We analyze the standard model of enzyme-catalyzed reactions at various substrate-enzyme ratios by adopting a different scaling scheme and computational procedure. The regions of validity of the quasi-steady-state approximation are noted. Certain prevalent conditions are checked and compared against the actual findings. Efficacies of a few other measures, obtained from the present work, are highlighted. Some recent observations are rationalized, particularly at moderate and high enzyme concentrations. © 2013 Springer Science+Business Media New York.

S DHATT

K BHATTACHARYYA

Fulltext

University of Calcutta (informally known as Calcutta University or CU) is a collegiate public state university located in Kolkata, West Bengal, India.&nbsp;Within India it is recognized as a &quot;Five-Star University&quot; and accredited &quot;A&quot; Grade by National Assessment and Accreditation Council.

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The University of Calcutta has secured the Fifth position among the Universities of India in the prestigious &quot;Indian University Ranking 2019&quot; list, released by the NIRF of the Ministry of Human Resource Development, Government of India.

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It was established on 24 January 1857, and was one of the first institutions in Asia to be established as a multidisciplinary and Western-style university. Its alumni and faculty include several heads of state, heads of government, social reformers, prominent artists, only academy award winner and Dirac medal winner in India, many Fellows of the Royal Society and five Nobel laureates as of 2019 which is highest in South Asia.

University Of Calcutta

Journal of Mathematical Chemistry

Michaelis–Menten (MM) scheme serves as the benchmark model to characterize enzyme kinetics. Standard theoretical analyses of product formation rate for such a scheme are based on the quasi-steady-state approximation (QSSA). There exist well-established criteria, applicable to both deterministic and stochastic scenarios, to judge the validity of QSSA. These criteria are given in terms of initial concentrations and rate parameters. In this work, we present a complementary stochastic signature to investigate the legitimacy of QSSA in MM kinetics with a finite copy number of species. Our condition is formulated in terms of the time-evolution of the product of coefficients of variation of suitable pair of species population. It can be measured, in principle, from time-series data of molecular population, avoiding estimation of model kinetic parameters. © 2019, Springer Nature Switzerland AG.

Efficacy of quasi-steady-state approximation in Michaelisâ€“Menten kinetics: a stochastic signature

A divergent perturbation series is known to yield very unreliable results for observables even at moderate coupling strengths. One of the most popular techniques in handling such series is to express them as rational functions, but it is often faithful only for small coupling. We outline here how one can gain considerable advantages in the large-coupling regime by properly embedding known asymptotic scaling relations for selected observables during construction of the aforesaid Padé approximants. Three new bypass routes are explored in this context. The first approach involves a weighted geometric mean of two neighboring PA. The second idea is to consider series for specific ratios of observables. The third strategy is to express observables as functionals of the total energy in the form of series expansions. Symanzik's scaling relation, and the virial and Hellmann-Feynman theorems, are used at appropriate places to aid each of the strategies. Pilot calculations on the ground-state perturbation series of certain observables for the quartic anharmonic oscillator problem reveal readily the benefit and novelty. © 2012 Wiley Periodicals, Inc.

International Journal of Quantum Chemistry

Embedding scaling relations in PadÃ© approximants: Detours to tame divergent perturbation series

Biochemistry

The Original Michaelis Constant: Translation of the 1913 Michaelis–Menten Paper

The Journal of Physical Chemistry A

Reactant Stationary Approximation in Enzyme Kinetics

Journal of Theoretical Biology

Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis–Menten constant

The total quasi-steady-state approximation is valid for reversible enzyme kinetics

Single-substrate enzyme kinetics: The quasi-steady-state approximation and beyond

Journal	Data powered by TypesetJournal of Mathematical Chemistry
Publisher	Data powered by TypesetSPRINGER
ISSN	0259-9791
Open Access	Yes