Aminoacyl-tRNA　synthetases　(aaRSs),　a　family　of　ubiquitous　and　essential　enzymes,　can　bind　target　tRNAs　and　catalyze　the　aminoacylation　reaction　in　genetic　code　translation.　In　this　work,　we　explore　the　dynamic　properties　and　allosteric　communication　of　human　mitochondrial　phenylalanyl-tRNA　synthetase　(hmPheRS)　in　free　and　bound　states　to　understand　the　mechanisms　of　its　tRNA(Phe)　recognition　and　allostery　using　molecular　dynamics　simulations　combined　with　the　torsional　mutual　information-based　network　model.　Our　results　reveal　that　hmPheRS＇s　residue　mobility　and　inter-residue　motional　coupling　are　significantly　enhanced　by　tRNA(Phe)　binding,　and　there　occurs　a　strong　allosteric　communication　which　is　critical　for　the　aminoacylation　reaction,　suggesting　the　vital　role　of　tRNA(Phe)　binding　in　the　enzyme＇s　function.　The　identified　signaling　pathways　mainly　make　the　connections　between　the　anticodon　binding　domain　(ABD)　and　catalytic　domain　(CAD),　as　well　as　within　the　CAD　composed　of　many　functional　fragments　and　active　sites,　revealing　the　co-regulation　role　of　them　to　act　coordinately　and　achieve　hmPheRS＇s　aminoacylation　function.　Besides,　several　key　residues　along　the　communication　pathways　are　identified　to　be　involved　in　mediating　the　coordinated　coupling　between　anticodon　recognition　at　the　ABD　and　activation　process　at　the　CAD,　showing　their　pivotal　role　in　the　allosteric　network,　which　are　well　consistent　with　the　experimental　observation.　This　study　sheds　light　on　the　allosteric　communication　mechanism　in　hmPheRS　and　can　provide　important　information　for　the　structure-based　drug　design　targeting　aaRSs.