This review summarizes knowledge on the effects of stress on two catecholamine biosynthetic enzymes, tyrosine hydroxylase (TH) and phenylethanolamine N-methyltransferase (PNMT). Information is presented on differential responses of the enzymes to a variety of stressors as well as differential responses of the enzymes localized to the central nervous system vs. peripheral nervous system and tissues. Changes in mRNA and protein or activity are described, including species- and stressor-specific effects. While temporal changes in these parameters may differ for the particular stressor or enzyme, in general, maximal changes in mRNA and protein content occur at 6-8 and 24 h after stressor exposure, respectively. Elevation of TH and PNMT transcriptional activators prior to mRNA induction and nuclear run-on assays show that stress activates the genes encoding these enzymes. Yet, extents of induction of mRNA, protein and enzyme activity are often discordant depending on the stress, its duration and repetition of exposure. The extremes are concordant changes in mRNA and protein/activity vs. highly elevated mRNA with no change in protein/activity. Post-transcriptional and/or post-translational regulatory influences that may contribute to the complex effects of stress on TH, PNMT and the stress hormone epinephrine are explored.