Proteinaceous α-amylase inhibitors

✍ Scribed by Birte Svensson; Kenji Fukuda; Peter K. Nielsen; Birgit C. Bønsager

• Publisher: Elsevier Science
• Year: 2004
• Tongue: English
• Weight: 954 KB
• Volume: 1696
• Category: Article
• ISSN: 1570-9639
• DOI: 10.1016/j.bbapap.2003.07.004

✦ Synopsis

Proteins that inhibit a-amylases have been isolated from plants and microorganisms. These inhibitors can have natural roles in the control of endogenous a-amylase activity or in defence against pathogens and pests; certain inhibitors are reported to be antinutritional factors. The a-amylase inhibitors belong to seven different protein structural families, most of which also contain evolutionary related proteins without inhibitory activity. Two families include bifunctional inhibitors acting both on a-amylases and proteases. High-resolution structures are available of target a-amylases in complex with inhibitors from five families. These structures indicate major diversity but also some similarity in the structural basis of a-amylase inhibition. Mutational analysis of the mechanism of inhibition was performed in a few cases and various protein engineering and biotechnological approaches have been outlined for exploitation of the inhibitory function.