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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.
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