Sensitivity to pH, product inhibition, and inhibition by NAD+ of 1,3-propanediol dehydrogenase purified from Enterobacter agglomerans CNCM 1210.
Because of its key role in the metabolism of glycerol during fermentation, 1,3-propanediol dehydrogenase (EC 1.1.1.202) of Enterobacter agglomerans CNCM 1210 was purified to homogeneity and studied with respect to its sensitivity to pH and to nucleotide and 1,3-propanediol concentrations. Enzyme activity was optimal at pH 7.8. The enzyme was competitively inhibited by NAD+ (Ki of 0.29 mM), and 1,3-propanediol exerted a strong inhibitory effect according to a mixed-type inhibition with a Ki of 13.7 mM and an a-factor of 9.0. It is proposed that these dehydrogenase properties be extended to the dehydrogenases of Citrobacter freundii and Klebsiella pneumoniae, which exhibited numerous similar physical properties.
Barbirato
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Institut National de la Recherche Agronomique, Laboratoire de Biotechnologie de l'Environnement, Avenue des étangs, F-11100 Narbonne, France.
Larguier
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Conte
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Astruc
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Bories
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D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*; D000447:Aldehydes; D000595:Amino Acid Sequence; D004754:Enterobacter / Q000201:enzymology*; D004791:Enzyme Inhibitors; D005985:Glyceraldehyde / Q000031:analogs & derivatives / Q000378:metabolism; D005990:Glycerol / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D009243:NAD / Q000494:pharmacology; D011407:Propane; D011409:Propylene Glycols / Q000494:pharmacology; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D000447:Aldehydes; D004791:Enzyme Inhibitors; D011409:Propylene Glycols; D009243:NAD; C047158:3-hydroxypropionaldehyde; D005985:Glyceraldehyde; C041787:1,3-propanediol; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; C052370:1,3-propanediol dehydrogenase; D005990:Glycerol; D011407:Propane