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GrainGenes Reference Report: FBS-582-2567

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Reference	FBS-582-2567
Title	Multi-site substrate binding and interplay in barley alpha-amylase 1.
Journal	FEBS Letters
Year	2008
Volume	582
Pages	2567-2571
Author	Nielsen MM [ Show all 7 ]
Abstract	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 Tyr(380), situated on a remote non-catalytic domain, and Tyr(105) 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 Tyr(380) and Tyr(105) is important, albeit not essential for binding, degradation, and multiple attack on polysaccharides, while Tyr(105) predominates in oligosaccharide hydrolysis. Additional delicate structure/function relationships of the secondary site are uncovered using Y380A/H395A, Y380A, and H395A AMY1 mutants.
External Databases	http://dx.doi.org/10.1016/j.febslet.2008.06.027

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