Key points are not available for this paper at this time.
Abstract Phosphoserine phosphatase has been partially purified from mouse brain. The preparation catalyzes the phosphohydrolysis of phosphoserine at an optimal pH of about 6.2. This hydrolysis is strongly inhibited by serine. The preparation also catalyzes an exchange reaction whereby the phosphoryl group of phosphoserine is transferred to serine at an optimal pH of about 7.5. Treatment with urea results in inhibition of the hydrolytic activity and enhancement of the transferase activity. Conversely, transferase activity is inhibited by sucrose while the hydrolase activity or its inhibition by serine is unaffected. These iindings are not compatible with a mechanism that equates serine's activity as an inhibitor of hydrolysis with serine's role as a substrate in phosphotransferase. It is suggested that these two activities may be separate phenomena.
William F. Bridgers (1967) studied this question.