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• W2126395871 abstract "1. Substrates or competitive inhibitors produced an increase in the fluorescence of yeast enolase (2-phospho-d-glycerate hydro-lyase, EC 4.2.1.11) in the presence of a high concentration (0.01 M) of Mg2+ or other activating metal ions. 2. The increase in fluorescence is ascribed to a decrease in quenching of one or more tryptophans in the enzyme upon binding metal ion and substrate. 3. Fluorometric titrations of the enzyme with substrate in the presence of excess Mg2+ have given substrate binding constants in agreement with substrate Michaelis constants. 4. Titrations with Mg2+ in the presence of excess substrate show two binding sites. The site with the smallest dissociation constant is identical with the site associated with structural changes in the enzyme when the metal ion is bound. The second site appears only in the presence of substrate and is not connected with enzymic activity, but perhaps with actual inhibition." @default.
• W2126395871 created "2016-06-24" @default.
• W2126395871 creator A5048918898 @default.
• W2126395871 date "1971-10-01" @default.
• W2126395871 modified "2023-10-03" @default.
• W2126395871 title "The increase in yeast enolase fluorescence produced by substrates and competitive inhibitors in the presence of excess Mg2+" @default.
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• W2126395871 doi "https://doi.org/10.1016/0005-2744(71)90140-9" @default.
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