4YAR
2-Hydroxyethylphosphonate dioxygenase (HEPD) E176H
Summary for 4YAR
| Entry DOI | 10.2210/pdb4yar/pdb |
| Descriptor | 2-hydroxyethylphosphonate dioxygenase, CADMIUM ION, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | dioxygenase, oxidoreductase |
| Biological source | Streptomyces viridochromogenes |
| Total number of polymer chains | 1 |
| Total formula weight | 49422.56 |
| Authors | Chekan, J.R.,Nair, S.K. (deposition date: 2015-02-17, release date: 2015-03-04, Last modification date: 2023-09-27) |
| Primary citation | Peck, S.C.,Chekan, J.R.,Ulrich, E.C.,Nair, S.K.,van der Donk, W.A. A Common Late-Stage Intermediate in Catalysis by 2-Hydroxyethyl-phosphonate Dioxygenase and Methylphosphonate Synthase. J.Am.Chem.Soc., 137:3217-3220, 2015 Cited by PubMed Abstract: 2-Hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS) are nonheme iron oxygenases that both catalyze the carbon-carbon bond cleavage of 2-hydroxyethylphosphonate but generate different products. Substrate labeling experiments led to a mechanistic hypothesis in which the fate of a common intermediate determined product identity. We report here the generation of a bifunctional mutant of HEPD (E176H) that exhibits the activity of both HEPD and MPnS. The product distribution of the mutant is sensitive to a substrate isotope effect, consistent with an isotope-sensitive branching mechanism involving a common intermediate. The X-ray structure of the mutant was determined and suggested that the introduced histidine does not coordinate the active site metal, unlike the iron-binding glutamate it replaced. PubMed: 25699631DOI: 10.1021/jacs.5b00282 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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