Kynurenine aminotransferase I activity in human placenta

The aim of the study was to detect and characterize placental kynurenine am inotransferase I (KAT I) activity in physiological pregnancy at term. Place ntal KAT I was inhibited by L-glutamine, L-tryptophan, and L-phenylalanine and reached optimum activity at pH 9.8. When pyruvate was used as a co-fact or, the KAT I activity was significantly higher than the activity of this e nzyme in the presence of 2-oxoglutarate. In the light of our findings place ntal KAT I seems to have biochemical characteristics of KAT I detected in h uman brain. (C) 2001 Harcourt Publishers.