Raghad zoubi: Difference between revisions

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== References ==
== References ==
  {{http://en.wikipedia.org/wiki/Amylase}}
  {{reflist}}
<references/>
<references/>

Revision as of 19:05, 22 November 2014

Example page for α-AmeylaseExample page for α-Ameylase


Introduction

The (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

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) [1]

Disease

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Structural highlights

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α-Ameylase

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ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Raghad Zoubi, Michal Harel