Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Certain starch hydrolases possess secondary carbohydrate binding sites outside of the active site, suggesting that multi-site substrate interactions are functionally significant. In barley alpha-amylase both Tyr380, situated on a remote non-catalytic domain, and Tyr105 in subsite -6 of the active site cleft are principal carbohydrate binding residues. The dual active site/secondary site mutants Y105A/Y380A and Y105A/Y380M show that each of Tyr380 and Tyr105 is important, albeit not essential for binding, degradation, and multiple attack on polysaccharides, while Tyr105 predominates in oligosaccharide hydrolysis. Additional delicate structure/function relationships of the secondary site are uncovered using Y380A/H395A, Y380A, and H395A AMY1 mutants.
Multi-site substrate binding and interplay in barley alpha-amylase 1.,Nielsen MM, Seo ES, Bozonnet S, Aghajari N, Robert X, Haser R, Svensson B FEBS Lett. 2008 Jul 23;582(17):2567-71. Epub 2008 Jun 25. PMID:18588886[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nielsen MM, Seo ES, Bozonnet S, Aghajari N, Robert X, Haser R, Svensson B. Multi-site substrate binding and interplay in barley alpha-amylase 1. FEBS Lett. 2008 Jul 23;582(17):2567-71. Epub 2008 Jun 25. PMID:18588886 doi:10.1016/j.febslet.2008.06.027
