The 4-oxalocrotonate tautomerase family of enzymes: how nature makes new enzymes using a β–α–β structural motif
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference32 articles.
1. Physically associated enzymes produce and metabolize 2-hydroxy-2,4-dienoate, a chemically unstable intermediate formed in catechol metabolism via meta cleavage in Pseudomonas putida
2. Chemical and enzymic ketonization of 2-hydroxymuconate, a conjugated enol
3. 4-Oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer.
4. Catalytic Role of the Amino-Terminal Proline in 4-Oxalocrotonate Tautomerase: Affinity Labeling and Heteronuclear NMR Studies
5. 4-Oxalocrotonate tautomerase, a 41-kDa homohexamer: Backbone and side-chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy
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2. The structure of a tautomerase superfamily member linked to the type VI secretion system of Acinetobacter baumannii;Acta Crystallographica Section F Structural Biology Communications;2023-01-01
3. Structural insights into the substrate specificity of 5-chloro-2-hydroxymuconate tautomerase CnbG;Biochemical and Biophysical Research Communications;2022-09
4. Symmetry of 4-Oxalocrotonate Tautomerase Trimers Influences Unfolding and Fragmentation in the Gas Phase;Journal of the American Chemical Society;2022-06-29
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