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• W1900100449 abstract "This chapter focuses on the contributions that domain interactions and calcium have on the properties of carbohydrate-active enzymes. It also focuses on the interactions between domains in one of the largest cellulosomal catalytic components, cellobiohydrolase A (CbhA). CbhA is the only Clostridium thermocellum cellulosomal enzyme whose domain interactions and role of calcium have been studied in detail by different techniques including genetic manipulations, crystallography, circular dichroism (CD) spectroscopy, and differential scanning calorimetry (DSC). In the presence of calcium, the stabilities of the domains are relatively independent, while in the absence of Ca2+, domain interactions play a stabilizing role. Thermal unfolding in buffer assumes coexistence of protein molecules (i) with calcium bound to all binding sites, (ii) with partially lost calcium, and (iii) without calcium. This chapter describes modular architectures of carbohydrate-active enzymes and analyzes the role of interdomain interactions in the structure, stability, and functionality of the interesting and important proteins. Even linkers between domains are crucial for the functionality of carbohydrate-active enzyme in that they serve as “molecular springs” allowing catalytic sites to reach and hydrolyze new glycosidic bonds, while the CBM is still bound to the substrate surface. As a general conclusion one may say that domain interactions in modular carbohydrate hydrolytic enzymes enhance the activity of the catalytic domains of the enzymes." @default.
• W1900100449 created "2016-06-24" @default.
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• W1900100449 date "2014-04-30" @default.
• W1900100449 modified "2023-09-26" @default.
• W1900100449 title "Contribution of Domain Interactions and Calcium Binding to the Stability of Carbohydrate-Active Enzymes" @default.
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• W1900100449 doi "https://doi.org/10.1128/9781555815547.ch9" @default.
• W1900100449 hasPublicationYear "2014" @default.
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