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  • Title: Beyond the catalytic core of ALDH: a web of important residues begins to emerge.
    Author: Hempel J, Lindahl R, Perozich J, Wang B, Kuo I, Nicholas H.
    Journal: Chem Biol Interact; 2001 Jan 30; 130-132(1-3):39-46. PubMed ID: 11306029.
    Abstract:
    Site-directed mutagenesis was performed in class 3 aldehyde dehydrogenase (ALDH) on both strictly conserved, non-glycine residues, Glu-333 and Phe-335. Both lie in Motif 8 and are indicated to be of central catalytic importance from their positions in the tertiary structure. In addition, a highly conserved residue at the end of Motif 8, Pro-337, and Asp-247, which interacts with the main chain of Motif 8, were also mutated. All substitutions were conservative. Kinetic values clearly show that Glu-333 and Phe-335 are crucial to efficient catalysis, along with Asp-247. Pro-337 appears to have a different role, most likely relating to folding.
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