By David A. Bender
The 3rd version of this major textbook builds upon the wonderful starting place of the former versions. It explains and explores the technological know-how underlying our present realizing of the interactions among nutrition and well-being, and the root for present nutritional targets and proposals. It additionally offers a concise and authoritative description of the biochemistry that's necessary to an realizing of the features of food and the significance of vitamin and meals for future health and illness. The dialogue of metabolic pathways and their rules is illustrated by way of transparent and easy diagrams, and is associated all through to dietary and physiological points.
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Additional resources for Introduction to Nutrition and Metabolism
This means that at high concentrations of substrate the enzyme will achieve the same maximum rate of reaction (Vmax) in the presence or absence of inhibitor. It is simply that in the presence of inhibitor the enzyme requires a higher concentration of substrate to achieve saturation – in other words, the Km of the enzyme is higher in the presence of a competitive inhibitor. The effect of a drug that is a competitive inhibitor is that the rate at which product is formed is unchanged, but there is an increase in the concentration of the substrate of the inhibited enzyme in the cell.
By contrast, an enzyme which has a high Km compared Enzymes and metabolic pathways 27 with the normal concentration of substrate in the cell will show a large change in the rate of reaction with relatively small changes in the concentration of substrate. If two enzymes in a cell can both act on the same substrate, catalysing different reactions, the enzyme with the lower Km will be able to bind more substrate, and therefore its reaction will be favoured at relatively low concentrations of substrate.
1), of the substrate. This is because the isomers have different shapes. In nonenzymic chemical reactions they may behave identically, and it may be difficult to distinguish between them. The shape and conformation of the substrate are critically important for binding to an enzyme. The participation of reactive groups at the active site provides specificity not only for the substrates that will bind, but also for the reaction that will be catalysed. 2), isomerization between the D- and L-isomers, or a variety of reactions involving elimination or replacement of the side-chain.