4FDX
Kinetic and structural characterization of the 4-oxalocrotonate tautomerase isozymes from Methylibium petroleiphilum
Summary for 4FDX
Entry DOI | 10.2210/pdb4fdx/pdb |
Related | 4FAZ |
Descriptor | 4-oxalocrotonase tautomerase isozyme (2 entities in total) |
Functional Keywords | alpha/beta barrel, 4ot, tautomerase superfamily, isomerase |
Biological source | Methylibium petroleiphilum |
Total number of polymer chains | 2 |
Total formula weight | 15205.46 |
Authors | Terrell, C.R.,Hoffman, D.W.,Whitman, C.P. (deposition date: 2012-05-29, release date: 2013-06-12, Last modification date: 2024-02-28) |
Primary citation | Terrell, C.R.,Burks, E.A.,Whitman, C.P.,Hoffman, D.W. Structural and kinetic characterization of two 4-oxalocrotonate tautomerases in Methylibium petroleiphilum strain PM1. Arch.Biochem.Biophys., 537:113-124, 2013 Cited by PubMed Abstract: Methylibium petroleiphilum strain PM1 uses various petroleum products including the fuel additive methyl tert-butyl ether and straight chain and aromatic hydrocarbons as sole carbon and energy sources. It has two operons, dmpI and dmpII, that code for the enzymes in a pair of parallel meta-fission pathways. In order to understand the roles of the pathways, the 4-oxalocrotonate tautomerase (4-OT) isozyme from each pathway was characterized. Tautomerase I and tautomerase II have the lowest pairwise sequence identity (35%) among the isozyme pairs in the parallel pathways, and could offer insight into substrate preferences and pathway functions. The kinetic parameters of tautomerase I and tautomerase II were determined using 2-hydroxymuconate and 5-(methyl)-2-hydroxymuconate. Both tautomerase I and tautomerase II process the substrates, but with different efficiencies. Crystal structures were determined for both tautomerase I and tautomerase II, at 1.57 and 1.64Å resolution, respectively. The backbones of tautomerase I and tautomerase II are highly similar, but have distinct active site environments. The results, in combination with those for other structurally and kinetically characterized 4-OT isozymes, suggest that tautomerase I catalyzes the tautomerization of both 2-hydroxymuconate and alkyl derivatives, whereas tautomerase II might specialize in other aromatic hydrocarbon metabolites. PubMed: 23831510DOI: 10.1016/j.abb.2013.06.016 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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