Journal article
The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs
Laboratoire de BioCristallographie, Institut de Biologie et Chimie des Protéines, UMR 5086-CNRS/UCBL1, 7 Passage du Vercors, F-69367 Lyon cedex 07, France.1
Though the three-dimensional structures of barley alpha-amylase isozymes AMY1 and AMY2 are very similar, they differ remarkably from each other in their affinity for Ca(2+) and when interacting with substrate analogs. A surface site recognizing maltooligosaccharides, not earlier reported for other alpha-amylases and probably associated with the different activity of AMY1 and AMY2 toward starch granules, has been identified.
It is located in the C-terminal part of the enzyme and, thus, highlights a potential role of domain C. In order to scrutinize the possible biological significance of this domain in alpha-amylases, a thorough comparison of their three-dimensional structures was conducted. An additional role for an earlier-identified starch granule binding surface site is proposed, and a new calcium ion is reported.
| Language: | English |
|---|---|
| Year: | 2003 |
| Pages: | 973-84 |
| ISSN: | 18784186 and 09692126 |
| Types: | Journal article |
| DOI: | 10.1016/s0969-2126(03)00151-5 |
Acarbose Amino Acid Sequence Calcium Carbohydrate Metabolism Carbohydrates Catalysis Crystallography, X-Ray Hordeum Hydrogen Bonding Hydrophobic and Hydrophilic Interactions Isoenzymes Ligands Models, Molecular Molecular Sequence Data Molecular Structure Pichia Protein Binding Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Starch Substrate Specificity Tyrosine Water alpha-Amylases
