Protein Kinase D (PKD) is a serine/threonine kinase that is activated by insults experienced in obese and diabetic conditions, namely diacylglycerol and reactive oxygen species. PKD once activated, is involved in numerous fundamental physiological processes however its’ role in energy metabolism has not been elucidated. We generated stable 3T3-L1 fibroblasts expressing either dominant negative (DN) PKD, constitutively activate (CA) PKD or GFP (Control), and found that inactivation of PKD increased cellular glycolytic rate and oxygen consumption, inferring greater energy expenditure. This was associated with enhanced expression of key brown fat genes including UCP-1, Cidea and Cox7a when cells were differentiated. Consistent with increased energy expenditure, basal and insulin stimulated glucose uptake was also increased. In addition, expression of DN PKD increased glucose and palmitate oxidation. Furthermore, expression of CA PKD had reciprocal effects on many of these parameters. The effects also appear dependent on the differentiation process, as pharmacological PKD inhibition in differentiated adipocytes had no effect on cellular bioenergetics, including glycolytic rate and respiration. Data thus far support the notion that white fat tissue can be made more like brown fat cells and provides an exciting opportunity to investigate further the therapeutic utility of PKD inhibition to increase energy expenditure.