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• W2123207812 startingPage "633" @default.
• W2123207812 abstract "Heterotetrameric sarcosine oxidase is a flavoprotein that catalyses the oxidative demethylation of sarcosine. It is thought that the dehydrogenated substrate is the anionic form of sarcosine. To verify this assumption, the rate of flavin-adenine dinucleotide (FAD) reduction (kred) was analysed using protiated and deuterated sarcosine (N-methyl-d3-Gly) at various pH values using stopped-flow method. By increasing the pH from 6.2 to 9.8, kred increased for both substrates and reached a plateau, but the pKa value (reflecting the ionization of the enzyme–substrate complex) was 6.8 and 7.1 for protiated and deuterated sarcosine, respectively, and the kinetic isotope effect of kred decreased from approximately 19 to 8, indicating deprotonation of the bound sarcosine. The kred/Kd (Kd, sarcosine dissociation constant) increased with increasing pH and reached a plateau. The pK (reflecting the ionization of free enzyme or free sarcosine) was 7.0 for both substrates, suggesting deprotonation of the βLys358 residue, which has a pKa of 6.7, as the pKa of the free sarcosine amine proton was determined to be approximately 10.1. These results indicate that the amine proton of sarcosine is transferred to the unprotonated Lys residue in the enzyme–substrate complex." @default.
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• W2123207812 date "2012-04-23" @default.
• W2123207812 modified "2023-09-27" @default.
• W2123207812 title "Deuterium kinetic isotope effects in heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96: the anionic form of the substrate in the enzyme–substrate complex is a reactive species" @default.
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• W2123207812 doi "https://doi.org/10.1093/jb/mvs045" @default.
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