Fructose-2,6-bisphosphatase and 6-phosphofructo-2-kinase are separable in yeast.
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ABSTRACT: Fructose-2,6-bisphosphatase was purified from yeast and separated from 6-phosphofructo-2-kinase and alkaline phosphatase. The enzyme released Pi from the 2-position of fructose 2,6-bisphosphate and formed fructose 6-phosphate in stoichiometric amounts. The enzyme displays hyperbolic kinetics towards fructose 2,6-bisphosphate, with a Km value of 0.3 microM. It is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by L-glycerol 3-phosphate. Phosphorylation of the enzyme by cyclic-AMP-dependent protein kinase causes inactivation, which is reversible by the action of protein phosphatase 2A.
SUBMITTER: Kretschmer M
PROVIDER: S-EPMC1148341 | biostudies-other | 1987 Sep
REPOSITORIES: biostudies-other
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