This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Amylase
From Proteopedia
| Line 7: | Line 7: | ||
==Structure== | ==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. | + | 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 are positional differences which reflect the flexible nature of catalytic resides. |
| - | =Function== | + | CaI, and CaII found at the interface of domain A and C, and CaIII with Na found in the interior of domain B, constitute the metal ion binding sites. CaI is consistent in all α-amylases, however there are differences between the linear trio of CaII, CaIII and Na in other enzymes. |
| + | ==Function== | ||
adasdasd | adasdasd | ||
==Digestion== | ==Digestion== | ||
Revision as of 00:57, 26 March 2010
| 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 |
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 are positional differences which reflect the flexible nature of catalytic resides. CaI, and CaII found at the interface of domain A and C, and CaIII with Na found in the interior of domain B, constitute the metal ion binding sites. CaI is consistent in all α-amylases, however there are differences between the linear trio of CaII, CaIII and Na in other enzymes.
Function
adasdasd
Digestion
texttext [2]
References
- ↑ 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
- ↑ 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
Proteopedia Page Contributors and Editors (what is this?)
Shane Riley, Michal Harel, Joel L. Sussman, Randi Woodbeck, Jaime Prilusky, Alexander Berchansky, Ann Taylor, Andrea Gorrell, David Canner
