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- W1120076945 abstract "BKDK specifically phosphorylates and inactivates the E1 subunit (branched-chain α-ketoacid dehydrogenase) of the branched-chain α-ketoacid dehydrogenase complex. This complex catalyses the committed step in the oxidative disposal of branched chain amino acids (leucine, isoleucine, and valine). Although BKDK is a serine PK according to the sites phosphorylated (S293 and S303 in the El a subunit), it lacks significant sequence similarity with known eukaryotic Ser/Thr PKs. A greater degree of similarity exists with members of the prokaryotic histidine PK family. Four subdomains (I, II, III, and IV) of these kinases are highly conserved in all members of this family. Considerable sequence similarity exists in BKDK within all four of these subdomains. The enzyme has been assayed by the rate of ATP-dependent inactivation of the branched-chain a-ketoacid dehydrogenase complex, and by the rate of incorporation of 32P from [γ32P]ATP into its E1 α subunit." @default.
- W1120076945 created "2016-06-24" @default.
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- W1120076945 date "1995-01-01" @default.
- W1120076945 modified "2023-09-23" @default.
- W1120076945 title "BKDK" @default.
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- W1120076945 doi "https://doi.org/10.1016/b978-012324719-3/50137-0" @default.
- W1120076945 hasPublicationYear "1995" @default.
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