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• W2007424462 abstract "ATP:cob(I)alamin adenosyltransferases (ACAs) catalyze the transfer of the 5′-deoxyadenosyl moiety from ATP to the upper axial ligand position of cobalamin in the synthesis of coenzyme B12. For the ACA-catalyzed reaction to proceed, cob(II)alamin must be reduced to cob(I)alamin in the enzyme active site. This reduction is facilitated through the generation of a four-coordinate cob(II)alamin intermediate on the enzyme. We have determined the high-resolution crystal structure of a human-type ACA from Lactobacillus reuteri with a four-coordinate cob(II)alamin bound in the enzyme active site and with the product, adenosylcobalamin, partially occupied in the active site. The assembled structures represent snapshots of the steps in the ACA-catalyzed formation of the cobalt−carbon bond of coenzyme B12. The structures define the corrinoid binding site and provide visual evidence for a base-off, four-coordinate cob(II)alamin intermediate. The complete structural description of ACA-mediated catalysis reveals the molecular features of four-coordinate cob(II)alamin stabilization and provides additional insights into the molecular basis for dysfunction in human patients suffering from methylmalonic aciduria." @default.
• W2007424462 created "2016-06-24" @default.
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• W2007424462 date "2008-05-01" @default.
• W2007424462 modified "2023-10-02" @default.
• W2007424462 title "Structural Characterization of a Human-Type Corrinoid Adenosyltransferase Confirms That Coenzyme B₁₂ Is Synthesized through a Four-Coordinate Intermediate" @default.
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• W2007424462 doi "https://doi.org/10.1021/bi800132d" @default.
• W2007424462 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6647012" @default.
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• W2007424462 hasPublicationYear "2008" @default.
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