226 functions as the acid/base catalyst.<ref>DOI 10.1016/j.jmb.2004.03.062</ref> a-Galactosidase is part of a group of enzymes known as glycoside hydrolases, which generally have 1 of 2 mechanisms. The 1st mechanism is a 1 step mechanism that induces the inversion of the stereochemistry of the substrate anomeric center, while the 2nd mechanism is a 2 step mechanism that preserves the stereochemistry. a-Galactosidase uses the 2-step mechanism. Also, glycoside hydrolases generally have two catalytic residues with carboxyl side groups, specifically Glutamic Acid and Aspartic Acid; in the case of T. reesei, the 2 Asp residues are consistent with this mechanism.

[[Image:Mechanism_Pic2.png | thumb]]

Sandbox GGC14: Difference between revisions

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 ==== Mechanism ====
-This a-Galactosidase, along with Human a-Galactosidase, reacts via a double displacement mechanism.  Asp132 acts as the nucleophile while Asp226 functions as the acid/base catalyst.<ref>DOI 10.1016/j.jmb.2004.03.062</ref>  a-Galactosidase is part of a group of enzymes known as glycoside hydrolases, which generally have 1 of 2 mechanisms.  The 1st mechanism is a 1 step mechanism that induces the inversion of the stereochemistry of the substrate anomeric center, while the 2nd mechanism is a 2 step mechanism that preserves the stereochemistry.  a-Galactosidase uses the 2-step mechanism.
+This a-Galactosidase, along with Human a-Galactosidase, reacts via a double displacement mechanism.  Asp132 acts as the nucleophile while Asp226 functions as the acid/base catalyst.<ref>DOI 10.1016/j.jmb.2004.03.062</ref>  a-Galactosidase is part of a group of enzymes known as glycoside hydrolases, which generally have 1 of 2 mechanisms.  The 1st mechanism is a 1 step mechanism that induces the inversion of the stereochemistry of the substrate anomeric center, while the 2nd mechanism is a 2 step mechanism that preserves the stereochemistry.  a-Galactosidase uses the 2-step mechanism.  Also, glycoside hydrolases generally have two catalytic residues with carboxyl side groups, specifically Glutamic Acid and Aspartic Acid; in the case of T. reesei, the 2 Asp residues are consistent with this mechanism.
 [[Image:Mechanism_Pic2.png | thumb]]