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- W2944434518 abstract "In Azospirillum brasilense , a gram‐negative nitrogen‐fixing bacterium, l ‐arabinose is converted to α‐ketoglutarate through a nonphosphorylative metabolic pathway. In the first step in the pathway, l ‐arabinose is oxidized to l ‐arabino‐γ‐lactone by NAD (P)‐dependent l ‐arabinose 1‐dehydrogenase (Ara DH ) belonging to the glucose‐fructose oxidoreductase/inositol dehydrogenase/rhizopine catabolism protein (Gfo/Idh/MocA) family. Here, we determined the crystal structures of apo‐ and NADP ‐bound Ara DH at 1.5 and 2.2 Å resolutions, respectively. A docking model of l ‐arabinose and NADP ‐bound Ara DH and structure‐based mutational analyses suggest that Lys91 or Asp169 serves as a catalytic base and that Glu147, His153, and Asn173 are responsible for substrate recognition. In particular, Asn173 may play a role in the discrimination between l ‐arabinose and d ‐xylose, the C4 epimer of l ‐arabinose." @default.
- W2944434518 created "2019-05-16" @default.
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- W2944434518 date "2019-05-16" @default.
- W2944434518 modified "2023-09-26" @default.
- W2944434518 title "Structural insights into the catalytic and substrate recognition mechanisms of bacterial<scp>l</scp>‐arabinose 1‐dehydrogenase" @default.
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- W2944434518 doi "https://doi.org/10.1002/1873-3468.13424" @default.
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