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Exact Product Formation Rates for Stochastic Enzyme Kinetics
https://oist.repo.nii.ac.jp/records/363
https://oist.repo.nii.ac.jp/records/3634eefe7fc-c765-4348-905b-eceb79d20f24
名前 / ファイル | ライセンス | アクション |
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acs.jpcb.6b08891 (1.1 MB)
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ACS Author Choice
https://pubs.acs.org/page/policy/authorchoice_termsofuse.html |
Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2018-04-12 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Exact Product Formation Rates for Stochastic Enzyme Kinetics | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者(英) |
Grima, Ramon
× Grima, Ramon× Leier, André |
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書誌情報 |
en : The Journal of Physical Chemistry B 巻 121, 号 1, p. 13-23, 発行日 2016-12-13 |
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抄録 | ||||||
内容記述タイプ | Other | |||||
内容記述 | 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, such assumption is well-known to break down in the context of cellular biochemistry. Instead, the concentration of available substrate can become rate limiting. Here we use the chemical master equation to obtain expressions for the instantaneous and time averaged rate of product formation without invoking the conventional substrate abundance assumption. The expressions are derived for a broad range of enzyme reaction mechanisms, including those that involve one or many enzyme molecules, require multiple substrates, and exhibit cooperativity and substrate inhibition. Novel results include: (i) the relationship between the average rate of product formation (calculated over the time it takes for the reaction to finish) and the substrate concentration, for a Michaelis–Menten (MM) reaction with one enzyme molecule, is approximately given by a logarithmically corrected MM form; (ii) intrinsic noise decreases the sharpness of cooperative switches but enhances the filtering response of substrate inhibition; (iii) the relationship between the initial average rate of product formation and the initial substrate concentration for a MM reaction with no reversible reaction and with any number of enzyme and substrate molecules is a sum of Michaelis–Menten equations. | |||||
出版者 | ||||||
出版者 | American Chemical Society | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1520-6106 | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1520-5207 | |||||
PubMed番号 | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | PMID | |||||
関連識別子 | info:pmid/27959536 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.1021/acs.jpcb.6b08891 | |||||
権利 | ||||||
権利情報 | © 2016 American Chemical Society | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://pubs.acs.org/doi/full/10.1021/acs.jpcb.6b08891 | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 |