Abstract:
:Multi-site enzymes, defined as where multiple substrate molecules can bind simultaneously to the same enzyme molecule, play a key role in a number of biological networks, with the Escherichia coli protease ClpXP a well-studied example. These enzymes can form a low latency 'waiting line' of substrate to the enzyme's catalytic core, such that the enzyme molecule can continue to collect substrate even when the catalytic core is occupied. To understand multi-site enzyme kinetics, we study a discrete stochastic model that includes a single catalytic core fed by a fixed number of substrate binding sites. A natural queueing systems analogy is found to provide substantial insight into the dynamics of the model. From this, we derive exact results for the probability distribution of the enzyme configuration and for the distribution of substrate departure times in the case of identical but distinguishable classes of substrate molecules. Comments are also provided for the case when different classes of substrate molecules are not processed identically.
journal_name
Interface Focusjournal_title
Interface focusauthors
Hochendoner P,Ogle C,Mather WHdoi
10.1098/rsfs.2013.0077subject
Has Abstractpub_date
2014-06-06 00:00:00pages
20130077issue
3eissn
2042-8898issn
2042-8901pii
rsfs20130077journal_volume
4pub_type
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