EC Number   |
General Information |
Reference  |
|---|
    5.3.2.6 | metabolism |
the enzyme is involved in the degradation of 4-hydroxybenzoate via the protocatechuate 2,3-cleavage pathway, overview |
704310 |
| 5.3.2.6 | malfunction |
modification by 3-bromopyruvate of three active sites per hexamer abolishes essentially all activity of the hexamer, spectrocopic and sequence analysis of labeled peptides, overview |
-, 718826 |
| 5.3.2.6 | metabolism |
the enzyme is part of a degradative pathway that converts various aromatic hydrocarbons to intermediates in the Krebs cycle |
-, 718830 |
| 5.3.2.6 | more |
structure-function relationship, spectroscopic NMR analysis, detailed overview. Three arginine residues, Arg11, Arg39, and Arg61, are localized in the active site of 4-oxalocrotonate tautomerase. Importance of Arg11 in properly orienting the dicarboxylate substrate by interacting with the charged 6-carboxylate group. Arg39 interacts with the 1-carboxylate and the 2-keto group of the substrate to promote carbonyl polarization and catalysis, while Pro-1 transfers protons from C-3 to C-5. Arg61 does not play a significant role in either substrate binding or catalysis |
-, 718830 |
| 5.3.2.6 | more |
structure-function relationship and kinetic analysis, detailed overview |
718840 |
| 5.3.2.6 | malfunction |
introduction of polar residues into the active site produces significant decreases in kcat and Km |
-, 718844 |
| 5.3.2.6 | malfunction |
covalent modification of Pro-1 by 3-bromopropiolate inactivates YwhB, implicating Pro-1 as a critical catalytic residue in the conversion of phenylenolpyruvate to phenylpyruvate |
718847 |
| 5.3.2.6 | evolution |
the enzyme is a member of the tautomerase superfamily |
-, 718874 |
| 5.3.2.6 | more |
the fully functional enzyme requires both subunits, active site structure and function of hh4-OT, overview. Three type II sites are formed at the other end of the heterodimeric unit interface around betaPro-1. As with the type I sites, two of the type II active site sides are composed of loops, but these loops are contributed from different subunits, that is, the alphaA'beta2' loop in the beta-subunit and the beta1alphaA loop in the alpha-subunit. The third side of the type II active site is composed of the intramonomeric alpha-subunit beta2-beta3 loop instead of a 310 helix |
-, 718874 |
| 5.3.2.6 | physiological function |
4-oxalocrotonate tautomerase isozymes play prominent roles in the bacterial utilization of aromatic hydrocarbons as sole carbon sources |
-, 718874 |
