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Sweet almond β-glucosidase is an enzyme (EC 3.2.1.21) that catalyzes the hydrolysis of glycosidic bonds at the non-reducing end of β-D-glucosides and oligosaccharides, releasing glucose. It is a member of glycoside hydrolase family 1, featuring an α/β TIM barrel structure as inferred by homology modeling, and consists of 544 amino acids (molecular mass ~62 kDa for monomers, with the native form as a dimer). The enzyme is active over a wide pH range (optimum pH ~5.5), stable below 50°C, and utilized in carbohydrate structure analysis, plant biochemistry, and research into enzyme inhibition. Historically known as "emulsin," it serves as a model for studying glycosidase mechanisms and inhibitor development. In plants, it is relevant for cell wall modification, defense, and aroma release, but it is not directly targeted in therapeutic interventions.
Competitive inhibition by cyclitol-azole compounds and gluco-azoles via mimicry of transition state or substrate conformation Mechanism-based irreversible inhibition by molecules forming stable enzyme intermediates
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