Structural Insight into the Working Mechanism of the FAD Synthetase from the Human Pathogen Streptococcus pneumoniae: A Molecular Docking Simulation Study.

ABSTRACT: Flavin adenine dinucleotide synthetases (FADSs) catalyze FAD biosynthesis through two consecutive catalytic reactions, riboflavin (RF) phosphorylation and flavin mononucleotide (FMN) adenylylation. Bacterial FADSs have RF kinase (RFK) and FMN adenylyltransferase (FMNAT) domains, whereas the two domains are separated into two independent enzymes in human FADSs. Bacterial FADSs have attracted considerable attention as drug targets due to the fact that they differ from human FADSs in structure and domain combinations. In this study, we analyzed the putative FADS structure from the human pathogen Streptococcus pneumoniae (SpFADS) determined by Kim et al., including conformational changes of key loops in the RFK domain upon substrate binding. Structural analysis and comparisons wi

SUBMITTER: Kwon S 

PROVIDER: S-EPMC9962085 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature