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4.2.1.141
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crystal structures of complexes of the enzyme with magnesium or calcium ions and either a substrate analog 2-oxobutyrate, or the aldehyde enzyme product 2,5-dioxopentanoate reveal the divalent metal ion in the active site is coordinated octahedrally by three conserved carboxylate residues, a water molecule, and both the carboxylate and the oxo groups of the substrate molecule
693645
4.2.1.141
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multiple sequence alignment analysis of the enzyme indicates the presence of a metal binding site consisting of Glu143, Glu145, and Asp164, which may implicate a metal dependent activity
719837
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