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• W1982132238 endingPage "2198" @default.
• W1982132238 startingPage "2189" @default.
• W1982132238 abstract "In order to clarify the function of the DXDDTA motif in squalene-hopene cyclase and to identify the acidic amino acid residues crucial for the catalysis, site-directed mutagenesis experiments were carried out. The following results were found: (1) residues D374 and D376 work for the initiation of polyolefin cyclization which arises from the proton attack on the terminal double bond; (2) residue D377 stabilizes C-10 carbocation of the initially cyclized A-ring intermediate, leading to subsequent B-ring closure, which was further verified by isolating the partially cyclized monocyclic product; (3) residues D313 and D447 outside the DXDDTA motif were identified as new active sites; (4) the H451 residue is likely to work in the protonated form to enhance the acidity of the carboxyl groups of D374 and/or D376." @default.
• W1982132238 created "2016-06-24" @default.
• W1982132238 creator A5022193625 @default.
• W1982132238 creator A5056901462 @default.
• W1982132238 date "1999-01-01" @default.
• W1982132238 modified "2023-10-09" @default.
• W1982132238 title "Functional Analysis of the DXDDTA Motif in Squalene-Hopene Cyclase by Site-directed Mutagenesis Experiments: Initiation Site of the Polycyclization Reaction and Stabilization Site of the Carbocation Intermediate of the Initially Cyclized A-Ring" @default.
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• W1982132238 doi "https://doi.org/10.1271/bbb.63.2189" @default.
• W1982132238 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10664852" @default.
• W1982132238 hasPublicationYear "1999" @default.
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