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• W2000434472 abstract "Significance Bifunctional enzymes catalyze two sequential reactions of a metabolic pathway using spatially separated and covalently connected active sites. Combining two enzymes into one protein chain creates efficiency because the product of the first reaction can be shuttled directly to the active site, catalyzing the second reaction in a process called substrate channeling. Here, we use X-ray crystallography to elucidate the three-dimensional structural basis of substrate channeling in the proline catabolic pathway. Structures of the bifunctional enzyme proline utilization A (PutA) reveal an elaborate and dynamic tunnel system featuring a 75-Å-long substrate-channeling path that links the two active sites. Furthermore, we have identified the elusive quinone-binding site of PutA, which provides insight into how PutAs interact with the membrane." @default.
• W2000434472 created "2016-06-24" @default.
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• W2000434472 date "2014-02-18" @default.
• W2000434472 modified "2023-10-18" @default.
• W2000434472 title "Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site" @default.
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• W2000434472 doi "https://doi.org/10.1073/pnas.1321621111" @default.
• W2000434472 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3948300" @default.
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