Reduced kynurenine aminotransferase-I activity in SHR rats may be due to lack of KAT-Ib activity.

Kynurenine aminotransferase I (KAT-I), which also shows glutamine transaminase K (GTK) activity, catalyses the conversion of kynurenine to kynurenic acid, an endogenous glutamate antagonist. Both the GTK and KAT enzyme activities were found to be significantly reduced in kidney, brain and medulla oblongata homogenates of spontaneously hypertensive (SHR) compared to Wistar-Kyoto (WKY) rats. Enzyme activity stains on native gel separations of partially purified kidney homogenates was associated with two major bands of GTK (KAT-I)-activity in WKY and Wistar rats, KAT-Ia and KAT-Ib. SHR rats however showed only KAT-Ia activity. These findings suggest that the absence of KAT-Ib activity may result in a reduced ability to synthesise kynurenic acid in SHR rats, this may help to explain the enhanced sensitivity to glutamate seen in this strain.