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Extra resources for An Introduction to the Khasia Language, Comprising Grammar, Selections for Reading, and a Vocabulary
Thus, if an enzyme is able to bind its substrate in a less favourable but more reactive conformation, then it is able to realise additional rate acceleration in this way. Analysis of this type requires detailed insight from X-ray crystallography, so it is not surprising that there are only a few well-documented examples of this phenomenon. One other is that of lysozyme, which we shall see in Chapter 5. However, it is possible that this strategy may be used in many enzyme-catalysed reactions. 21 Strained substrate conformation in carboxypeptidase A.
43, 219–410. R. J. Snider (2001) The depth of chemical time and the power of enzymes as catalysts. Acc. Chem. , 34, 938–45. M. J. H. W. Dijkstra (1991) Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes. , 10, 1297–302. F. Pries, J. Kingma, M. Pentenga, G. M. P. B. Janssen (1994) Site-directed mutagenesis and oxygen isotope incorporation studies of the nucleophilic aspartate of haloalkane dehalogenase. Biochemistry, 33, 1242–7. P. J. Benkovic (1998) Stretching exercises – Xexibility in dihydrofolate reductase catalysis.
8d, the enzyme can bind selectively the transition state, then it can reduce the activation energy and hence speed up the reaction. The conclusion of this thought experiment is that in order to achieve optimal catalysis, enzymes should selectively bind the transition state, rather than the substrate. Hence, it is not advantageous for enzymes to bind their substrates too tightly. 3). Typical KM values for enzymes are in the mm –mm range (10À3 ---10À6 m), whereas dissociation constants for binding proteins and antibodies whose function is to bind small molecules tightly are in the range nm –pm (10À9 ---10À12 m).