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Pregled bibliografske jedinice broj: 864140

Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production


Bonačić Lošić, Željana; Donđivić, Tomislav; Juretić, Davor
Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production // Journal of biological physics, 43 (2017), 1; 69-86 doi:10.1007/s10867-016-9434-3 (međunarodna recenzija, članak, znanstveni)


CROSBI ID: 864140 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production

Autori
Bonačić Lošić, Željana ; Donđivić, Tomislav ; Juretić, Davor

Izvornik
Journal of biological physics (0092-0606) 43 (2017), 1; 69-86

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Enzyme kinetic scheme ; Triosephosphate isomerase ; Maximum entropy production ; Kinetic constants

Sažetak
Triosephosphate isomerase (TIM) is often described as a fully evolved housekeeping enzyme with near-maximal possible reaction rate. The assumption that an enzyme is perfectly evolved has not been easy to confirm or refute. In this paper, we use maximization of entropy production within known constraints to examine this assumption by calculating steady-state cyclic flux, corresponding entropy production, and catalytic activity in a reversible four-state scheme of TIM functional states. The maximal entropy production (MaxEP) requirement for any of the first three transitions between TIM functional states leads to decreased total entropy production. Only the MaxEP requirement for the product (R-glyceraldehyde-3-phosphate) release step led to a 30% increase in enzyme activity, specificity constant kcat/KM, and overall entropy production. The product release step, due to the TIM molecular machine working in the physiological direction of glycolysis, has not been identified before as the rate-limiting step by using irreversible thermodynamics. Together with structural studies, our results open the possibility for finding amino acid substitutions leading to an increased frequency of loop six opening and product release.

Izvorni jezik
Engleski

Znanstvena područja
Fizika



POVEZANOST RADA


Projekti:
HRZZ-IP-2013-11-8481 - Biofizikalni dizajn antimikrobnih peptida i inovativni molekularni deskriptori (BioAmpMode) (Vukičević, Damir, HRZZ - IP-2013-11) ( POIROT)

Ustanove:
Prirodoslovno-matematički fakultet, Split,
Mediteranski institut za istraživanje života

Citiraj ovu publikaciju

Bonačić Lošić, Željana; Donđivić, Tomislav; Juretić, Davor
Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production // Journal of biological physics, 43 (2017), 1; 69-86 doi:10.1007/s10867-016-9434-3 (međunarodna recenzija, članak, znanstveni)
Bonačić Lošić, Ž., Donđivić, T. & Juretić, D. (2017) Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production. Journal of biological physics, 43 (1), 69-86 doi:10.1007/s10867-016-9434-3.
@article{article, year = {2017}, pages = {69-86}, DOI = {10.1007/s10867-016-9434-3}, keywords = {Enzyme kinetic scheme, Triosephosphate isomerase, Maximum entropy production, Kinetic constants}, journal = {Journal of biological physics}, doi = {10.1007/s10867-016-9434-3}, volume = {43}, number = {1}, issn = {0092-0606}, title = {Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production}, keyword = {Enzyme kinetic scheme, Triosephosphate isomerase, Maximum entropy production, Kinetic constants} }
@article{article, year = {2017}, pages = {69-86}, DOI = {10.1007/s10867-016-9434-3}, keywords = {Enzyme kinetic scheme, Triosephosphate isomerase, Maximum entropy production, Kinetic constants}, journal = {Journal of biological physics}, doi = {10.1007/s10867-016-9434-3}, volume = {43}, number = {1}, issn = {0092-0606}, title = {Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production}, keyword = {Enzyme kinetic scheme, Triosephosphate isomerase, Maximum entropy production, Kinetic constants} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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