EC Number   |
General Information |
Reference |
|---|
    1.13.11.15 | evolution |
the enzyme PaDHPAO likely belongs to the mononuclear non-heme metal-containing 2-His-1-carboxylate facial triad enzyme superfamily |
-, 743618 |
| 1.13.11.15 | malfunction |
In mutant Y257F, steps of the catalytic cycle are slowed by as much as 100fold by the mutation compared to the wild-type enzyme due to failure of mutant Y257F to facilitate the observed distortion of the bound 3,4-dihydroxyphenylacetate that is proposed to promote transfer of one electron to O2, Steady-state and transient kinetic analyses |
724360 |
| 1.13.11.15 | metabolism |
the catalytic reaction with substrate 4-nitrocatechol is comprised of four steps: (1) A dioxygen attacks the aromatic ring to produce an alkylperoxo species. (2) O-O bond cleavage and the formation of an epoxide species occur. (3) A seven-membered O-heterocyclic compound is generated by the extinction of the epoxy structure. (4) The seven-membered ring undergoes ring opening to form the final product (C2-C3 cleavage product). The effective free energy barrier of the catalytic reaction of the system is 26.2 kcal/mol |
764507 |
| 1.13.11.15 | more |
proposed mechanism for homoprotocatechuate binding to homoprotocatechuate 2,3-dioxygenase, substrate binding structure and thermodynamics, isothermal titration calorimetry analysis, overview |
725555 |
| 1.13.11.15 | more |
reaction mechanism and intermediate formation, Mössbauer spectral analysis of wild-type and Y257F mutant enzymes, detailed overview. Residue His200 is positioned to interact with both the substrate C4-OH substituent and the bound oxygen. It plays many roles including that of an acid-base catalyst to promote the Criegee rearrangement chemistry |
724360 |
| 1.13.11.15 | more |
the enzyme requires Fe2+ for catalysis, but Mn2+ can be substituted (MnHPCD) with essentially no change in the steady-state kinetic parameters, spectral analysis, overview |
725557 |
