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Carbohydrase is the name of a set of enzymes that catalyze five types of reactions, turning carbohydrates into simple sugars, from the large family of glycosidases. [ 1 ] Carbohydrases are produced in the pancreas , salivary glands and small intestine , breaking down polysaccharides .
A single glucose molecule is cleaved from a branch of glycogen, and is transformed into glucose-1-phosphate during this process. [1] This molecule can then be converted to glucose-6-phosphate, an intermediate in the glycolysis pathway. [1] Glucose-6-phosphate can then progress through glycolysis. [1]
This gives a total of four FAD molecules and four acyl-CoA substrate binding sites per enzyme. FAD is bound between the three domains of the monomer, where only the nucleotide portion is accessible. FAD binding contributes significantly to overall enzyme stability. The acyl-CoA substrate is bound completely within each monomer of the enzyme ...
An example of a coupled reaction is the phosphorylation of fructose-6-phosphate to form the intermediate fructose-1,6-bisphosphate by the enzyme phosphofructokinase accompanied by the hydrolysis of ATP in the pathway of glycolysis. The resulting chemical reaction within the metabolic pathway is highly thermodynamically favorable and, as a ...
where + (forward rate constant), (reverse rate constant), and (catalytic rate constant) denote the rate constants, [14] the double arrows between A (substrate) and EA (enzyme-substrate complex) represent the fact that enzyme-substrate binding is a reversible process, and the single forward arrow represents the formation of P (product).
The biosynthesis of aspartate is a one step reaction that is catalyzed by a single enzyme. The enzyme aspartate aminotransferase catalyzes the transfer of an amino group from aspartate onto α-ketoglutarate to yield glutamate and oxaloacetate . [ 41 ]
Nearly all KS1 members are produced by bacteria, with a few formed by eukaryota and only one by an archaeon. There are 12 subfamilies. The dominant enzyme in the KS1 family is 3-ketoacyl-ACP synthase III (KAS III), also known as 3-oxoacyl-ACP synthase III and β-ketoacyl-ACP synthase III, and is defined as EC 2.3.1.180. [5] [1]
However, the proposed connection between a single gene and a single protein enzyme outlived the protein theory of gene structure. In a 1948 paper, Norman Horowitz named the concept the "one gene–one enzyme hypothesis". [2] Although influential, the one gene–one enzyme hypothesis was not unchallenged.