P21-activated kinase (Pak1), a serine-threonine kinase is found to be upregulated in many solid tumors including Pancreatic ductal adenocarcinoma (PDAC), an highly aggressive cancer. Pak1 promotes tumorigenesis by phosphorylating various substrates involved in cell growth, survival, and apoptosis. PDAC tumors undergo certain metabolic adaptations like increased aerobic glycolysis and reduced mitochondrial oxidative phosphorylation to face the metabolic challenges created by the dense stromal mass surrounding the tumor cells. Though the oncogenic potential of Pak1 is widely studied, very few reports have shown the role of Pak1 in mediating glucose utilization and maintaining energy homeostasis. Silencing Pak1 gene expression using CRISPR-Cas9 KO system in PDAC cells drastically reduced its tumorigenic potential. Also, Pak1 gene deletion altered the metabolism of PDAC cells -reduced basal glycolysis and increased basal respiration in PDAC cells. Western blot analysis revealed that Pak1 influences glycolysis and OXPHOS by altering the expression level of key metabolic enzymes. Global metabolic profiling of PDAC wild-type and Pak1 KO model systems gave insights into the overall metabolic changes adapted in PDAC cells upon Pak1 gene deletion. Pyruvate metabolism is identified as one of the most altered pathways by Pak1. In vitro kinase assay showed that Pak1 phosphorylates Pyruvate dehydrogenase E1α (PDHA1), which catalyses the conversion of Pyruvate to Acetyl Co-A. Further, we demonstrated that Pak1 interacts with PDHA1 by co-immunoprecipitation. The findings from our study highlights the novel function of Pak1 in regulating cancer cell metabolism, providing valuable insights for the development of Pak1-based therapeutic interventions.