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• W2964314511 abstract "Recent fluorescence spectroscopy measurements of the turnover time distribution of single-enzyme turnover kinetics of β-galactosidase provide evidence of Michaelis-Menten kinetics at low substrate concentration. However, at high substrate concentrations, the dimensionless variance of the turnover time distribution shows systematic deviations from the Michaelis-Menten prediction. This difference is attributed to conformational fluctuations in both the enzyme and the enzyme-substrate complex and to the possibility of both parallel- and off-pathway kinetics. Here, we use the chemical master equation to model the kinetics of a single fluctuating enzyme that can yield a product through either parallel- or off-pathway mechanisms. An exact expression is obtained for the turnover time distribution from which the mean turnover time and randomness parameters are calculated. The parallel- and off-pathway mechanisms yield strikingly different dependences of the mean turnover time and the randomness parameter on the substrate concentration. In the parallel mechanism, the distinct contributions of enzyme and enzyme-substrate fluctuations are clearly discerned from the variation of the randomness parameter with substrate concentration. From these general results, we conclude that an off-pathway mechanism, with substantial enzyme-substrate fluctuations, is needed to rationalize the experimental findings of single-enzyme turnover kinetics of β-galactosidase." @default.
• W2964314511 created "2019-07-30" @default.
• W2964314511 creator A5009663694 @default.
• W2964314511 creator A5023383324 @default.
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• W2964314511 date "2015-06-30" @default.
• W2964314511 modified "2023-10-17" @default.
• W2964314511 title "Parallel versus Off-Pathway Michaelis–Menten Mechanism for Single-Enzyme Kinetics of a Fluctuating Enzyme" @default.
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• W2964314511 doi "https://doi.org/10.1021/acs.jpcb.5b03752" @default.
• W2964314511 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26079147" @default.
• W2964314511 hasPublicationYear "2015" @default.
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