Generic placeholder image

Current Pharmaceutical Design

Editor-in-Chief

ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

The Prokaryotic FAD Synthetase Family: A Potential Drug Target

Author(s): Ana Serrano, Patricia Ferreira, Marta Martinez-Julvez and Milagros Medina

Volume 19, Issue 14, 2013

Page: [2637 - 2648] Pages: 12

DOI: 10.2174/1381612811319140013

Price: $65

Abstract

Disruption of cellular production of the flavin cofactors, flavin adenine mononucleotide (FMN) and flavin adenine dinucleotide (FAD) will prevent the assembly of a large number of flavoproteins and flavoenzymes involved in key metabolic processes in all types of organisms. The enzymes responsible for FMN and FAD production in prokaryotes and eukaryotes exhibit various structural characteristics to catalyze the same chemistry, a fact that converts the prokaryotic FAD synthetase (FADS) in a potential drug target for the development of inhibitors endowed with anti-pathogenic activity. The first step before searching for selective inhibitors of FADS is to understand the structural and functional mechanisms for the riboflavin kinase and FMN adenylyltransferase activities of the prokaryotic enzyme, and particularly to identify their differential functional characteristics with regard to the enzymes performing similar functions in other organisms, particularly humans. In this paper, an overview of the current knowledge of the structure-function relationships in prokaryotic FADS has been presented, as well as of the state of the art in the use of these enzymes as drug targets.

Keywords: FAD synthetase, riboflavin kinase, FMN adenylyltransferase, FMN biosynthesis, FAD biosynthesis


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy