Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E.coli and some other bacteria, that are bifunctional and possess a CM domain. NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH Is inhibited by NaCl; more than half of the enzyme activity is abolished in the presence of 10 uM of NaCl. kcat is 170.36 sec(-1) toward prephenate, and 356.07 sec(-1) toward NAD(+) (at pH 7.9 and 37 degrees Celsius). Optimum pH is 7.9. Optimum temperature is 37 degrees Celsius. Is not stable even stored at -80 degrees Celsius. About 50% of the activity is lost when stored at 4 degrees Celsius for 24 hours. Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1. Belongs to the prephenate/arogenate dehydrogenase family. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus.