Abstract:
:An alternative theoretical approach to enzyme kinetics that is particularly applicable to single-molecule enzymology is presented. The theory, originated by Van Slyke and Cullen in 1914, develops enzyme kinetics from a "time perspective" rather than the traditional "rate perspective" and emphasizes the nonequilibrium steady-state nature of enzymatic reactions and the significance of small copy numbers of enzyme molecules in living cells. Sigmoidal cooperative substrate binding to slowly fluctuating, monomeric enzymes is shown to arise from association pathways with very small probability but extremely long passage time, which would be disregarded in the traditional rate perspective: A single enzyme stochastically takes alternative pathways in serial order rather than different pathways in parallel. The theory unifies dynamic cooperativity and Hopfield-Ninio's kinetic proofreading mechanism for specificity amplification.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Qian Hdoi
10.1529/biophysj.108.131771subject
Has Abstractpub_date
2008-07-01 00:00:00pages
10-7issue
1eissn
0006-3495issn
1542-0086pii
S0006-3495(08)70280-7journal_volume
95pub_type
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