Page, Michael I. (2003) Past times - the efficiency of enzyme catalysis. Biochemist, 25 (4). pp. 52-53. ISSN 0954-982XMetadata only available from this repository.
Understanding enzyme catalysis on a molecular and energetic basis has fascinated scientists for more than half a century. In addition to their obvious physiological involvement, the incredible efficiency of enzymes continues to intrigue us. In the absence of enzymes, many
reactions of biological interest, e.g. the hydrolysis of proteins, carbohydrates and DNA, have half-lives of hundreds to millions of years. After a substrate is bound at an enzyme’s active site, its halflife is usually milliseconds.The low concentration of enzymes in
cells, which is often at or below the micromolar level, means that a rapid turnover is necessary to produce a significant rate of reaction and many reactions occur at near the diffusion controlled limit. The high catalytic efficiency of enzymes has not been emulated by
artificial systems and therefore many have wondered if they could even be understood by ordinary chemistry.
|Subjects:||Q Science > Q Science (General)|
Q Science > QD Chemistry
|Schools:||School of Applied Sciences|
School of Applied Sciences > Biomolecular Sciences Research Centre
|Depositing User:||Cherry Edmunds|
|Date Deposited:||20 Oct 2008 16:03|
|Last Modified:||24 Nov 2008 15:27|
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