Kinetic properties of the class II glycerate kinase of T. tenax. The glycerate kinase activity was determined in a discontinuous assay at 70°C by coupling the formation of 2-phosphoglycerate with NADH oxidation via enolase, pyruvate kinase and lactate dehydrogenase. The dependence of the specific enzyme activity on the glycerate concentration is shown. The enzyme is inhibited at higher glycerate concentrations. The insert shows the linear transformation according to Hanes for glycerate concentrations up to 0.3 mM.