A New Mechanism for Ethanol Oxidation Mediated by Cytochrome P450 2E1: Bulk Polarity of the Active Site Makes a Difference | Zendy

Wang Yong | Zendy; Yang  Chuanlu | Zendy; Wang Hongming | Zendy; Han  Keli | Zendy; Shaik Sason | Zendy

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A New Mechanism for Ethanol Oxidation Mediated by Cytochrome P450 2E1: Bulk Polarity of the Active Site Makes a Difference

Author(s) -

Wang Yong,

Yang Chuanlu,

Wang Hongming,

Han Keli,

Shaik Sason

Publication year - 2007

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.200600510

Subject(s) - cyp2e1 , ethanol , cytochrome p450 , chemistry , mechanism (biology) , biochemistry , population , metabolism , physics , medicine , environmental health , quantum mechanics

Breaking the habit . A new mechanism, called reversed dual hydrogen abstraction (R‐DHA), is presented for ethanol oxidation by cytochrome P450 2E1 (CYP2E1). It is shown that the competition of R‐DHA with the consensus mechanism ( gem ‐diol) is modulated by the ethanol population in the enzyme pocket. Thus, as a response to growing blood ethanol level, CYP2E1 adapts its ethanol metabolism by a mechanistic switch from gem ‐diol to R‐DHA.

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