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Properties of fructose-1,6-diphosphate phosphatase and fructose-1,6-diphosphate aldolase fromPseudomonas putida

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Abstract

The fructose-1,6-P2 (FDP) phosphatase, (FDPase) and FDP aldolase fromPseudomonas putida were partially purified by a combination of (NH4)2SO4 fractionation and DEAE-Sephadex column chromatography. Michaelis-Menten kinetics were observed with, respect to FDP in both FDPase and FDP aldolase. TheK m for FDP at pH 8.0 was 1.2×10−5M for FDPase and 3.0×10−5M for FDP aldolase. The specific activities of these two enzymes (assayed under optimal conditions in cell-free extracts ofP. putida grown ond-fructose), as well as their kinetic properties, are consistent with the suggestion that during growth ond-fructose most, of the FDP generated is converted to fructose-6-P (F-6-P), which is subsequently utilized via the Entner-Doudoroff pathway (EDP).

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Authors and Affiliations

  1. Department of Bacteriology, University of California, 95616, Davis, California, USA

    Sookie S. Bang & Paul Baumann

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  1. Sookie S. Bang
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  2. Paul Baumann
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Bang, S.S., Baumann, P. Properties of fructose-1,6-diphosphate phosphatase and fructose-1,6-diphosphate aldolase fromPseudomonas putida . Current Microbiology 1, 5–9 (1978). https://doi.org/10.1007/BF02601698

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