v5.1.0.3
Cicer data from the Legume Information System
Type | Family |
Description | 4-hydroxybenzoate 3-monooxygenase is a flavoprotein that converts its substrate to 3,4-dihydroxybenzoate, which subsequently enters the beta-ketioadipate pathway of aromatic degradation, using molecular oxygen and NADPH as shown below [ ].4-hydroxybenzoate + NADPH + O(2) = 3,4-dihydroxybenzoate + NADP(+) + H(2)O4-hydroxybenzoate is an intermediate in the degradation of lignin and other aromatic plant compounds, and this enzyme is found extensively in soil bacteria.This enzyme is a homodimer where each subunit is composed of three distinct domains: an N-terminal flavin-binding domain with a beta-α-β fold, a small substrate-binding domain composed of a single alpha helix and β-sheet, and a C-terminal helical domain [ ]. The active site is found at the interface of all three domains. Catalysis occurs by a two-step reaction. In the first step, flavin is reduced by NADPH. Subsequently, the reduced flavin is oxygenated to a hydroperoxide which transfers the hydroxyl group to the substrate, forming 3,4-dihydroxybenzoate. |
Short Name | HB_mOase |