Raghad zoubi

AmeylaseAmeylase

This is a default text for your page Raghad zoubi. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Introduction The α-amylases (EC 3.2.1.1 ) (CAS# 9014-71-5) (alternative names: 1,4-α-D-glucan glucanohydrolase; glycogenase) are calcium metalloenzymes, completely unable to function in the absence of calcium. By acting at random locations along the starch chain, α-amylase breaks down long-chain carbohydrates, ultimately yielding maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase. In animals, it is a major digestive enzyme, and its optimum pH is 6.7–7.0.[3] In human physiology, both the salivary and pancreatic amylases are α-amylases. The α-amylases form is also found in plants, fungi (ascomycetes and basidiomycetes) and bacteria (Bacillus) Structural highlights This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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