Characteristics of Fructose-1,6-bisphosphatase from the Methanol-utilizing Yeast Hansenula polymorpha

Department of Microbiology, The University, Sheffield S10 2TN, U.K. Department of Microbiology, The University of Technology, Julianalaan 67A, 2628 BC Delft, The Netherlands ABSTRACT SUMMARY: Fructose-1,6-bisphosphatase (EC 3.1.3.11 ) has been partially purified from methanol- and ethanol-grown Hansenula polymorpha . The enzyme was specific for fructose 1,6-bisphosphate as a substrate and did not react with sedoheptulose 1,7-bisphosphate. The enzyme purified from ethanol-grown cells resembled that from methanol-grown cells in all properties investigated, namely, temperature stability, substrate affinity, pH-dependent inhibition by AMP, and pH-dependent stimulation of activity by EDTA. It is concluded that, although the metabolic role of fructose-1,6-bisphosphatase during growth on methanol and ethanol is completely different, growth on these substrates probably involves the same enzyme.