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Shane Riley

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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+.Domain C consisting of eight β-strands assembles into a globular unit forming a Greek key motif. It also holds the third Ca2+ binding site in association with domain A.Positioned on the C-terminal side of the β-strands of the (β/ α)8barrel in domain A, is the active site. The catalytic residues involved in the active site are Asp234, Glu264, and Asp331, for BSTA. The residues are identical to other α-amylases, yet there positional differences which reflect the flexible nature of catalytic resides.

Function=

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Digestion

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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