Structural biology of starch-degrading enzymes and their regulation
(2016) In Current Opinion in Structural Biology 40. p.33-42- Abstract
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 α-glucosidase. Important inhibitor complexes include a flavonol glycoside, montbretin A, binding at the active site of human pancreatic α-amylase and barley limit dextrinase inhibitor binding to the debranching enzyme, limit dextrinase using a new binding mode for cereal protein inhibitors.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/cdb4f61e-5352-48e0-9ed8-873c9416b4a1
- author
- Møller, Marie Sofie LU and Svensson, Birte
- organization
- publishing date
- 2016-10-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Current Opinion in Structural Biology
- volume
- 40
- pages
- 10 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:84979695897
- pmid:27450115
- wos:000390744700007
- ISSN
- 0959-440X
- DOI
- 10.1016/j.sbi.2016.07.006
- language
- English
- LU publication?
- yes
- id
- cdb4f61e-5352-48e0-9ed8-873c9416b4a1
- date added to LUP
- 2016-10-17 10:37:23
- date last changed
- 2024-04-05 06:46:29
@article{cdb4f61e-5352-48e0-9ed8-873c9416b4a1,
abstract = {{<p>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 α-glucosidase. Important inhibitor complexes include a flavonol glycoside, montbretin A, binding at the active site of human pancreatic α-amylase and barley limit dextrinase inhibitor binding to the debranching enzyme, limit dextrinase using a new binding mode for cereal protein inhibitors.</p>}},
author = {{Møller, Marie Sofie and Svensson, Birte}},
issn = {{0959-440X}},
language = {{eng}},
month = {{10}},
pages = {{33--42}},
publisher = {{Elsevier}},
series = {{Current Opinion in Structural Biology}},
title = {{Structural biology of starch-degrading enzymes and their regulation}},
url = {{http://dx.doi.org/10.1016/j.sbi.2016.07.006}},
doi = {{10.1016/j.sbi.2016.07.006}},
volume = {{40}},
year = {{2016}},
}