2-aminobenzoyl-coa Monooxygenase/reductase, a Novel Type of Flavoprotein Hydroxylase
Year: 1991
Type: book-chapter
Abstract: Recently we reported on the unusual course of areaction catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase from a Pseudomonas sp.(l). This enzyme catalyzes the insertion of one atom of oxygen into the aromatic moiety of the CoA substrate. This enzyme is uncommon in several aspects: a) It is the fIrSt flavin dependent hydroxylase to act' on a CoA thioester as a substrate. b) it inserts a hydroxyl function into the para position of the aromatic amine and c) it catalyzes the reduction of an intermediate to yield a hydrogenated and hydroxylated product. In order to better understand the chemistry of this peculiar reaction course, and possibly to gain information on the general mechanismofflavin-dependent hydroxylation, we have studied some of the basic properties ofthis enzyme in comparison with the properties ofsome typical hydroxylases.
Source: De Gruyter eBooks
Authors: B. Langkau, S. Ghisla, V. Massey, G. Fuchs
Language: English
Subfield: Pharmacology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W807833435