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• W2033717022 startingPage "2509" @default.
• W2033717022 abstract "The catalytic effects of perdeuterating the pyridoxal phosphate-dependent enzyme alanine racemase from Geobacillus stearothermophilus are reported. The mass of the heavy perdeuterated form is ∼5.5% greater than that of the protiated form, causing kinetic isotope effects (KIEs) of ∼1.3 on kcat and kcat/KM for both l- and d-alanine. These values increase when Cα-deuterated alanine is used as the substrate. The heavy-enzyme KIEs of ∼3 on kcat/KM with deuterated substrates are greater than the product of the individual heavy-enzyme and primary substrate KIEs. This breakdown of the rule of the geometric mean is likely due to coupled motion between the protein and the proton-transfer reaction coordinate in the rate-limiting step. These data implicate a direct role for protein vibrational motions in barrier crossing for proton-transfer steps in alanine racemase." @default.
• W2033717022 created "2016-06-24" @default.
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• W2033717022 date "2013-02-05" @default.
• W2033717022 modified "2023-09-23" @default.
• W2033717022 title "Heavy-Enzyme Kinetic Isotope Effects on Proton Transfer in Alanine Racemase" @default.
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• W2033717022 doi "https://doi.org/10.1021/ja3101243" @default.
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