A queueing approach to multi-site enzyme kinetics.

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 Focus

journal_title

Interface focus

authors

Hochendoner P,Ogle C,Mather WH

doi

10.1098/rsfs.2013.0077

subject

Has Abstract

pub_date

2014-06-06 00:00:00

pages

20130077

issue

3

eissn

2042-8898

issn

2042-8901

pii

rsfs20130077

journal_volume

4

pub_type

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