2HG2
Structure of Lactaldehyde Dehydrogenase
Summary for 2HG2
Entry DOI | 10.2210/pdb2hg2/pdb |
Descriptor | Aldehyde dehydrogenase A, SULFATE ION (3 entities in total) |
Functional Keywords | dehydrogenase, nad dependent, oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 52516.66 |
Authors | Di Costanzo, L.,Gomez, G.A.,Christianson, D.W. (deposition date: 2006-06-26, release date: 2007-05-08, Last modification date: 2024-02-14) |
Primary citation | Di Costanzo, L.,Gomez, G.A.,Christianson, D.W. Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity J.Mol.Biol., 366:481-493, 2007 Cited by PubMed Abstract: Aldehyde dehydrogenases catalyze the oxidation of aldehyde substrates to the corresponding carboxylic acids. Lactaldehyde dehydrogenase from Escherichia coli (aldA gene product, P25553) is an NAD(+)-dependent enzyme implicated in the metabolism of l-fucose and l-rhamnose. During the heterologous expression and purification of taxadiene synthase from the Pacific yew, lactaldehyde dehydrogenase from E. coli was identified as a minor (PubMed: 17173928 DOI: 10.1016/j.jmb.2006.11.023 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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