Sandbox Reserved 459: Difference between revisions

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[[Image:Amylase Hydrolysis.png | Hydrolysis of sugar using Amylase | left | thumb | 300px]]

Hydrolysis of starch or oligosaccharides by mammalian amylases, in general, results in maltose as the leaving group. The active site of these amylases harbors three aromatic residues Trp59, Tyr62, and Tyr151, which provide stacking interactions to the bound glucose moieties. The hydrolysis is catalyzed by three carboxyl groups and its starts from a water nucleophilic attack and opening of the glucose ring in the catalytic center rather than from protonation of the glycosidic oxygen. The chain length of the oligosaccharide has an impact on both the rate of the hydrolytic degradation and the product pattern produced by a-amylase. Oligomers with more than six glucose units are hydrolyzed more rapidly, because they are more akin to the natural substrates of a-amylase.

Hydrolysis of starch or oligosaccharides by mammalian amylases, in general, results in maltose as the leaving group. The active site of these amylases harbors three aromatic residues Trp59, Tyr62, and Tyr151, which provide stacking interactions to the bound glucose moieties. The hydrolysis is catalyzed by three carboxyl groups and its starts from a water nucleophilic attack and opening of the glucose ring in the catalytic center rather than from protonation of the glycosidic oxygen. One of the carboxylic acids in the active site acts as the catalytic nucleophile during the formation of the intermediate. A second carboxylic acid operates as the acid/base catalyst, supporting the stabilization of the transition states during the hydrolysis. The chain length of the oligosaccharide has an impact on both the rate of the hydrolytic degradation and the product pattern produced by a-amylase. Oligomers with more than six glucose units are hydrolyzed more rapidly, because they are more akin to the natural substrates of a-amylase.

Sandbox Reserved 459: Difference between revisions

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Revision as of 01:57, 5 May 2012 view source Alisha Parks (talk \| contribs) 115 edits No edit summary ← Older edit		Revision as of 02:01, 5 May 2012 view source Alisha Parks (talk \| contribs) 115 edits No edit summary Newer edit →
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	[[Image:Amylase Hydrolysis.png \| Hydrolysis of sugar using Amylase \| left \| thumb \| 300px]]		[[Image:Amylase Hydrolysis.png \| Hydrolysis of sugar using Amylase \| left \| thumb \| 300px]]

	Hydrolysis of starch or oligosaccharides by mammalian amylases, in general, results in maltose as the leaving group. The active site of these amylases harbors three aromatic residues Trp59, Tyr62, and Tyr151, which provide stacking interactions to the bound glucose moieties. The hydrolysis is catalyzed by three carboxyl groups and its starts from a water nucleophilic attack and opening of the glucose ring in the catalytic center rather than from protonation of the glycosidic oxygen. The chain length of the oligosaccharide has an impact on both the rate of the hydrolytic degradation and the product pattern produced by a-amylase. Oligomers with more than six glucose units are hydrolyzed more rapidly, because they are more akin to the natural substrates of a-amylase.		Hydrolysis of starch or oligosaccharides by mammalian amylases, in general, results in maltose as the leaving group. The active site of these amylases harbors three aromatic residues Trp59, Tyr62, and Tyr151, which provide stacking interactions to the bound glucose moieties. The hydrolysis is catalyzed by three carboxyl groups and its starts from a water nucleophilic attack and opening of the glucose ring in the catalytic center rather than from protonation of the glycosidic oxygen. One of the carboxylic acids in the active site acts as the catalytic nucleophile during the formation of the intermediate. A second carboxylic acid operates as the acid/base catalyst, supporting the stabilization of the transition states during the hydrolysis. The chain length of the oligosaccharide has an impact on both the rate of the hydrolytic degradation and the product pattern produced by a-amylase. Oligomers with more than six glucose units are hydrolyzed more rapidly, because they are more akin to the natural substrates of a-amylase.