Zobrazeno 1 - 10
of 32
pro vyhledávání: '"diffusion‐limited enzyme"'
Autor:
Meng‐Hsuan Wu, Cheng‐Chung Lee, An‐Shan Hsiao, Su‐May Yu, Andrew H.‐J. Wang, Tuan‐Hua David Ho
Publikováno v:
FEBS Open Bio, Vol 8, Iss 8, Pp 1230-1246 (2018)
A high‐efficiency laccase, DLac, was isolated from Cerrena sp. RSD1. The kinetic studies indicate that DLac is a diffusion‐limited enzyme. The crystal structure of DLac was determined to atomic resolution, and its overall structure shares high ho
Externí odkaz:
https://doaj.org/article/7cb7cac5457f474eb8a364426d1037f1
Autor:
Narupat Hongdilokkul, Pimchai Chaiyen, Parinthon Nearmnala, Watanalai Panbangred, Manutsawee Thanaburakorn
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
Scientific Reports
Scientific Reports
In vivo selection systems are powerful tools for directed evolution of enzymes. The selection pressure of the systems can be tuned by regulating the expression levels of the catalysts. In this work, we engineered a selection system for laboratory evo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c030b05d92c10ae898e347cfdc453ea
https://doaj.org/article/dab1a6356dce467a8b7038d09ed89775
https://doaj.org/article/dab1a6356dce467a8b7038d09ed89775
Autor:
Ramon Grima, André Leier
Publikováno v:
Grima, R & Laier, A 2016, ' Exact Product Formation Rates for Stochastic Enzyme Kinetics ', The Journal of physical chemistry, vol. 121, no. 1, pp. 13-23 . https://doi.org/10.1021/acs.jpcb.6b08891
The rate of product formation is an important measure of the speed of enzyme reactions. Classical studies of enzyme reactions have been conducted in dilute solutions and under conditions that justified the substrate abundance assumption. However, suc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cbab53797d5d0f27d327279c3fd008d
https://www.pure.ed.ac.uk/ws/files/30238426/acs_2Ejpcb_2E6b08891.pdf
https://www.pure.ed.ac.uk/ws/files/30238426/acs_2Ejpcb_2E6b08891.pdf
Autor:
T. D. H. Bugg
Publikováno v:
Introduction to Enzyme and Coenzyme Chemistry, Second Edition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a0f9a97affe2cf6eca7d4bc0f258ae5
https://doi.org/10.1002/9781118348970.ch3
https://doi.org/10.1002/9781118348970.ch3
Publikováno v:
Journal of the American Chemical Society. 131:5648-5658
The protein enzyme ribonuclease A (RNaseA) cleaves RNA with catalytic perfection, although with little sequence specificity, by a divalent metal ion (M(2+))-independent mechanism in which a pair of imidazoles provides general acid and base catalysis,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35a9c4ddd3006ddbf3587449b2fc7c49
https://doi.org/10.1021/ja900125n
https://doi.org/10.1021/ja900125n
Publikováno v:
Chemical Reviews. 106:3188-3209
Most enzymatic reactions have very large and remarkably similar apparent second-order rate constants, kcat/KM, at mean values of about 107 M−1 s−1 with kcat in the range of 10–1000 s−1.1–3 In fact, many reactions approach the diffusional en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6af330f72667fd3e5790b81909038acf
https://doi.org/10.1021/cr050293k
https://doi.org/10.1021/cr050293k
Akademický článek
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Publikováno v:
Biophysical Journal. 106(2)
In cells, many enzyme-catalyzed reactions are coupled as a series of biochemical steps. Thus, the reaction rate is dependent on the kinetics of intermediate reaction steps. In this work, we study the case of two coupled enzyme reactions, where the pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ad8eabf888f537b904aef90a5909245
Autor:
Irina V. Gopich, Attila Szabo
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 110(49)
The simplest way to describe the influence of the relative diffusion of the reactants on the time course of bimolecular reactions is to modify or renormalize the phenomenological rate constants that enter into the rate equations of conventional chemi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c66c8063c6501f9dde32a867a0e55ae0
https://pubmed.ncbi.nlm.nih.gov/24248348
https://pubmed.ncbi.nlm.nih.gov/24248348
Akademický článek
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