{"title":"Phosphotriesterase: an enzyme in search of its natural substrate.","authors":"F M Raushel, H M Holden","doi":"10.1002/9780470123201.ch2","DOIUrl":null,"url":null,"abstract":"<p><p>The bacterial PTE is able to catalyze the hydrolysis of a wide range of organophosphate nerve agents. The active site has been shown to consist of a unique binuclear metal center that has evolved to deliver hydroxide to the site of bond cleavage. The reaction rate for the hydrolysis of activated substrates such as paraoxon is limited by product release or an associated protein conformational change.</p>","PeriodicalId":50865,"journal":{"name":"Advances in Enzymology and Related Subjects","volume":"74 ","pages":"51-93"},"PeriodicalIF":0.0000,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/9780470123201.ch2","citationCount":"71","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Advances in Enzymology and Related Subjects","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/9780470123201.ch2","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 71
Abstract
The bacterial PTE is able to catalyze the hydrolysis of a wide range of organophosphate nerve agents. The active site has been shown to consist of a unique binuclear metal center that has evolved to deliver hydroxide to the site of bond cleavage. The reaction rate for the hydrolysis of activated substrates such as paraoxon is limited by product release or an associated protein conformational change.
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