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- W1491283823 abstract "Abstract Studies on the exchange of oxygen catalyzed by Escherichia coli glutaminase between water and substrates are reported. The rates of the virtual hydrolysis of glutamic acid, i.e. the exchange of 18O between water and the γ-carboxyl oxygen atoms, allow determination of the Km and kcat values for this substrate. These values are 2.9 mm and 5080 sec-1, respectively, at 25° and pH 5.0. The kcat, which is shown to be the number of complete catalytic cycles of the enzyme per sec, is the highest of any known substrate of this enzyme, and among the highest for an enzyme-catalyzed reaction of a carboxylic derivative. Glutaminase does not catalyze exchange between the γ-carbonyl oxygen atoms of glutamine and water." @default.
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- W1491283823 date "1968-03-01" @default.
- W1491283823 modified "2023-09-29" @default.
- W1491283823 title "Glutaminase of Escherichia coli" @default.
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- W1491283823 doi "https://doi.org/10.1016/s0021-9258(18)93596-9" @default.
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