Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77

Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review

Published:2014-05-04 Issue:6 Volume:69 Page:705-712
ISSN:0006-3088
Container-title:Biologia
language:en
Short-container-title:Biologia

Author:

Cockburn Darrell,Wilkens Casper,Ruzanski Christian,Andersen Susan,Willum Nielsen Jonas,Smith Alison M.,Field Robert A.,Willemoës Martin,Abou Hachem Maher,Svensson Birte

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Plant Science,Genetics,Molecular Biology,Animal Science and Zoology,Biochemistry,Ecology, Evolution, Behavior and Systematics

Link

http://link.springer.com/content/pdf/10.2478/s11756-014-0373-9.pdf

Reference51 articles.

1. Abe A., Yoshida H., Tonozuka T., Sakano Y. & Kamitori S. 2005. Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligosaccharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages. FEBS J. 272: 6145–6153.

2. Albenne C., Skov L.K., Mirza O., Gajhede M., Feller G., D’Amico S., André G., Potocki-Véronèse G., van der Veen B.A., Monsan P. & Remaud-Simeon M. 2004. Molecular basis of the amylose-like polymer formation catalyzed by Neisseria polysaccharea amylosucrase. J. Biol. Chem. 279: 726–734.

3. Baskaran S., Chikwana V.M., Contreras C.J., Davis K.D., Wilson W.A., Depaoli-Roach A.A., Roach P.J. & Hurley T.D. 2011. Multiple glycogen binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen. J. Biol. Chem. 286: 33999–34006.

4. Bozonnet S., Jensen M.T., Nielsen M.M., Aghajari N., Jensen M.H., Kramhøft B., Willemoës M., Tranier S., Haser R. & Svensson B. 2007. The ‘pair of sugar tongs’ on the noncatalytic domain C of barley α-amylase participates in substrate binding and activity. FEBS J. 274: 5055–5067.

5. Caner S., Nguyen N., Aguda A., Zhang R., Pan Y.T., Withers S.G. & Brayer G. 2013. The structure of Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding-mode. Glycobiology 23: 1075–1083.

Cited by 53 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structural insight into sugar-binding modes of microbial ß-amylase;Biochemical and Biophysical Research Communications;2024-09

2. Probing the function of C-terminal region of recombinant α-amylase BmaN1 from Bacillus megaterium NL3;Microbiology Spectrum;2024-08-30

3. Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis;AMB Express;2024-06-14

4. Accelerated molecular dynamics study to compare the thermostability of Bacillus licheniformis and Aspergillus niger α-amylase;Journal of Biomolecular Structure and Dynamics;2023-11-18

5. Differences in the activities of domain-swapped chimeras of two homologous GH57 glucanotransferases suggest that a glucan-binding DUF could influence donor substrate specificity;2023-08-26