From Proteopedia

proteopedia linkproteopedia link

Shane Riley

Template:STRUCTURE 1hvx

Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell.

Contents 1 Introduction 2 Structure 3 Function= 3.1 Digestion 4 References

Introduction

α-Amylase is an enzyme that acts as a catalyst for the hydrolysis of alpha-linked polysaccharides into α-anomeric products.^[1]The enzyme comes from a variety of sources, each with different characteristics.

Structure

BSTA comprises of a single polypeptide chain. This chain is folded into three domains A, B and C. These domains are generally recognized on α-amylase enzymes. The A domain constitutes the core structure, with a (β/α)barrel.The B domain consists of a sheet of four anti-parallel β-strands with a pair of anti-parallel β-strands. Long loops are observed between the β-strands. Located within the B domain is the binding site for Ca2+- Na+- Ca2+.

Function=

adasdasd

Digestion

texttext ^[2]

References

1. ↑ Suvd D, Fujimoto Z, Takase K, Matsumura M, Mizuno H. Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability. J Biochem. 2001 Mar;129(3):461-8. PMID:11226887
2. ↑ Suvd D, Fujimoto Z, Takase K, Matsumura M, Mizuno H. Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability. J Biochem. 2001 Mar;129(3):461-8. PMID:11226887