Mechanistic insights into allosteric regulation of the reductase component of p-hydroxyphenylacetate 3-hydroxylase by p-hydroxyphenylacetate: a model for effector-controlled activity of redox enzymes.

ABSTRACT: Understanding how an enzyme regulates its function through substrate or allosteric regulation is crucial for controlling metabolic pathways. Some flavin-dependent monooxygenases (FDMOs) have evolved an allosteric mechanism to produce reduced flavin while minimizing the use of NADH and the production of harmful hydrogen peroxide (H₂O₂). In this work, we investigated in-depth mechanisms of how the reductase component (C1) of p-hydroxyphenylacetate (HPA) 3-hydroxylase (HPAH) from Acinetobacter baumanii is allosterically controlled by the binding of HPA, which is a substrate of its monooxygenase counterpart (C2). The C1 structure can be divided into three regions: the N-terminal domain (flavin reductase); a flexible loop; and the C-terminal domain, which is

SUBMITTER: Visitsatthawong S 

PROVIDER: S-EPMC11618861 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature