期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 40, 期 -, 页码 33-42出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2016.07.006
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资金
- Danish Council for Independent Research \ Technology and Production Sciences
- Sapere Aude-Research Talent grant
- Danish Council for Independent Research \ Natural Sciences
Starch is a major energy source for all domains of life. Recent advances in structures of starch-degrading enzymes encompass the substrate complex of starch debranching enzyme, the function of surface binding sites in plant isoamylase, details on individual steps in the mechanism of plant disproportionating enzyme and a self-stabilised conformation of amylose accommodated in the active site of plant a-glucosidase. Important inhibitor complexes include a flavonol glycoside, montbretin A, binding at the active site of human pancreatic alpha-amylase and barley limit dextrinase inhibitor binding to the debranching enzyme, limit dextrinase using a new binding mode for cereal protein inhibitors.
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